The Enzyme Database

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EC 2.4.1.290     
Accepted name: N,N′-diacetylbacillosaminyl-diphospho-undecaprenol α-1,3-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol = UDP + N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here
Glossary: N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose
Other name(s): PglA
Systematic name: UDP-N-acetyl-α-D-galactosamine:N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-α-N-acetyl-D-galactosaminyltransferase
Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480]
[EC 2.4.1.290 created 2012]
 
 
EC 2.4.1.291     
Accepted name: N-acetylgalactosamine-N,N′-diacetylbacillosaminyl-diphospho-undecaprenol 4-α-N-acetylgalactosaminyltransferase
Reaction: UDP-N-acetyl-α-D-galactosamine + N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol = UDP + N-acetyl-D-galactosaminyl-α-(1→4)-N-acetyl-D-galactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol
For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here
Glossary: N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose
Other name(s): PglJ
Systematic name: UDP-N-acetyl-α-D-galactosamine:N-acetylgalactosaminyl-α-(1→3)-N,N′-diacetyl-α-D-bacillosaminyl-diphospho-tritrans,heptacis-undecaprenol 3-α-N-acetyl-D-galactosaminyltransferase
Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480]
2.  Chen, M.M., Weerapana, E., Ciepichal, E., Stupak, J., Reid, C.W., Swiezewska, E. and Imperiali, B. Polyisoprenol specificity in the Campylobacter jejuni N-linked glycosylation pathway. Biochemistry 46 (2007) 14342–14348. [DOI] [PMID: 18034500]
[EC 2.4.1.291 created 2012]
 
 
EC 2.4.1.292     
Accepted name: GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-undecaprenol α-1,4-N-acetyl-D-galactosaminyltransferase
Reaction: 3 UDP-N-acetyl-α-D-galactosamine + GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol = 3 UDP + [GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol
For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here
Glossary: diNAcBac = N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose
Other name(s): PglH
Systematic name: UDP-N-acetyl-α-D-galactosamine:GalNAc-α-(1→4)-GalNAc-α-(1→3)-diNAcBac-PP-tritrans,heptacis-undecaprenol 4-α-N-acetyl-D-galactosaminyltransferase
Comments: Isolated from Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480]
2.  Troutman, J.M. and Imperiali, B. Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions. Biochemistry 48 (2009) 2807–2816. [DOI] [PMID: 19159314]
3.  Borud, B., Viburiene, R., Hartley, M.D., Paulsen, B.S., Egge-Jacobsen, W., Imperiali, B. and Koomey, M. Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system. Proc. Natl. Acad. Sci. USA 108 (2011) 9643–9648. [DOI] [PMID: 21606362]
[EC 2.4.1.292 created 2012]
 
 
EC 2.4.1.293     
Accepted name: GalNAc5-diNAcBac-PP-undecaprenol β-1,3-glucosyltransferase
Reaction: UDP-α-D-glucose + [GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol = UDP + [GalNAc-α-(1→4)]2-[Glc-β-(1→3)]-[GalNAc-α-(1→4)]2-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol
For diagram of undecaprenyldiphosphoheptasaccharide biosynthesis, click here
Glossary: diNAcBac = N,N′-diacetyl-D-bacillosamine = 2,4-diacetamido-2,4,6-trideoxy-D-glucopyranose
Other name(s): PglI
Systematic name: UDP-α-D-glucose:[GalNAc-α-(1→4)]4-GalNAc-α-(1→3)-diNAcBac-diphospho-tritrans,heptacis-undecaprenol 3-β-D-glucosyltransferase
Comments: Isolated from the bacterium Campylobacter jejuni. Part of a bacterial N-linked glycosylation pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Glover, K.J., Weerapana, E. and Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102 (2005) 14255–14259. [DOI] [PMID: 16186480]
2.  Kelly, J., Jarrell, H., Millar, L., Tessier, L., Fiori, L.M., Lau, P.C., Allan, B. and Szymanski, C.M. Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer. J. Bacteriol. 188 (2006) 2427–2434. [DOI] [PMID: 16547029]
[EC 2.4.1.293 created 2012]
 
 
EC 2.4.1.325     
Accepted name: TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase
Reaction: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose + N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = dTDP + 4-acetamido-4,6-dideoxy-α-D-galactosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Glossary: dTDP-4-acetamido-4,6-dideoxy-α-D-galactose = dTDP-N-acetyl-α-D-fucosamine
a lipid II = an undecaprenyldiphospho-N-acetyl-(N-acetylglucosaminyl)muramoyl peptide; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof = an undecaprenyldiphospho-4-O-(N-acetyl-β-D-glucosaminyl)-3-O-peptidyl-α-N-acetylmuramate; the peptide element refers to L-alanyl-D-γ-glutamyl-L-lysyl/meso-2,6-diaminopimelyl-D-alanyl-D-alanine or a modified version thereof
lipid III = N-acetyl-β-D-fucosyl-(1→4)-N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): TDP-Fuc4NAc:lipid II Fuc4NAc-transferase; TDP-Fuc4NAc:lipid II Fuc4NAc transferase; wecF (gene name)
Systematic name: dTDP-N-acetyl-α-D-fucose:N-acetyl-β-D-mannosaminouronyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol N-acetylfucosaminyltransferase
Comments: Involved in the enterobacterial common antigen (ECA) biosynthesis in the bacterium Escherichia coli. The trisaccharide of the product (lipid III) is the repeat unit of ECA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Rahman, A., Barr, K. and Rick, P.D. Identification of the structural gene for the TDP-Fuc4NAc:lipid II Fuc4NAc transferase involved in synthesis of enterobacterial common antigen in Escherichia coli K-12. J. Bacteriol. 183 (2001) 6509–6516. [DOI] [PMID: 11673418]
[EC 2.4.1.325 created 2014]
 
 
EC 2.4.1.385     
Accepted name: sterol 27-β-glucosyltransferase
Reaction: UDP-α-D-glucose + a 27-hydroxysteroid = UDP + a sterol 27-β-D-glucoside
For diagram of all-cis-polyprenyl diphosphate, click here
Systematic name: UDP-α-D-glucose:sterol 27-O-β-D-glucosyltransferase
Comments: The enzyme, isolated from the plant Withania somnifera (ashwagandha), transfers D-glucose to a β-hydroxyl group present at the C-27 position in sterols/withanolides, provided the substrate possesses a 17α-OH group. Natural substrates are 17α-hydroxywithaferin A, 27β-hydroxywithanone, and 5α,6β,17α,27β-tetrahydroxywithanolide. The enzyme's activity with withanolide A and withanolide U, which lack a 17α-hydroxyl group, suggests it may also be able to glucosylate the C-20 β-OH position, although this has not been verified yet. The enzyme does not glucosylate sterols at the C-3 position.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Madina, B.R., Sharma, L.K., Chaturvedi, P., Sangwan, R.S. and Tuli, R. Purification and characterization of a novel glucosyltransferase specific to 27β-hydroxy steroidal lactones from Withania somnifera and its role in stress responses. Biochim. Biophys. Acta 1774 (2007) 1199–1207. [DOI] [PMID: 17704015]
[EC 2.4.1.385 created 2021]
 
 
EC 2.4.2.43     
Accepted name: lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase
Reaction: (1) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = α-Kdo-(2→4)-α-Kdo-(2→6)-[4-P-L-Ara4N]-lipid A + ditrans,octacis-undecaprenyl phosphate
(2) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + lipid IVA = lipid IIA + ditrans,octacis-undecaprenyl phosphate
(3) 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate + α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA + ditrans,octacis-undecaprenyl phosphate
For diagram of lipid IIA biosynthesis, click here
Glossary: lipid IVA = 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
lipid IIA = 4-amino-4-deoxy-β-L-arabinopyranosyl 2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-α-D-glucopyranosyl phosphate
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-hydroxytetradecanoyl]amino}-3-O-[(3R)-3-hydroxytetradecanoyl]-4-O-phosphono-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
4′-α-L-Ara4N-α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA = 4-amino-4-deoxy-α-L-arabinopyranosyl 2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-4-phospho-β-D-glucopyranosy-(1→6)-2-deoxy-2-[(3R)-3-hydroxytetradecanamido]-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucopyranosyl phosphate
lipid A = lipid A of Escherichia coli = 2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
α-Kdo-(2→4)-α-Kdo-(2→6)-[4′-P-α-L-Ara4N]-lipid A = (3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→4)-(3-deoxy-α-D-manno-oct-2-ulopyranosylonate)-(2→6)-2-deoxy-2-{[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino}-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-(4-amino-4-deoxy-α-L-arabinopyranosyl)phospho-β-D-glucopyranosyl-(1→6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-{[(3R)-3-hydroxytetradecanoyl]amino}-1-O-phosphono-α-D-glucopyranose
Other name(s): undecaprenyl phosphate-α-L-Ara4N transferase; 4-amino-4-deoxy-L-arabinose lipid A transferase; polymyxin resistance protein PmrK; arnT (gene name)
Systematic name: 4-amino-4-deoxy-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl-phosphate:lipid IVA 4-amino-4-deoxy-L-arabinopyranosyltransferase
Comments: Integral membrane protein present in the inner membrane of certain Gram negative endobacteria. In strains that do not produce 3-deoxy-D-manno-octulosonic acid (Kdo), the enzyme adds a single arabinose unit to the 1-phosphate moiety of the tetra-acylated lipid A precursor, lipid IVA. In the presence of a Kdo disaccharide, the enzyme primarily adds an arabinose unit to the 4-phosphate of lipid A molecules. The Salmonella typhimurium enzyme can add arabinose units to both positions.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Trent, M.S., Ribeiro, A.A., Lin, S., Cotter, R.J. and Raetz, C.R. An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor. J. Biol. Chem. 276 (2001) 43122–43131. [DOI] [PMID: 11535604]
2.  Trent, M.S., Ribeiro, A.A., Doerrler, W.T., Lin, S., Cotter, R.J. and Raetz, C.R. Accumulation of a polyisoprene-linked amino sugar in polymyxin-resistant Salmonella typhimurium and Escherichia coli: structural characterization and transfer to lipid A in the periplasm. J. Biol. Chem. 276 (2001) 43132–43144. [DOI] [PMID: 11535605]
3.  Zhou, Z., Ribeiro, A.A., Lin, S., Cotter, R.J., Miller, S.I. and Raetz, C.R. Lipid A modifications in polymyxin-resistant Salmonella typhimurium: PMRA-dependent 4-amino-4-deoxy-L-arabinose, and phosphoethanolamine incorporation. J. Biol. Chem. 276 (2001) 43111–43121. [DOI] [PMID: 11535603]
4.  Bretscher, L.E., Morrell, M.T., Funk, A.L. and Klug, C.S. Purification and characterization of the L-Ara4N transferase protein ArnT from Salmonella typhimurium. Protein Expr. Purif. 46 (2006) 33–39. [DOI] [PMID: 16226890]
5.  Impellitteri, N.A., Merten, J.A., Bretscher, L.E. and Klug, C.S. Identification of a functionally important loop in Salmonella typhimurium ArnT. Biochemistry 49 (2010) 29–35. [DOI] [PMID: 19947657]
[EC 2.4.2.43 created 2010, modified 2011]
 
 
EC 2.4.2.45     
Accepted name: decaprenyl-phosphate phosphoribosyltransferase
Reaction: trans,octacis-decaprenyl phosphate + 5-phospho-α-D-ribose 1-diphosphate = trans,octacis-decaprenylphospho-β-D-ribofuranose 5-phosphate + diphosphate
For diagram of decaprenylphosphoarabinofuranose biosynthesis, click here
Other name(s): 5-phospho-α-D-ribose-1-diphosphate:decaprenyl-phosphate 5-phosphoribosyltransferase; 5-phospho-α-D-ribose 1-pyrophosphate:decaprenyl phosphate 5-phosphoribosyltransferase; DPPR synthase; Rv3806
Systematic name: trans,octacis-decaprenylphospho-β-D-ribofuranose 5-phosphate:diphosphate phospho-α-D-ribosyltransferase
Comments: Requires Mg2+. Isolated from Mycobacterium tuberculosis. Has some activity with other polyprenyl phosphates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Huang, H., Scherman, M.S., D'Haeze, W., Vereecke, D., Holsters, M., Crick, D.C. and McNeil, M.R. Identification and active expression of the Mycobacterium tuberculosis gene encoding 5-phospho-α-D-ribose-1-diphosphate: decaprenyl-phosphate 5-phosphoribosyltransferase, the first enzyme committed to decaprenylphosphoryl-D-arabinose synthesis. J. Biol. Chem. 280 (2005) 24539–24543. [DOI] [PMID: 15878857]
[EC 2.4.2.45 created 2012]
 
 
EC 2.4.2.46     
Accepted name: galactan 5-O-arabinofuranosyltransferase
Reaction: Adds an α-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-β-D-arabinofuranose at the 5-O-position of the eighth, tenth and twelfth galactofuranose unit of the galactofuranan chain of [β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→6)]14-β-D-galactofuranosyl-(1→5)-β-D-galactofuranosyl-(1→4)-α-L-rhamnopyranosyl-(1→3)-N-acetyl-α-D-glucosaminyl-diphospho-trans,octacis-decaprenol
For diagram of arabinofuranogalactofuranan biosynthesis, click here
Other name(s): AftA; Rv3792
Systematic name: galactofuranan:trans,octacis-decaprenylphospho-β-D-arabinofuranose 5-O-α-D-arabinofuranosyltransferase
Comments: Isolated from Mycobacterium tuberculosis and Corynebacterium glutamicum. These arabinofuranosyl groups form the start of an arabinofuranan chain as part of the of the cell wall in mycobacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Alderwick, L.J., Seidel, M., Sahm, H., Besra, G.S. and Eggeling, L. Identification of a novel arabinofuranosyltransferase (AftA) involved in cell wall arabinan biosynthesis in Mycobacterium tuberculosis. J. Biol. Chem. 281 (2006) 15653–15661. [DOI] [PMID: 16595677]
[EC 2.4.2.46 created 2012]
 
 
EC 2.4.2.47     
Accepted name: arabinofuranan 3-O-arabinosyltransferase
Reaction: Adds an α-D-arabinofuranosyl group from trans,octacis-decaprenylphospho-β-D-arabinofuranose at the 3-O-position of an α-(1→5)-arabinofuranan chain attached to a β-(1→5)-galactofuranan chain
For diagram of arabinofuranogalactofuranan biosynthesis, click here
Other name(s): AftC
Systematic name: α-(1→5)-arabinofuranan:trans,octacis-decaprenylphospho-β-D-arabinofuranose 3-O-α-D-arabinofuranosyltransferase
Comments: Isolated from Mycobacterium smegmatis. Involved in the formation of the cell wall in mycobacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Birch, H.L., Alderwick, L.J., Bhatt, A., Rittmann, D., Krumbach, K., Singh, A., Bai, Y., Lowary, T.L., Eggeling, L. and Besra, G.S. Biosynthesis of mycobacterial arabinogalactan: identification of a novel α(1-→3) arabinofuranosyltransferase. Mol. Microbiol. 69 (2008) 1191–1206. [DOI] [PMID: 18627460]
2.  Zhang, J., Angala, S.K., Pramanik, P.K., Li, K., Crick, D.C., Liav, A., Jozwiak, A., Swiezewska, E., Jackson, M. and Chatterjee, D. Reconstitution of functional mycobacterial arabinosyltransferase AftC proteoliposome and assessment of decaprenylphosphorylarabinose analogues as arabinofuranosyl donors. ACS Chem. Biol. 6 (2011) 819–828. [DOI] [PMID: 21595486]
[EC 2.4.2.47 created 2012]
 
 
EC 2.4.2.53     
Accepted name: undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
Reaction: UDP-4-deoxy-4-formamido-β-L-arabinopyranose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-α-L-arabinopyranosyl ditrans,octacis-undecaprenyl phosphate
For diagram of UDP-4-amino-4-deoxy-β-L-arabinose biosynthesis, click here
Other name(s): undecaprenyl-phosphate Ara4FN transferase; Ara4FN transferase; polymyxin resistance protein PmrF; UDP-4-amino-4-deoxy-α-L-arabinose:ditrans,polycis-undecaprenyl phosphate 4-amino-4-deoxy-α-L-arabinosyltransferase
Systematic name: UDP-4-amino-4-deoxy-α-L-arabinose:ditrans,octacis-undecaprenyl phosphate 4-amino-4-deoxy-α-L-arabinosyltransferase
Comments: The enzyme shows no activity with UDP-4-amino-4-deoxy-β-L-arabinose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Breazeale, S.D., Ribeiro, A.A. and Raetz, C.R. Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid a species modified with 4-amino-4-deoxy-L-arabinose. J. Biol. Chem. 277 (2002) 2886–2896. [DOI] [PMID: 11706007]
2.  Breazeale, S.D., Ribeiro, A.A., McClerren, A.L. and Raetz, C.R.H. A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose. Identification and function of UDP-4-deoxy-4-formamido-L-arabinose. J. Biol. Chem. 280 (2005) 14154–14167. [DOI] [PMID: 15695810]
[EC 2.4.2.53 created 2010 as EC 2.7.8.30, modified 2011, transferred 2013 to EC 2.4.2.53]
 
 
EC 2.4.99.19     
Accepted name: undecaprenyl-diphosphooligosaccharide—protein glycotransferase
Reaction: tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine = tritrans,heptacis-undecaprenyl diphosphate + a glycoprotein with the oligosaccharide chain attached by N-β-D-glycosyl linkage to protein L-asparagine
Other name(s): PglB
Systematic name: tritrans,heptacis-undecaprenyl-diphosphooligosaccharide:protein-L-asparagine N-β-D-oligosaccharidotransferase
Comments: A bacterial enzyme that has been isolated from Campylobacter jejuni [1] and Campylobacter lari [2]. It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N′-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa’-Ser/Thr- (Xaa and Xaa’ not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Maita, N., Nyirenda, J., Igura, M., Kamishikiryo, J. and Kohda, D. Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases. J. Biol. Chem. 285 (2010) 4941–4950. [DOI] [PMID: 20007322]
2.  Lizak, C., Gerber, S., Numao, S., Aebi, M. and Locher, K.P. X-ray structure of a bacterial oligosaccharyltransferase. Nature 474 (2011) 350–355. [DOI] [PMID: 21677752]
[EC 2.4.99.19 created 2012]
 
 
EC 2.4.99.26     
Accepted name: O-antigen ligase
Reaction: a lipid-linked O antigen + a lipid A-core oligosaccharide = a lipopolysaccharide + a polyisoprenyl diphosphate
Other name(s): waaL (gene name); surface polymer:lipid A-core ligase; rfaL (gene name)
Systematic name: lipid-linked O-antigen:lipid A-core oligosaccharide O-antigen transferase (configuration-inverting)
Comments: This Gram-negative bacterial enzyme attaches the polymerized O antigen molecule to the outer core region of the lipid A-core oligosaccharide, finalizing the biosynthesis of the lipopolysaccharide. Prior to the reaction the two substrates are attached to the periplasmic-facing side of the inner membrane, and the enzyme transfers the O-antigen from its polyprenyl diphosphate membrane anchor (usually ditrans,octacis-undecaprenyl diphosphate) to a terminal sugar of the lipid A-core oligosaccharide. Despite the popular name "ligase", the enzyme is not a real ligase, as the reaction does not involve the hydrolysis of a phosphate bond in a triphosphate. The enzyme is embedded in the inner membrane and often has 12 trans-membrane segments. It is a metal-independent inverting glycosyltransferase, and in some cases it can attach surface polymers other than O-antigens to the lipid A-core oligosaccharide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  MacLachlan, P.R., Kadam, S.K. and Sanderson, K.E. Cloning, characterization, and DNA sequence of the rfaLK region for lipopolysaccharide synthesis in Salmonella typhimurium LT2. J. Bacteriol. 173 (1991) 7151–7163. [DOI] [PMID: 1657881]
2.  Whitfield, C., Amor, P.A. and Koplin, R. Modulation of the surface architecture of gram-negative bacteria by the action of surface polymer:lipid A-core ligase and by determinants of polymer chain length. Mol. Microbiol. 23 (1997) 629–638. [DOI] [PMID: 9157235]
3.  Ruan, X., Loyola, D.E., Marolda, C.L., Perez-Donoso, J.M. and Valvano, M.A. The WaaL O-antigen lipopolysaccharide ligase has features in common with metal ion-independent inverting glycosyltransferases. Glycobiology 22 (2012) 288–299. [DOI] [PMID: 21983211]
4.  Ruan, X., Monjaras Feria, J., Hamad, M. and Valvano, M.A. Escherichia coli and Pseudomonas aeruginosa lipopolysaccharide O-antigen ligases share similar membrane topology and biochemical properties. Mol. Microbiol. 110 (2018) 95–113. [DOI] [PMID: 30047569]
[EC 2.4.99.26 created 2023]
 
 
EC 2.4.99.27     
Accepted name: O-antigen polymerase Wzy
Reaction: n lipid-linked O-antigen repeat units = a lipid-linked O antigen + (n−1) polyisoprenyl diphosphate
Other name(s): wzy (gene name); rfc (gene name); Wzy O-antigen polymerase; Wzy polymerase
Systematic name: lipid-linked O-antigen repeat unit:O-antigen O-antigen repeat-unit transferase
Comments: The Wzy-type polymerase polymerizes O antigen repeat unit oligosaccharides that are anchored to the periplasmic face of the inner membrane, forming an O antigen polysaccharide that is still anchored to the membrane. A Wzz chain length regulator (sometimes referred to as an O-antigen co-polymerase) normally interacts with Wzy to confer a distinctive modal chain length distribution. The resultant polysaccharide is transferred from the membrane anchor to the lipid A-core oligosaccharide by EC 2.4.99.26, O-antigen ligase, forming a complete lipopolysaccharide structure. There is an enormous diversity of O antigen polymerases with different specificities, reflecting the variability in the structure and composition of O-antigens.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Collins, L.V. and Hackett, J. Molecular cloning, characterization, and nucleotide sequence of the rfc gene, which encodes an O-antigen polymerase of Salmonella typhimurium. J. Bacteriol. 173 (1991) 2521–2529. [DOI] [PMID: 1707412]
2.  Woodward, R., Yi, W., Li, L., Zhao, G., Eguchi, H., Sridhar, P.R., Guo, H., Song, J.K., Motari, E., Cai, L., Kelleher, P., Liu, X., Han, W., Zhang, W., Ding, Y., Li, M. and Wang, P.G. In vitro bacterial polysaccharide biosynthesis: defining the functions of Wzy and Wzz. Nat. Chem. Biol. 6 (2010) 418–423. [DOI] [PMID: 20418877]
3.  Kenyon, J.J. and Reeves, P.R. The Wzy O-antigen polymerase of Yersinia pseudotuberculosis O:2a has a dependence on the Wzz chain-length determinant for efficient polymerization. FEMS Microbiol. Lett. 349 (2013) 163–170. [DOI] [PMID: 24164168]
4.  Islam, S.T., Huszczynski, S.M., Nugent, T., Gold, A.C. and Lam, J.S. Conserved-residue mutations in Wzy affect O-antigen polymerization and Wzz-mediated chain-length regulation in Pseudomonas aeruginosa PAO1. Sci. Rep. 3:3441 (2013). [DOI] [PMID: 24309320]
5.  Islam, S.T. and Lam, J.S. Synthesis of bacterial polysaccharides via the Wzx/Wzy-dependent pathway. Can. J. Microbiol. 60 (2014) 697–716. [DOI] [PMID: 25358682]
6.  Nath, P. and Morona, R. Mutational analysis of the major periplasmic loops of Shigella flexneri Wzy: identification of the residues affecting O antigen modal chain length control, and Wzz-dependent polymerization activity. Microbiology (Reading) 161 (2015) 774–785. [DOI] [PMID: 25627441]
7.  Merino, S., Gonzalez, V. and Tomas, J.M. The first sugar of the repeat units is essential for the Wzy polymerase activity and elongation of the O-antigen lipopolysaccharide. Future Microbiol 11 (2016) 903–918. [DOI] [PMID: 27357519]
[EC 2.4.99.27 created 2023]
 
 
EC 2.4.99.28     
Accepted name: peptidoglycan glycosyltransferase
Reaction: [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
Glossary: Mur2Ac = N-acetylmuramic acid
Other name(s): PG-II; bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase; penicillin binding protein (3 or 1B); peptidoglycan transglycosylase; undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide):undecaprenyldiphospho-(N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide) disaccharidetransferase
Systematic name: [poly-N-acetyl-D-glucosaminyl-(1→4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1→4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase
Comments: The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here). Involved in the synthesis of cell-wall peptidoglycan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 79079-04-2
References:
1.  Taku, A., Stuckey, M. and Fan, D.P. Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257 (1982) 5018–5022. [DOI] [PMID: 6802846]
2.  Goffin, C. and Ghuysen, J.-M. Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs. Microbiol. Mol. Biol. Rev. 62 (1998) 1079–1093. [DOI] [PMID: 9841666]
3.  van Heijenoort, J. Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11 (2001) 25. [DOI] [PMID: 11320055]
[EC 2.4.99.28 created 1984 as EC 2.4.1.129, modified 2002, transferred 2023 to EC 2.4.99.28]
 
 
EC 2.5.1.1     
Accepted name: dimethylallyltranstransferase
Reaction: prenyl diphosphate + 3-methylbut-3-en-1-yl diphosphate = diphosphate + geranyl diphosphate
For diagram of terpenoid biosynthesis, click here
Glossary: 3-methylbut-3-en-1-yl = isopentenyl (ambiguous)
prenyl = 3-methylbut-2-en-1-yl = dimethylallyl (ambiguous)
Other name(s): geranyl-diphosphate synthase; prenyltransferase; dimethylallyltransferase; DMAPP:IPP-dimethylallyltransferase; (2E,6E)-farnesyl diphosphate synthetase; diprenyltransferase; geranyl pyrophosphate synthase; geranyl pyrophosphate synthetase; trans-farnesyl pyrophosphate synthetase; dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallyltranstransferase
Systematic name: prenyl-diphosphate:3-methylbut-3-en-1-yl-diphosphate prenyltranstransferase
Comments: This enzyme will not accept larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-79-5
References:
1.  Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan, M.G. Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochemistry 15 (1976) 91–100.
2.  Sagami, H., Ogura, K., Seto, S. and Kurokawa, T. A new prenyltransferase from Micrococcus lysodeikticus. Biochem. Biophys. Res. Commun. 85 (1978) 572–578. [DOI] [PMID: 736921]
[EC 2.5.1.1 created 1961]
 
 
EC 2.5.1.10     
Accepted name: (2E,6E)-farnesyl diphosphate synthase
Reaction: geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2E,6E)-farnesyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): farnesyl-diphosphate synthase; geranyl transferase I; prenyltransferase; farnesyl pyrophosphate synthetase; farnesylpyrophosphate synthetase; geranyltranstransferase
Systematic name: geranyl-diphosphate:isopentenyl-diphosphate geranyltranstransferase
Comments: Some forms of this enzyme will also use dimethylallyl diphosphate as a substrate. The enzyme will not accept larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37277-79-5
References:
1.  Lynen, F., Agranoff, B.W., Eggerer, H., Henning, V. and Möslein, E.M. Zur Biosynthese der Terpene. VI. γ,γ-Dimethyl-allyl-pyrophosphat und Geranyl-pyrophosphat, biologische Vorstufen des Squalens. Angew. Chem. 71 (1959) 657–663.
2.  Ogura, K., Nishino, T. and Seto, S. The purification of prenyltransferase and isopentenyl pyrophosphate isomerase of pumpkin fruit and their some properties. J. Biochem. (Tokyo) 64 (1968) 197–203. [PMID: 4303505]
3.  Reed, B.C. and Rilling, H. Crystallization and partial characterization of prenyltransferase from avian liver. Biochemistry 14 (1975) 50–54. [PMID: 1109590]
4.  Takahashi, I. and Ogura, K. Farnesyl pyrophosphate synthetase from Bacillus subtilis. J. Biochem. (Tokyo) 89 (1981) 1581–1587. [PMID: 6792191]
5.  Takahashi, I. and Ogura, K. Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase. J. Biochem. (Tokyo) 92 (1982) 1527–1537. [PMID: 6818223]
[EC 2.5.1.10 created 1972, modified 2010]
 
 
EC 2.5.1.11      
Transferred entry: trans-octaprenyltranstransferase. Now covered by EC 2.5.1.84 (all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific]) and EC 2.5.1.85 (all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific])
[EC 2.5.1.11 created 1972, deleted 2010]
 
 
EC 2.5.1.20     
Accepted name: rubber cis-polyprenylcistransferase
Reaction: polycis-polyprenyl diphosphate + isopentenyl diphosphate = diphosphate + a polycis-polyprenyl diphosphate longer by one C5 unit
For diagram of all-cis-polyprenyl diphosphate, click here
Other name(s): rubber allyltransferase; rubber transferase; isopentenyl pyrophosphate cis-1,4-polyisoprenyl transferase; cis-prenyl transferase; rubber polymerase; rubber prenyltransferase
Systematic name: polycis-polyprenyl-diphosphate:isopentenyl-diphosphate polyprenylcistransferase
Comments: Rubber particles act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-41-6
References:
1.  Archer, B.L. and Cockbain, E.G. Rubber transferase from Hevea brasiliensis latex. Methods Enzymol. 15 (1969) 476–480.
2.  McMullen, A.I. and McSweeney, G.P. The biosynthesis of rubber. Incorporation of isopentenyl pyrophosphate into purified rubber particles by a soluble latex-serum enzyme. Biochem. J. 101 (1966) 42–47. [PMID: 16742418]
[EC 2.5.1.20 created 1976]
 
 
EC 2.5.1.21     
Accepted name: squalene synthase
Reaction: 2 (2E,6E)-farnesyl diphosphate + NAD(P)H + H+ = squalene + 2 diphosphate + NAD(P)+ (overall reaction)
(1a) 2 (2E,6E)-farnesyl diphosphate = diphosphate + presqualene diphosphate
(1b) presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate + NAD(P)+
For diagram of squalene, phytoene and 4,4′-diapophytoene biosynthesis, click here
Other name(s): farnesyltransferase; presqualene-diphosphate synthase; presqualene synthase; squalene synthetase; farnesyl-diphosphate farnesyltransferase; SQS
Systematic name: (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase
Comments: This microsomal enzyme catalyses the first committed step in the biosynthesis of sterols. The enzyme from yeast requires either Mg2+ or Mn2+ for activity. In the absence of NAD(P)H, presqualene diphosphate (PSPP) is accumulated. When NAD(P)H is present, presqualene diphosphate does not dissociate from the enzyme during the synthesis of squalene from farnesyl diphosphate (FPP) [8]. High concentrations of FPP inhibit the production of squalene but not of PSPP [8].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9077-14-9
References:
1.  Kuswick-Rabiega, G. and Rilling, H.C. Squalene synthetase. Solubilization and partial purification of squalene synthetase, copurification of presqualene pyrophosphate and squalene synthetase activities. J. Biol. Chem. 262 (1987) 1505–1509. [PMID: 3805037]
2.  Ericsson, J., Appelkvist, E.L., Thelin, A., Chojnacki, T. and Dallner, G. Isoprenoid biosynthesis in rat liver peroxisomes. Characterization of cis-prenyltransferase and squalene synthetase. J. Biol. Chem. 267 (1992) 18708–18714. [PMID: 1527001]
3.  Tansey, T.R. and Shechter, I. Structure and regulation of mammalian squalene synthase. Biochim. Biophys. Acta 1529 (2000) 49–62. [DOI] [PMID: 11111077]
4.  LoGrasso, P.V., Soltis, D.A. and Boettcher, B.R. Overexpression, purification, and kinetic characterization of a carboxyl-terminal-truncated yeast squalene synthetase. Arch. Biochem. Biophys. 307 (1993) 193–199. [DOI] [PMID: 8239656]
5.  Shechter, I., Klinger, E., Rucker, M.L., Engstrom, R.G., Spirito, J.A., Islam, M.A., Boettcher, B.R. and Weinstein, D.B. Solubilization, purification, and characterization of a truncated form of rat hepatic squalene synthetase. J. Biol. Chem. 267 (1992) 8628–8635. [PMID: 1569107]
6.  Agnew, W.S. and Popják, G. Squalene synthetase. Stoichiometry and kinetics of presqualene pyrophosphate and squalene synthesis by yeast microsomes. J. Biol. Chem. 253 (1978) 4566–4573. [PMID: 26684]
7.  Pandit, J., Danley, D.E., Schulte, G.K., Mazzalupo, S., Pauly, T.A., Hayward, C.M., Hamanaka, E.S., Thompson, J.F. and Harwood, H.J., Jr. Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. J. Biol. Chem. 275 (2000) 30610–30617. [DOI] [PMID: 10896663]
8.  Radisky, E.S. and Poulter, C.D. Squalene synthase: steady-state, pre-steady-state, and isotope-trapping studies. Biochemistry 39 (2000) 1748–1760. [DOI] [PMID: 10677224]
[EC 2.5.1.21 created 1976, modified 2005, modified 2012]
 
 
EC 2.5.1.27     
Accepted name: adenylate dimethylallyltransferase (AMP-dependent)
Reaction: prenyl diphosphate + AMP = diphosphate + N6-prenyladenosine 5′-phosphate
For diagram of N6-(Dimethylallyl)adenosine phosphates biosynthesis, click here
Glossary: prenyl = 3-methylbut-2-en-1-yl = dimethylallyl (ambiguous)
Other name(s): cytokinin synthase (ambiguous); isopentenyltransferase (ambiguous); 2-isopentenyl-diphosphate:AMP Δ2-isopentenyltransferase; adenylate isopentenyltransferase (ambiguous); IPT; adenylate dimethylallyltransferase; dimethylallyl-diphosphate:AMP dimethylallyltransferase
Systematic name: prenyl-diphosphate:AMP prenyltransferase
Comments: Involved in the biosynthesis of cytokinins in plants. Some isoforms from the plant Arabidopsis thaliana are specific for AMP while others also have the activity of EC 2.5.1.112, adenylate dimethylallyltransferase (ADP/ATP-dependent).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 72840-95-0
References:
1.  Chen, C.-M. and Melitz, D.K. Cytokinin biosynthesis in a cell-free system from cytokinin-autotrophic tobacco tissue cultures. FEBS Lett. 107 (1979) 15–20. [DOI] [PMID: 499537]
2.  Takei, K., Sakakibara, H. and Sugiyama, T. Identification of genes encoding adenylate isopentenyltransferase, a cytokinin biosynthesis enzyme, in Arabidopsis thaliana. J. Biol. Chem. 276 (2001) 26405–26410. [DOI] [PMID: 11313355]
3.  Sakano, Y., Okada, Y., Matsunaga, A., Suwama, T., Kaneko, T., Ito, K., Noguchi, H. and Abe, I. Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.). Phytochemistry 65 (2004) 2439–2446. [DOI] [PMID: 15381407]
[EC 2.5.1.27 created 1984, modified 2002, modified 2013]
 
 
EC 2.5.1.28     
Accepted name: dimethylallylcistransferase
Reaction: prenyl diphosphate + 3-methyl-but-3-en-1-yl diphosphate = diphosphate + neryl diphosphate
For diagram of all-cis-polyprenyl diphosphate, click here
Glossary: neryl = (2Z)-3,7-dimethylocta-2,6-dien-1-yl
Other name(s): neryl-diphosphate synthase; dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallylcistransferase
Systematic name: prenyl-diphosphate:3-methyl-but-3-en-1-yl-diphosphate prenylcistransferase
Comments: This enzyme will not use larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-79-5
References:
1.  Banthorpe, D.V., Bucknall, G.A., Doonan, H.J., Doonan, S. and Rowan, M.G. Biosynthesis of geraniol and nerol in cell-free extracts of Tanacetum vulgare. Phytochemistry 15 (1976) 91–100.
2.  Beytía, E., Valenzuela, P. and Cori, O. Terpene biosynthesis: formation of nerol, geraniol, and other prenols by an enzyme system from Pinus radiata seedlings. Arch. Biochem. Biophys. 129 (1969) 346–356. [DOI] [PMID: 4303098]
[EC 2.5.1.28 created 1984]
 
 
EC 2.5.1.29     
Accepted name: geranylgeranyl diphosphate synthase
Reaction: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): geranylgeranyl-diphosphate synthase; geranylgeranyl pyrophosphate synthetase; geranylgeranyl-PP synthetase; farnesyltransferase; geranylgeranyl pyrophosphate synthase; farnesyltranstransferase (obsolete)
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase
Comments: Some forms of this enzyme will also use geranyl diphosphate and dimethylallyl diphosphate as donors; it will not use larger prenyl diphosphates as efficient donors.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-58-0
References:
1.  Sagami, H., Ishi, K. and Ogura, K. Occurrence and unusual properties of geranylgeranyl pyrophosphate synthetase of pig liver. Biochem. Int. 3 (1981) 669–675.
[EC 2.5.1.29 created 1984, modified 2011]
 
 
EC 2.5.1.30     
Accepted name: heptaprenyl diphosphate synthase
Reaction: (2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate = 4 diphosphate + all-trans-heptaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): all-trans-heptaprenyl-diphosphate synthase; heptaprenyl pyrophosphate synthase; heptaprenyl pyrophosphate synthetase; HepPP synthase; HepPS; heptaprenylpyrophosphate synthetase
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 4 isopentenyl units)
Comments: This enzyme catalyses the condensation reactions resulting in the formation of all-trans-heptaprenyl diphosphate, the isoprenoid side chain of ubiquinone-7 and menaquinone-7. The enzyme adds four isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 74506-59-5
References:
1.  Takahashi, I., Ogura, K. and Seto, S. Heptaprenyl pyrophosphate synthetase from Bacillus subtilis. J. Biol. Chem. 255 (1980) 4539–4543. [PMID: 6768722]
2.  Zhang, Y.W., Koyama, T., Marecak, D.M., Prestwich, G.D., Maki, Y. and Ogura, K. Two subunits of heptaprenyl diphosphate synthase of Bacillus subtilis form a catalytically active complex. Biochemistry 37 (1998) 13411–13420. [DOI] [PMID: 9748348]
3.  Zhang, Y.W., Li, X.Y., Sugawara, H. and Koyama, T. Site-directed mutagenesis of the conserved residues in component I of Bacillus subtilis heptaprenyl diphosphate synthase. Biochemistry 38 (1999) 14638–14643. [DOI] [PMID: 10545188]
4.  Suzuki, T., Zhang, Y.W., Koyama, T., Sasaki, D.Y. and Kurihara, K. Direct observation of substrate-enzyme complexation by surface forces measurement. J. Am. Chem. Soc. 128 (2006) 15209–15214. [DOI] [PMID: 17117872]
[EC 2.5.1.30 created 1984, modified 2010]
 
 
EC 2.5.1.31     
Accepted name: ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
Reaction: (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = 8 diphosphate + ditrans,octacis-undecaprenyl diphosphate
For diagram of di- and tritrans,polycis-polyprenol biosynthesis, click here
Other name(s): di-trans,poly-cis-undecaprenyl-diphosphate synthase; undecaprenyl-diphosphate synthase; bactoprenyl-diphosphate synthase; UPP synthetase; undecaprenyl diphosphate synthetase; undecaprenyl pyrophosphate synthetase; di-trans,poly-cis-decaprenylcistransferase
Systematic name: (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 8 isopentenyl units)
Comments: Undecaprenyl pyrophosphate synthase catalyses the consecutive condensation reactions of a farnesyl diphosphate with eight isopentenyl diphosphates, in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52350-87-5
References:
1.  Muth, J.D. and Allen, C.M. Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: a dimeric protein. Arch. Biochem. Biophys. 230 (1984) 49–60. [DOI] [PMID: 6712246]
2.  Takahashi, I. and Ogura, K. Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase. J. Biochem. (Tokyo) 92 (1982) 1527–1537. [PMID: 6818223]
3.  Guo, R.T., Ko, T.P., Chen, A.P., Kuo, C.J., Wang, A.H. and Liang, P.H. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J. Biol. Chem. 280 (2005) 20762–20774. [DOI] [PMID: 15788389]
4.  Ko, T.P., Chen, Y.K., Robinson, H., Tsai, P.C., Gao, Y.G., Chen, A.P., Wang, A.H. and Liang, P.H. Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. J. Biol. Chem. 276 (2001) 47474–47482. [DOI] [PMID: 11581264]
5.  Fujikura, K., Zhang, Y.W., Fujihashi, M., Miki, K. and Koyama, T. Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. Biochemistry 42 (2003) 4035–4041. [DOI] [PMID: 12680756]
6.  Fujihashi, M., Zhang, Y.W., Higuchi, Y., Li, X.Y., Koyama, T. and Miki, K. Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl. Acad. Sci. USA 98 (2001) 4337–4342. [DOI] [PMID: 11287651]
7.  Pan, J.J., Chiou, S.T. and Liang, P.H. Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction. Biochemistry 39 (2000) 10936–10942. [DOI] [PMID: 10978182]
8.  Kharel, Y., Zhang, Y.W., Fujihashi, M., Miki, K. and Koyama, T. Significance of highly conserved aromatic residues in Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. J. Biochem. 134 (2003) 819–826. [PMID: 14769870]
[EC 2.5.1.31 created 1984, modified 2011]
 
 
EC 2.5.1.33      
Transferred entry: trans-pentaprenyltranstransferase. Now covered by EC 2.5.1.82 (hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]) and EC 2.5.1.83 (hexaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific])
[EC 2.5.1.33 created 1984, deleted 2010]
 
 
EC 2.5.1.34     
Accepted name: 4-dimethylallyltryptophan synthase
Reaction: prenyl diphosphate + L-tryptophan = diphosphate + 4-(3-methylbut-2-en-1-yl)-L-tryptophan
For diagram of ergot alkaloid biosynthesis, click here
Glossary: prenyl diphosphate = dimethylallyl diphosphate
Other name(s): dimethylallylpyrophosphate:L-tryptophan dimethylallyltransferase; dimethylallyltryptophan synthetase; dimethylallylpyrophosphate:tryptophan dimethylallyl transferase; DMAT synthetase; 4-(γ,gamma-dimethylallyl)tryptophan synthase; tryptophan dimethylallyltransferase; dimethylallyl-diphosphate:L-tryptophan 4-dimethylallyltransferase
Systematic name: prenyl-diphosphate:L-tryptophan 4-prenyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 55127-01-0
References:
1.  Lee, S.L., Floss, H.G. and Heinstein, P. Purification and properties of dimethylallylpyrophosphate:tryptophan dimethylallyl transferase, the first enzyme of ergot alkaloid biosynthesis in Claviceps sp. SD 58. Arch. Biochem. Biophys. 177 (1976) 84–94. [DOI] [PMID: 999297]
[EC 2.5.1.34 created 1984, modified 2010]
 
 
EC 2.5.1.35     
Accepted name: aspulvinone dimethylallyltransferase
Reaction: 2 prenyl diphosphate + aspulvinone E = 2 diphosphate + aspulvinone H
Other name(s): dimethylallyl pyrophosphate:aspulvinone dimethylallyltransferase; dimethylallyl-diphosphate:aspulvinone-E dimethylallyltransferase
Systematic name: prenyl-diphosphate:aspulvinone-E prenyltransferase
Comments: This enzyme will also use as acceptor aspulvinone G, a hydroxylated derivative of the complex phenolic pigment aspulvinone E.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 67584-68-3
References:
1.  Takahashi, I., Ojima, N., Ogura, K. and Seto, S. Purification and characterization of dimethylallyl pyrophosphate: aspulvinone dimethylallyltransferase from Aspergillus terreus. Biochemistry 17 (1978) 2696–2702. [PMID: 678538]
[EC 2.5.1.35 created 1984]
 
 
EC 2.5.1.36     
Accepted name: trihydroxypterocarpan dimethylallyltransferase
Reaction: (1) prenyl diphosphate + (6aS,11aS)-3,6a,9-trihydroxypterocarpan = diphosphate + (6aS,11aS)-3,6a,9-trihydroxy-2-prenylpterocarpan
(2) prenyl diphosphate + (6aS,11aS)-3,6a,9-trihydroxypterocarpan = diphosphate + (6aS,11aS)-3,6a,9-trihydroxy-4-prenylpterocarpan
For diagram of glyceollin biosynthesis (part 2), click here
Other name(s): glyceollin synthase; dimethylallylpyrophosphate:3,6a,9-trihydroxypterocarpan dimethylallyltransferase; dimethylallylpyrophosphate:trihydroxypterocarpan dimethylallyl transferase; dimethylallyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan dimethyltransferase; dimethylallyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan dimethylallyltransferase
Systematic name: prenyl-diphosphate:(6aS,11aS)-3,6a,9-trihydroxypterocarpan prenyltransferase
Comments: Part of the glyceollin biosynthesis system in soy bean.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 70851-94-4
References:
1.  Leube, J. and Grisebach, H. Further studies on induction of enzymes of phytoalexin synthesis in soybean and cultured soybean cells. Z. Naturforsch. C: Biosci. 38 (1983) 730–735.
2.  Zähringer, U., Schaller, E. and Grisebach, H. Induction of phytoalexin synthesis in soybean. Structure and reactions of naturally occurring and enzymatically prepared prenylated pterocarpans from elicitor-treated cotyledons and cell cultures of soybean. Z. Natursforsch. C: Biosci. 36 (1981) 234–241.
[EC 2.5.1.36 created 1989]
 
 
EC 2.5.1.39     
Accepted name: 4-hydroxybenzoate polyprenyltransferase
Reaction: a polyprenyl diphosphate + 4-hydroxybenzoate = diphosphate + a 4-hydroxy-3-polyprenylbenzoate
For diagram of ubiquinol biosynthesis, click here
Other name(s): nonaprenyl-4-hydroxybenzoate transferase; 4-hydroxybenzoate transferase; p-hydroxybenzoate dimethylallyltransferase; p-hydroxybenzoate polyprenyltransferase; p-hydroxybenzoic acid-polyprenyl transferase; p-hydroxybenzoic-polyprenyl transferase; 4-hydroxybenzoate nonaprenyltransferase
Systematic name: polyprenyl-diphosphate:4-hydroxybenzoate polyprenyltransferase
Comments: This enzyme, involved in the biosynthesis of ubiquinone, attaches a polyprenyl side chain to a 4-hydroxybenzoate ring, producing the first ubiquinone intermediate that is membrane bound. The number of isoprenoid subunits in the side chain varies in different species. The enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency [2,4,5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-77-7
References:
1.  Kalén, A., Appelkvist, E.-L., Chojnacki, T. and Dallner, G. Nonaprenyl-4-hydroxybenzoate transferase, an enzyme involved in ubiquinone biosynthesis, in the endoplasmic reticulum-Golgi system of rat liver. J. Biol. Chem. 265 (1990) 1158–1164. [PMID: 2295606]
2.  Melzer, M. and Heide, L. Characterization of polyprenyldiphosphate: 4-hydroxybenzoate polyprenyltransferase from Escherichia coli. Biochim. Biophys. Acta 1212 (1994) 93–102. [DOI] [PMID: 8155731]
3.  Okada, K., Ohara, K., Yazaki, K., Nozaki, K., Uchida, N., Kawamukai, M., Nojiri, H. and Yamane, H. The AtPPT1 gene encoding 4-hydroxybenzoate polyprenyl diphosphate transferase in ubiquinone biosynthesis is required for embryo development in Arabidopsis thaliana. Plant Mol. Biol. 55 (2004) 567–577. [DOI] [PMID: 15604701]
4.  Forsgren, M., Attersand, A., Lake, S., Grunler, J., Swiezewska, E., Dallner, G. and Climent, I. Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ. Biochem. J. 382 (2004) 519–526. [DOI] [PMID: 15153069]
5.  Tran, U.C. and Clarke, C.F. Endogenous synthesis of coenzyme Q in eukaryotes. Mitochondrion 7 Suppl (2007) S62–S71. [DOI] [PMID: 17482885]
[EC 2.5.1.39 created 1992, modified 2010]
 
 
EC 2.5.1.41     
Accepted name: phosphoglycerol geranylgeranyltransferase
Reaction: geranylgeranyl diphosphate + sn-glycerol 1-phosphate = diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate
For diagram of archaetidylserine biosynthesis, click here
Glossary: sn-glycerol 1-phosphate = sn-glyceryl phosphate = (S)-2,3-dihydroxypropyl dihydrogen phosphate
Other name(s): glycerol phosphate geranylgeranyltransferase; geranylgeranyl-transferase (ambiguous); prenyltransferase (ambiguous); (S)-3-O-geranylgeranylglyceryl phosphate synthase; (S)-geranylgeranylglyceryl phosphate synthase; GGGP synthase; (S)-GGGP synthase; GGGPS; geranylgeranyl diphosphate:sn-glyceryl phosphate geranylgeranyltransferase; geranylgeranyl diphosphate:sn-glycerol-1-phosphate geranylgeranyltransferase
Systematic name: geranylgeranyl-diphosphate:sn-glycerol-1-phosphate geranylgeranyltransferase
Comments: This cytosolic enzyme catalyses the first pathway-specific step in the biosynthesis of the core membrane diether lipids in archaebacteria [2]. Requires Mg2+ for maximal activity [2]. It catalyses the alkylation of the primary hydroxy group in sn-glycerol 1-phosphate by geranylgeranyl diphosphate (GGPP) in a prenyltransfer reaction where a hydroxy group is the nucleophile in the acceptor substrate [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase) and EC 2.7.7.67 (CDP-archaeol synthase), which lead to the formation of CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 124650-69-7
References:
1.  Zhang, D.-L., Daniels, L. and Poulter, C.D. Biosynthesis of archaebacterial membranes. Formation of isoprene ethers by a prenyl transfer reaction. J. Am. Chem. Soc. 112 (1990) 1264–1265.
2.  Chen, A., Zhang, D. and Poulter, C.D. (S)-Geranylgeranylglyceryl phosphate synthase. Purification and characterization of the first pathway-specific enzyme in archaebacterial membrane lipid biosynthesis. J. Biol. Chem. 268 (1993) 21701–21705. [PMID: 8408023]
3.  Nemoto, N., Oshima, T. and Yamagishi, A. Purification and characterization of geranylgeranylglyceryl phosphate synthase from a thermoacidophilic archaeon, Thermoplasma acidophilum. J. Biochem. 133 (2003) 651–657. [PMID: 12801917]
4.  Payandeh, J., Fujihashi, M., Gillon, W. and Pai, E.F. The crystal structure of (S)-3-O-geranylgeranylglyceryl phosphate synthase reveals an ancient fold for an ancient enzyme. J. Biol. Chem. 281 (2006) 6070–6078. [DOI] [PMID: 16377641]
5.  Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568–36574. [DOI] [PMID: 10960477]
[EC 2.5.1.41 created 1992, modified 2009]
 
 
EC 2.5.1.42     
Accepted name: geranylgeranylglycerol-phosphate geranylgeranyltransferase
Reaction: geranylgeranyl diphosphate + 3-(O-geranylgeranyl)-sn-glycerol 1-phosphate = diphosphate + 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate
For diagram of archaetidylserine biosynthesis, click here
Other name(s): geranylgeranyloxyglycerol phosphate geranylgeranyltransferase; geranylgeranyltransferase II; (S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase; DGGGP synthase; DGGGPS; geranylgeranyl diphosphate:sn-3-O-(geranylgeranyl)glycerol 1-phosphate geranylgeranyltransferase
Systematic name: geranylgeranyl-diphosphate:3-(O-geranylgeranyl)-sn-glycerol 1-phosphate geranylgeranyltransferase
Comments: This enzyme is an integral-membrane protein that carries out the second prenyltransfer reaction involved in the formation of polar membrane lipids in Archaea. Requires a divalent metal cation, such as Mg2+ or Mn2+, for activity [2]. 4-Hydroxybenzoate, 1,4-dihydroxy 2-naphthoate, homogentisate and α-glycerophosphate cannot act as prenyl-acceptor substrates [2]. The other enzymes involved in the biosynthesis of polar lipids in Archaea are EC 1.1.1.261 (sn-glycerol-1-phosphate dehydrogenase), EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase), which, together with this enzyme, alkylates the hydroxy groups of glycerol 1-phosphate to yield unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 [CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase] to form CDP-unsaturated archaeol. The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine [3]. Belongs in the UbiA prenyltransferase family [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 124650-68-6
References:
1.  Zhang, D.-L., Daniels, L. and Poulter, C.D. Biosynthesis of archaebacterial membranes. Formation of isoprene ethers by a prenyl transfer reaction. J. Am. Chem. Soc. 112 (1990) 1264–1265.
2.  Hemmi, H., Shibuya, K., Takahashi, Y., Nakayama, T. and Nishino, T. (S)-2,3-Di-O-geranylgeranylglyceryl phosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. Molecular cloning and characterization of a membrane-intrinsic prenyltransferase involved in the biosynthesis of archaeal ether-linked membrane lipids. J. Biol. Chem. 279 (2004) 50197–50203. [DOI] [PMID: 15356000]
3.  Morii, H., Nishihara, M. and Koga, Y. CTP:2,3-di-O-geranylgeranyl-sn-glycero-1-phosphate cytidyltransferase in the methanogenic archaeon Methanothermobacter thermoautotrophicus. J. Biol. Chem. 275 (2000) 36568–36574. [DOI] [PMID: 10960477]
[EC 2.5.1.42 created 1992, modified 2009]
 
 
EC 2.5.1.58     
Accepted name: protein farnesyltransferase
Reaction: farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Other name(s): FTase
Systematic name: farnesyl-diphosphate:protein-cysteine farnesyltransferase
Comments: This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, γ-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 131384-38-8
References:
1.  Furfine, E.S., Leban, J.J., Landavazo, A., Moomaw, J.F. and Casey, P.J. Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. Biochemistry 34 (1995) 6857–6862. [PMID: 7756316]
2.  Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289–5292. [DOI] [PMID: 8621375]
3.  Long, S.B., Casey, P.J. and Beese, L.S. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry 37 (1998) 9612–9618. [DOI] [PMID: 9657673]
4.  Micali, E., Chehade, K.A., Isaacs, R.J., Andres, D.A. and Spielmann, H.P. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. Biochemistry 40 (2001) 12254–12265. [DOI] [PMID: 11591144]
5.  Long, S.B., Casey, P.J. and Beese, L.S. Reaction path of protein farnesyltransferase at atomic resolution. Nature 419 (2002) 645–650. [DOI] [PMID: 12374986]
6.  Gibbs, R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, pp. 31–118.
[EC 2.5.1.58 created 2003]
 
 
EC 2.5.1.59     
Accepted name: protein geranylgeranyltransferase type I
Reaction: geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Other name(s): GGTase-I; GGTaseI
Systematic name: geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Comments: This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 atom of the geranylgeranyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably leucine; serine, methionine, alanine or glutamine makes the protein a substrate for EC 2.5.1.58. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Known targets of this enzyme include most γ-subunits of heterotrimeric G proteins and Ras-related GTPases such as members of the Ras and Rac/Rho families. A zinc metalloenzyme. The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 135371-29-8
References:
1.  Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289–5292. [DOI] [PMID: 8621375]
2.  Zhang, F.L. and Casey, P.J. Influence of metal ions on substrate binding and catalytic activity of mammalian protein geranylgeranyltransferase type-I. Biochem. J. 320 (1996) 925–932. [PMID: 9003382]
3.  Gibbs, R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, pp. 31–118.
[EC 2.5.1.59 created 2003]
 
 
EC 2.5.1.60     
Accepted name: protein geranylgeranyltransferase type II
Reaction: geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Other name(s): GGTaseII; Rab geranylgeranyltransferase; RabGGTase; geranylgeranyl-diphosphate,geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Systematic name: geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
Comments: This enzyme, along with protein farnesyltransferase (EC 2.5.1.58) and protein geranylgeranyltransferase type I (EC 2.5.1.59), constitutes the protein prenyltransferase family of enzymes. Attaches geranylgeranyl groups to two C-terminal cysteines in Ras-related GTPases of a single family, the Rab family (Ypt/Sec4 in lower eukaryotes) that terminate in XXCC, XCXC and CCXX motifs. Reaction is entirely dependent on the Rab substrate being bound to Rab escort protein (REP). Post-translational modification with the geranylgeranyl moiety is essential for Rab GTPases to be able to control the processes of membrane docking and fusion [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 135371-29-8
References:
1.  Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289–5292. [DOI] [PMID: 8621375]
2.  Wilson, A.L., Erdman, R.A., Castellano, F. and Maltese, W.A. Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases. Biochem. J. 333 (1998) 497–504. [PMID: 9677305]
3.  Zhang, H., Seabra, M.C. and Deisenhofer, J. Crystal structure of Rab geranylgeranyltransferase at 2.0 Å resolution. Structure 8 (2000) 241–251. [PMID: 10745007]
4.  Thomä, N.H., Niculae, A., Goody, R.S. and Alexandrov, K. Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate. J. Biol. Chem. 276 (2001) 48631–48636. [DOI] [PMID: 11591706]
5.  Rak, A., Niculae, A., Kalinin, A., Thomä, N.H., Sidorovitch, V., Goody, R.S. and Alexandrov, K. In vitro assembly, purification, and crystallization of the Rab geranylgeranyl transferase:substrate complex. Protein Expr. Purif. 25 (2002) 23–30. [DOI] [PMID: 12071695]
6.  Gibbs, R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, pp. 31–118.
[EC 2.5.1.60 created 2003]
 
 
EC 2.5.1.62     
Accepted name: chlorophyll synthase
Reaction: chlorophyllide a + phytyl diphosphate = chlorophyll a + diphosphate
For diagram of the later stages of chlorophyll biosynthesis, click here
Systematic name: chlorophyllide-a:phytyl-diphosphate phytyltransferase
Comments: Requires Mg2+. The enzyme is modified by binding of the first substrate, phytyl diphosphate, before reaction of the modified enzyme with the second substrate, chlorophyllide a, can occur. The reaction also occurs when phytyl diphosphate is replaced by geranylgeranyl diphosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9077-08-1
References:
1.  Schmid, H.C., Rassadina, V., Oster, U., Schoch, S. and Rüdiger, W. Pre-loading of chlorophyll synthase with tetraprenyl diphosphate is an obligatory step in chlorophyll biosynthesis. Biol. Chem. 383 (2002) 1769–1778. [DOI] [PMID: 12530542]
2.  Oster, U., Bauer, C.E. and Rüdiger, W. Characterization of chlorophyll a and bacteriochlorophyll a synthases by heterologous expression in Escherichia coli. J. Biol. Chem. 272 (1997) 9671–9676. [DOI] [PMID: 9092496]
3.  Rüdiger, W., Benz, J. and Guthoff, C. Detection and partial characterization of activity of chlorophyll synthetase in etioplast membranes. Eur. J. Biochem. 109 (1980) 193–200. [DOI] [PMID: 7408876]
[EC 2.5.1.62 created 2003]
 
 
EC 2.5.1.67     
Accepted name: chrysanthemyl diphosphate synthase
Reaction: 2 prenyl diphosphate = diphosphate + chrysanthemyl diphosphate
For diagram of reaction, click here
Glossary: chrysanthemyl = [2,2-dimethyl-3-(2-methylprop-1-en-1-yl)cyclopropyl]methyl
chrysanthemic acid = 2,2-dimethyl-3-(2-methylprop-1-en-1-yl)cyclopropane-1-carboxylic acid
Other name(s): CPPase; dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (chrysanthemyl-diphosphate-forming)
Systematic name: prenyl-diphosphate:prenyl-diphosphate prenyltransferase (chrysanthemyl-diphosphate-forming)
Comments: Requires a divalent metal ion for activity, with Mg2+ being better than Mn2+ [1]. Chrysanthemyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. The mechanism of its formation is similar to that of the early steps of squalene and phytoene biosynthesis. Chrysanthemyl diphosphate is the precursor of chrysanthemic acid, the acid half of the pyrethroid insecticides found in chrysanthemums.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Rivera, S.B., Swedlund, B.D., King, G.J., Bell, R.N., Hussey, C.E., Jr., Shattuck-Eidens, D.M., Wrobel, W.M., Peiser, G.D. and Poulter, C.D. Chrysanthemyl diphosphate synthase: isolation of the gene and characterization of the recombinant non-head-to-tail monoterpene synthase from Chrysanthemum cinerariaefolium. Proc. Natl. Acad. Sci. USA 98 (2001) 4373–4378. [DOI] [PMID: 11287653]
2.  Erickson, H.K. and Poulter, C.D. Chrysanthemyl diphosphate synthase. The relationship among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway. J. Am. Chem. Soc. 125 (2003) 6886–6888. [DOI] [PMID: 12783539]
[EC 2.5.1.67 created 2007]
 
 
EC 2.5.1.68     
Accepted name: (2Z,6E)-farnesyl diphosphate synthase
Reaction: geranyl diphosphate + isopentenyl diphosphate = diphosphate + (2Z,6E)-farnesyl diphosphate
For diagram of trans-polycis-polyprenol diphosphate biosynthesis, click here
Other name(s): (Z)-farnesyl diphosphate synthase; Z-farnesyl diphosphate synthase
Systematic name: geranyl-diphosphate:isopentenyl-diphosphate geranylcistransferase
Comments: Requires Mg2+ or Mn2+ for activity. The product of this reaction is an intermediate in the synthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of most features of the mycobacterial cell wall, including peptidoglycan, linker unit galactan and arabinan. Neryl diphosphate can also act as substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Schulbach, M.C., Mahapatra, S., Macchia, M., Barontini, S., Papi, C., Minutolo, F., Bertini, S., Brennan, P.J. and Crick, D.C. Purification, enzymatic characterization, and inhibition of the Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J. Biol. Chem. 276 (2001) 11624–11630. [DOI] [PMID: 11152452]
[EC 2.5.1.68 created 2007, modified 2010]
 
 
EC 2.5.1.69     
Accepted name: lavandulyl diphosphate synthase
Reaction: 2 prenyl diphosphate = diphosphate + lavandulyl diphosphate
For diagram of reaction, click here
Glossary: lavandulyl = 5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl
Other name(s): FDS-5; dimethylallyl-diphosphate:dimethylallyl-diphosphate dimethylallyltransferase (lavandulyl-diphosphate-forming)
Systematic name: prenyl-diphosphate:prenyl-diphosphate prenyltransferase (lavandulyl-diphosphate-forming)
Comments: Lavandulyl diphosphate is a monoterpene with a non-head-to-tail linkage. It is unlike most monoterpenoids, which are derived from geranyl diphosphate and have isoprene units that are linked head-to-tail. When this enzyme is incubated with prenyl diphosphate and 3-methylbut-3-en-1-yl diphosphate, it also forms the regular monoterpene geranyl diphosphate [2]. The enzyme from Artemisia tridentata (big sagebrush) forms both lavandulyl diphosphate and chrysanthemyl diphosphate (see EC 2.5.1.67, chrysanthemyl diphosphate synthase) when prenyl diphosphate is the sole substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Erickson, H.K. and Poulter, C.D. Chrysanthemyl diphosphate synthase. The relationship among chain elongation, branching, and cyclopropanation reactions in the isoprenoid biosynthetic pathway. J. Am. Chem. Soc. 125 (2003) 6886–6888. [DOI] [PMID: 12783539]
2.  Hemmerlin, A., Rivera, S.B., Erickson, H.K. and Poulter, C.D. Enzymes encoded by the farnesyl diphosphate synthase gene family in the Big Sagebrush Artemisia tridentata ssp. spiciformis. J. Biol. Chem. 278 (2003) 32132–32140. [DOI] [PMID: 12782626]
[EC 2.5.1.69 created 2007]
 
 
EC 2.5.1.70     
Accepted name: naringenin 8-dimethylallyltransferase
Reaction: prenyl diphosphate + (–)-(2S)-naringenin = diphosphate + sophoraflavanone B
For diagram of sophoraflavanone G biosynthesis, click here
Glossary: dimethylallyl = prenyl = 3-methylbut-2-en-1-yl
(–)-(2S)-naringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-2,3-dihydrochromen-4-one
sophoraflavanone B = (–)-(2S)-8-prenylnaringenin = (–)-(2S)-5,7-dihydroxy-2-(4-hydroxyphenyl)-8-(3-methylbut-2-en-1-yl)-2,3-dihydrochromen-4-one
Other name(s): N8DT; dimethylallyl-diphosphate:naringenin 8-dimethylallyltransferase
Systematic name: prenyl-diphosphate:naringenin 8-prenyltransferase
Comments: Requires Mg2+. This membrane-bound protein is located in the plastids [2]. In addition to naringenin, the enzyme can prenylate several other flavanones at the C-8 position, but more slowly. Along with EC 1.14.14.142 (8-dimethylallylnaringenin 2′-hydroxylase) and EC 2.5.1.71 (leachianone-G 2′′-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yamamoto, H., Senda, M. and Inoue, K. Flavanone 8-dimethylallyltransferase in Sophora flavescens cell suspension cultures. Phytochemistry 54 (2000) 649–655. [DOI] [PMID: 10975499]
2.  Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [DOI] [PMID: 14551337]
[EC 2.5.1.70 created 2007]
 
 
EC 2.5.1.71     
Accepted name: leachianone-G 2′′-dimethylallyltransferase
Reaction: prenyl diphosphate + leachianone G = diphosphate + sophoraflavanone G
For diagram of sophoraflavanone G biosynthesis, click here
Glossary: dimethylallyl = prenyl = 3-methylbut-2-en-1-yl
isopentenyl = 3-methylbut-3-en-1-yl
lavandulyl = 5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl
leachianone G = (–)-(2S)-2′-hydroxy-8-prenylnaringenin = (–)-(2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-(3-methylbut-2-en-1-yl)-2,3-dihydro-4H-chromen-4-one
sophoraflavanone G = (2S)-2-(2,4-dihydroxyphenyl)-5,7-dihydroxy-8-[(2R)-5-methyl-2-(prop-1-en-2-yl)hex-4-en-1-yl]-2,3-dihydro-4H-chromen-4-one
Other name(s): LG 2′′-dimethylallyltransferase; leachianone G 2′′-dimethylallyltransferase; LGDT; dimethylallyl-diphosphate:leachianone-G 2′′-dimethylallyltransferase
Systematic name: prenyl-diphosphate:leachianone-G 2′′-prenyltransferase
Comments: This membrane-bound enzyme is located in the plastids and requires Mg2+ for activity. The reaction forms the lavandulyl sidechain of sophoraflavanone G by transferring a prenyl group to the 2′′ position of another prenyl group attached at position 8 of leachianone G. The enzyme is specific for prenyl diphosphate as the prenyl donor, as it cannot be replaced by isopentenyl diphosphate or geranyl diphosphate. Euchrenone a7 (a 5-deoxy derivative of leachianone G) and kenusanone I (a 7-methoxy derivative of leachianone G) can also act as substrates, but more slowly. Along with EC 1.14.14.142 (8-dimethylallylnaringenin 2′-hydroxylase) and EC 2.5.1.70 (naringenin 8-dimethylallyltransferase), this enzyme forms part of the sophoraflavanone-G-biosynthesis pathway.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhao, P., Inoue, K., Kouno, I. and Yamamoto, H. Characterization of leachianone G 2′′-dimethylallyltransferase, a novel prenyl side-chain elongation enzyme for the formation of the lavandulyl group of sophoraflavanone G in Sophora flavescens Ait. cell suspension cultures. Plant Physiol. 133 (2003) 1306–1313. [DOI] [PMID: 14551337]
[EC 2.5.1.71 created 2007]
 
 
EC 2.5.1.74     
Accepted name: 1,4-dihydroxy-2-naphthoate polyprenyltransferase
Reaction: an all-trans-polyprenyl diphosphate + 1,4-dihydroxy-2-naphthoate = a demethylmenaquinone + diphosphate + CO2
For diagram of vitamin K biosynthesis, click here
Glossary: menaquinone = vitamin K2
Systematic name: all-trans-polyprenyl-diphosphate:1,4-dihydroxy-2-naphthoate polyprenyltransferase
Comments: This enzyme catalyses a step in the synthesis of menaquinone, in which the prenyl chain synthesized by polyprenyl diphosphate synthase is transferred to 1,4-dihydroxy-2-naphthoate (DHNA). The bacterial enzyme is an inner membrane protein [1], with the C-terminus located in the periplasm [3]. It is highly specific for DHNA but not for a specific length of the prenyl chain [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Shineberg, B. and Young, I.G. Biosynthesis of bacterial menaquinones: the membrane-associated 1,4-dihydroxy-2-naphthoate octaprenyltransferase of Escherichia coli. Biochemistry 15 (1976) 2754–2758. [PMID: 949474]
2.  Saito, Y. and Ogura, K. Biosynthesis of menaquinones. Enzymatic prenylation of 1,4-dihydroxy-2-naphthoate by Micrococcus luteus membrane fractions. J. Biochem. 89 (1981) 1445–1452. [PMID: 7275947]
3.  Suvarna, K., Stevenson, D., Meganathan, R. and Hudspeth, M.E. Menaquinone (vitamin K2) biosynthesis: localization and characterization of the menA gene from Escherichia coli. J. Bacteriol. 180 (1998) 2782–2787. [PMID: 9573170]
4.  Daley, D.O., Rapp, M., Granseth, E., Melen, K., Drew, D. and von Heijne, G. Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 (2005) 1321–1323. [DOI] [PMID: 15919996]
[EC 2.5.1.74 created 2009]
 
 
EC 2.5.1.75     
Accepted name: tRNA dimethylallyltransferase
Reaction: prenyl diphosphate + adenosine37 in tRNA = diphosphate + N6-(3-methylbut-2-en-1-yl)-adenosine37 in tRNA
For diagram of N6-(Dimethylallyl)adenosine37 modified tRNA biosynthesis, click here
Glossary: N6-(3-methylbut-2-en-1-yl)-adenine37 in tRNA = N6-dimethylallyladenine37 in tRNA
Other name(s): tRNA prenyltransferase; MiaA; transfer ribonucleate isopentenyltransferase (incorrect); Δ2-isopentenyl pyrophosphate:tRNA-Δ2-isopentenyl transferase (incorrect); Δ2-isopentenyl pyrophosphate:transfer ribonucleic acid Δ2-isopentenyltransferase (incorrect); dimethylallyl-diphosphate: tRNA dimethylallyltransferase; dimethylallyl-diphosphate:adenine37 in tRNA dimethylallyltransferase
Systematic name: prenyl-diphosphate:adenine37 in tRNA prenyltransferase
Comments: Formerly known as tRNA isopentenyltransferase, but it is now known that prenyl diphosphate, rather than isopentenyl diphosphate, is the substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Leung, H.C., Chen, Y. and Winkler, M.E. Regulation of substrate recognition by the MiaA tRNA prenyltransferase modification enzyme of Escherichia coli K-12. J. Biol. Chem. 272 (1997) 13073–13083. [DOI] [PMID: 9148919]
2.  Soderberg, T. and Poulter, C.D. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: essential elements for recognition of tRNA substrates within the anticodon stem-loop. Biochemistry 39 (2000) 6546–6553. [DOI] [PMID: 10828971]
3.  Moore, J.A., Mathis, J.R. and Poulter, C.D. Escherichia coli dimethylallyl diphosphate:tRNA dimethylallyltransferase: pre-steady-state kinetic studies. Biochim. Biophys. Acta 1479 (2000) 166–174. [DOI] [PMID: 11004538]
[EC 2.5.1.75 created 1972 as EC 2.5.1.8, transferred 2009 to EC 2.5.1.75]
 
 
EC 2.5.1.80     
Accepted name: 7-dimethylallyltryptophan synthase
Reaction: prenyl diphosphate + L-tryptophan = diphosphate + 7-prenyl-L-tryptophan
Glossary: prenyl = 3-methylbut-2-en-1-yl
Other name(s): 7-DMATS; dimethylallyl-diphosphate:L-tryptophan 7-dimethylallyltransferase
Systematic name: prenyl-diphosphate:L-tryptophan 7-prenyltransferase
Comments: This enzyme is more flexible towards the aromatic substrate than EC 2.5.1.34 (4-dimethylallyltryptophan synthase), but similar to that enzyme, accepts only prenyl diphosphate as the prenyl donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kremer, A. and Li, S.M. Potential of a 7-dimethylallyltryptophan synthase as a tool for production of prenylated indole derivatives. Appl. Microbiol. Biotechnol. 79 (2008) 951–961. [DOI] [PMID: 18481055]
2.  Kremer, A., Westrich, L. and Li, S.M. A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: overproduction, purification and biochemical characterization. Microbiology 153 (2007) 3409–3416. [DOI] [PMID: 17906140]
[EC 2.5.1.80 created 2010]
 
 
EC 2.5.1.81     
Accepted name: geranylfarnesyl diphosphate synthase
Reaction: geranylgeranyl diphosphate + isopentenyl diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate + diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): FGPP synthase; (all-E) geranylfarnesyl diphosphate synthase; GFPS; Fgs
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 1 isopentenyl unit)
Comments: The enzyme from Methanosarcina mazei is involved in biosynthesis of the polyprenyl side-chain of methanophenazine, an electron carrier utilized for methanogenesis. It prefers geranylgeranyl diphosphate and farnesyl diphosphate as allylic substrate [1]. The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate. The enzyme is involved in the biosynthesis of C25-C25 membrane lipids [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ogawa, T., Yoshimura, T. and Hemmi, H. Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: Different role, different evolution. Biochem. Biophys. Res. Commun. 393 (2010) 16–20. [DOI] [PMID: 20097171]
2.  Tachibana, A., Yano, Y., Otani, S., Nomura, N., Sako, Y. and Taniguchi, M. Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. Molecular evolution with alteration in product specificity. Eur. J. Biochem. 267 (2000) 321–328. [DOI] [PMID: 10632701]
3.  Tachibana, A. A novel prenyltransferase, farnesylgeranyl diphosphate synthase, from the haloalkaliphilic archaeon, Natronobacterium pharaonis. FEBS Lett. 341 (1994) 291–294. [DOI] [PMID: 8137956]
4.  Lee, P.C., Mijts, B.N., Petri, R., Watts, K.T. and Schmidt-Dannert, C. Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution. Protein Eng. Des. Sel. 17 (2004) 771–777. [DOI] [PMID: 15548566]
[EC 2.5.1.81 created 2010]
 
 
EC 2.5.1.82     
Accepted name: hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
Reaction: geranylgeranyl diphosphate + 2 (3-methylbut-3-en-1-yl diphosphate) = 2 diphosphate + all-trans-hexaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): HexPS(ambiguous); (all-E) hexaprenyl diphosphate synthase; (all-trans) hexaprenyl diphosphate synthase; hexaprenyl pyrophosphate synthase (ambiguous); HexPPs (ambiguous); hexaprenyl diphosphate synthase (ambiguous); geranylgeranyl-diphosphate:isopentenyl-diphosphate transferase (adding 2 isopentenyl units)
Systematic name: geranylgeranyl-diphosphate:3-methylbut-3-en-1-yl-diphosphate transferase (adding 2 units of 3-methylbut-3-en-1-yl)
Comments: The enzyme prefers geranylgeranyl diphosphate to farnesyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and prenyl diphosphate. Requires Mg2+ [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hemmi, H., Ikejiri, S., Yamashita, S. and Nishino, T. Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus. J. Bacteriol. 184 (2002) 615–620. [DOI] [PMID: 11790729]
2.  Hemmi, H., Noike, M., Nakayama, T. and Nishino, T. Change of product specificity of hexaprenyl diphosphate synthase from Sulfolobus solfataricus by introducing mimetic mutations. Biochem. Biophys. Res. Commun. 297 (2002) 1096–1101. [DOI] [PMID: 12372398]
3.  Sun, H.Y., Ko, T.P., Kuo, C.J., Guo, R.T., Chou, C.C., Liang, P.H. and Wang, A.H. Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic crenarchaeon Sulfolobus solfataricus displays asymmetric subunit structures. J. Bacteriol. 187 (2005) 8137–8148. [DOI] [PMID: 16291686]
[EC 2.5.1.82 created 1984 as EC 2.5.1.33, part transferred 2010 to EC 2.5.1.82]
 
 
EC 2.5.1.83     
Accepted name: hexaprenyl diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
Reaction: (2E,6E)-farnesyl diphosphate + 3 (3-methylbut-3-en-1-yl diphosphate) = 3 diphosphate + all-trans-hexaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Other name(s): HexPS (ambiguous); hexaprenyl pyrophosphate synthetase (ambiguous); hexaprenyl diphosphate synthase (ambiguous); (2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase (adding 3 isopentenyl units)
Systematic name: (2E,6E)-farnesyl-diphosphate:3-methylbut-3-en-1-yl-diphosphate farnesyltranstransferase (adding 3 units of 3-methylbut-3-en-1-yl)
Comments: The enzyme prefers farnesyl diphosphate to geranylgeranyl diphosphate as an allylic substrate and does not show activity for geranyl diphosphate and prenyl diphosphate [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Fujii, H., Koyama, T. and Ogura, K. Hexaprenyl pyrophosphate synthetase from Micrococcus luteus B-P 26. Separation of two essential components. J. Biol. Chem. 257 (1982) 14610–14612. [PMID: 7174655]
2.  Shimizu, N., Koyama, T. and Ogura, K. Molecular cloning, expression, and characterization of the genes encoding the two essential protein components of Micrococcus luteus B-P 26 hexaprenyl diphosphate synthase. J. Bacteriol. 180 (1998) 1578–1581. [PMID: 9515931]
3.  Nagaki, M., Kimura, K., Kimura, H., Maki, Y., Goto, E., Nishino, T. and Koyama, T. Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases. Bioorg. Med. Chem. Lett. 11 (2001) 2157–2159. [DOI] [PMID: 11514159]
[EC 2.5.1.83 created 1984 as EC 2.5.1.33, part transferred 2010 to EC 2.5.1.83]
 
 
EC 2.5.1.84     
Accepted name: all-trans-nonaprenyl diphosphate synthase [geranyl-diphosphate specific]
Reaction: geranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-nonaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Glossary: solanesyl diphosphate = all-trans-nonaprenyl diphosphate
Other name(s): nonaprenyl diphosphate synthase (ambiguous); solanesyl diphosphate synthase (ambiguous); SolPP synthase (ambiguous); SPP-synthase (ambiguous); SPP synthase (ambiguous); solanesyl-diphosphate synthase (ambiguous); OsSPS2
Systematic name: geranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 7 isopentenyl units)
Comments: (2E,6E)-Farnesyl diphosphate and geranylgeranyl diphosphate are less effective as substrates than geranyl diphosphate. The enzyme is involved in the synthesis of the side chain of menaquinone-9 [1]. In Oryza sativa the enzyme SPS2 is involved in providing solanesyl diphosphate for plastoquinone-9 formation [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sagami, H., Ogura, K. and Seto, S. Solanesyl pyrophosphate synthetase from Micrococcus lysodeikticus. Biochemistry 16 (1977) 4616–4622. [PMID: 911777]
2.  Fujii, H., Sagami, H., Koyama, T., Ogura, K., Seto, S., Baba, T. and Allen, C.M. Variable product specificity of solanesyl pyrophosphate synthetase. Biochem. Biophys. Res. Commun. 96 (1980) 1648–1653. [DOI] [PMID: 7447947]
3.  Ohara, K., Sasaki, K. and Yazaki, K. Two solanesyl diphosphate synthases with different subcellular localizations and their respective physiological roles in Oryza sativa. J. Exp. Bot. 61 (2010) 2683–2692. [DOI] [PMID: 20421194]
4.  Ohnuma, S., Koyama, T. and Ogura, K. Purification of solanesyl-diphosphate synthase from Micrococcus luteus. A new class of prenyltransferase. J. Biol. Chem. 266 (1991) 23706–23713. [PMID: 1748647]
5.  Gotoh, T., Koyama, T. and Ogura, K. Farnesyl diphosphate synthase and solanesyl diphosphate synthase reactions of diphosphate-modified allylic analogs: the significance of the diphosphate linkage involved in the allylic substrates for prenyltransferase. J. Biochem. 112 (1992) 20–27. [PMID: 1429508]
6.  Teclebrhan, H., Olsson, J., Swiezewska, E. and Dallner, G. Biosynthesis of the side chain of ubiquinone:trans-prenyltransferase in rat liver microsomes. J. Biol. Chem. 268 (1993) 23081–23086. [PMID: 8226825]
[EC 2.5.1.84 created 1972 as EC 2.5.1.11, part transferred 2010 to EC 2.5.1.84]
 
 
EC 2.5.1.85     
Accepted name: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]
Reaction: geranylgeranyl diphosphate + 5 isopentenyl diphosphate = 5 diphosphate + all-trans-nonaprenyl diphosphate
For diagram of terpenoid biosynthesis, click here
Glossary: solanesyl diphosphate = all-trans-nonaprenyl diphosphate
Other name(s): nonaprenyl diphosphate synthase (ambiguous); solanesyl diphosphate synthase (ambiguous); At-SPS2; At-SPS1; SPS1; SPS2
Systematic name: geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase (adding 5 isopentenyl units)
Comments: Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate [1]. The plant Arabidopsis thaliana has two different enzymes that catalyse this reaction. SPS1 contributes to the biosynthesis of the ubiquinone side-chain while SPS2 supplies the precursor of the plastoquinone side-chains [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Hirooka, K., Bamba, T., Fukusaki, E. and Kobayashi, A. Cloning and kinetic characterization of Arabidopsis thaliana solanesyl diphosphate synthase. Biochem. J. 370 (2003) 679–686. [DOI] [PMID: 12437513]
2.  Hirooka, K., Izumi, Y., An, C.I., Nakazawa, Y., Fukusaki, E. and Kobayashi, A. Functional analysis of two solanesyl diphosphate synthases from Arabidopsis thaliana. Biosci. Biotechnol. Biochem. 69 (2005) 592–601. [DOI] [PMID: 15784989]
3.  Jun, L., Saiki, R., Tatsumi, K., Nakagawa, T. and Kawamukai, M. Identification and subcellular localization of two solanesyl diphosphate synthases from Arabidopsis thaliana. Plant Cell Physiol. 45 (2004) 1882–1888. [DOI] [PMID: 15653808]
[EC 2.5.1.85 created 1972 as EC 2.5.1.11, part transferred 2010 to EC 2.5.1.85]
 
 
EC 2.5.1.86     
Accepted name: trans,polycis-decaprenyl diphosphate synthase
Reaction: (2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + trans,octacis-decaprenyl diphosphate
For diagram of trans,polycis-polyprenol diphosphate biosynthesis, click here
Other name(s): Rv2361c; (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate synthase
Systematic name: (2Z,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesylcistransferase (adding 7 isopentenyl units)
Comments: The enzyme is involved in the biosynthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of essential mycobacterial cell wall components, such as the mycolyl-arabinogalactan-peptidoglycan complex and lipoarabinomannan [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kaur, D., Brennan, P.J. and Crick, D.C. Decaprenyl diphosphate synthesis in Mycobacterium tuberculosis. J. Bacteriol. 186 (2004) 7564–7570. [DOI] [PMID: 15516568]
2.  Wang, W., Dong, C., McNeil, M., Kaur, D., Mahapatra, S., Crick, D.C. and Naismith, J.H. The structural basis of chain length control in Rv1086. J. Mol. Biol. 381 (2008) 129–140. [DOI] [PMID: 18597781]
3.  Crick, D.C., Schulbach, M.C., Zink, E.E., Macchia, M., Barontini, S., Besra, G.S. and Brennan, P.J. Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and Mycobacterium smegmatis. J. Bacteriol. 182 (2000) 5771–5778. [DOI] [PMID: 11004176]
[EC 2.5.1.86 created 2010]
 
 


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