The Enzyme Database

Your query returned 17 entries.    printer_iconPrintable version

EC 1.17.1.2      
Transferred entry: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, now classified as EC 1.17.7.4, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase.
[EC 1.17.1.2 created 2003, modified 2009, deleted 2016]
 
 
EC 2.5.1.8      
Transferred entry: tRNA isopentenyltransferase. As it is now known that the substrate is dimethylallyl diphosphate, the enzyme has been transferred to EC 2.5.1.75, tRNA dimethylallyltransferase
[EC 2.5.1.8 created 1972, deleted 2009]
 
 
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 2.5.1.29     
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 2.5.1.34     
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 2.5.1.75     
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 2.5.1.92     
Accepted name: (2Z,6Z)-farnesyl diphosphate synthase
Reaction: prenyl diphosphate + 2 isopentenyl diphosphate = 2 diphosphate + (2Z,6Z)-farnesyl diphosphate
(1a) prenyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate
(1b) neryl diphosphate + isopentenyl diphosphate = diphosphate + (2Z,6Z)-farnesyl diphosphate
For diagram of all-cis-polyprenyl diphosphate, click here
Glossary: prenyl diphosphate = dimethylallyl diphosphate
Other name(s): cis,cis-farnesyl diphosphate synthase; Z,Z-FPP synthase; zFPS; Z,Z-farnesyl pyrophosphate synthase; dimethylallyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 2 isopentenyl units)
Systematic name: prenyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 2 isopentenyl units)
Comments: This enzyme, originally characterized from wild tomato, specifically forms (2Z,6Z)-farnesyl diphosphate via neryl diphosphate and isopentenyl diphosphate. In wild tomato it is involved in the biosynthesis of several sesquiterpenes. See also EC 2.5.1.68 [(2Z,6E)-farnesyl diphosphate synthase] and EC 2.5.1.10 [(2E,6E)-farnesyl diphosphate synthase].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sallaud, C., Rontein, D., Onillon, S., Jabes, F., Duffe, P., Giacalone, C., Thoraval, S., Escoffier, C., Herbette, G., Leonhardt, N., Causse, M. and Tissier, A. A novel pathway for sesquiterpene biosynthesis from Z,Z-farnesyl pyrophosphate in the wild tomato Solanum habrochaites. Plant Cell 21 (2009) 301–317. [DOI] [PMID: 19155349]
[EC 2.5.1.92 created 2010, modified 2011]
 
 
EC 2.5.1.107     
Accepted name: verruculogen prenyltransferase
Reaction: prenyl diphosphate + verruculogen = diphosphate + fumitremorgin A
For diagram of fumitremorgin alkaloid biosynthesis (part 2), click here
Glossary: prenyl diphosphate = dimethylallyl diphosphate
verruculogen = (5R,10S,10aR,14aS,15bS)-10,10a-dihydroxy-6-methoxy-2,2-dimethyl-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(2H,13H)-dione
fumitremorgin A = (5R,10S,10aR,14aS,15bS)-10a-hydroxy-7-methoxy-2,2-dimethyl-10-[(3-methylbut-2-en-1-yl)oxy]-5-(2-methylprop-1-en-1-yl)-1,10,10a,14,14a,15b-hexahydro-12H-3,4-dioxa-5a,11a,15a-triazacycloocta[1,2,3-lm]indeno[5,6-b]fluorene-11,15(H,13H)-dione
Other name(s): FtmPT3; dimethylallyl-diphosphate:verruculogen dimethylallyl-O-transferase
Systematic name: prenyl-diphosphate:verruculogen dimethylallyl-O-transferase
Comments: Found in a number of fungi. Catalyses the last step in the biosynthetic pathway of the indole alkaloid fumitremorgin A. The enzyme from the fungus Neosartorya fischeri is also active with fumitremorgin B and 12α,13α-dihydroxyfumitremorgin C.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mundt, K., Wollinsky, B., Ruan, H.L., Zhu, T. and Li, S.M. Identification of the verruculogen prenyltransferase FtmPT3 by a combination of chemical, bioinformatic and biochemical approaches. ChemBioChem 13 (2012) 2583–2592. [DOI] [PMID: 23109474]
[EC 2.5.1.107 created 2013]
 
 
EC 2.5.1.111     
Accepted name: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Reaction: prenyl diphosphate + 3-(4-hydroxyphenyl)pyruvate = diphosphate + 3-(4-hydroxy-3-prenylphenyl)pyruvate
For diagram of 3-dimethylallyl-4-hydroxybenzoate biosynthesis, click here and for diagram of 4-hydroxyphenylpyruvate metabolites, click here
Glossary: 3-dimethylallyl-4-hydroxyphenylpyruvate = 3-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]-2-oxopropanoate
Other name(s): CloQ; 4HPP dimethylallyltransferase; NovQ; dimethylallyl diphosphate:4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Systematic name: prenyl-diphosphate:3-(4-hydroxyphenyl)pyruvate 3′-prenyltransferase
Comments: The enzyme's product feeds into the biosynthesis of the aminocoumarin antibiotics clorobiocin and novobiocin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Pojer, F., Wemakor, E., Kammerer, B., Chen, H., Walsh, C.T., Li, S.M. and Heide, L. CloQ, a prenyltransferase involved in clorobiocin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 2316–2321. [DOI] [PMID: 12618544]
2.  Keller, S., Pojer, F., Heide, L. and Lawson, D.M. Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1153–1155. [DOI] [PMID: 17077503]
3.  Metzger, U., Keller, S., Stevenson, C.E., Heide, L. and Lawson, D.M. Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway. J. Mol. Biol. 404 (2010) 611–626. [DOI] [PMID: 20946900]
4.  Ozaki, T., Mishima, S., Nishiyama, M. and Kuzuyama, T. NovQ is a prenyltransferase capable of catalyzing the addition of a dimethylallyl group to both phenylpropanoids and flavonoids. J. Antibiot. (Tokyo) 62 (2009) 385–392. [DOI] [PMID: 19557032]
[EC 2.5.1.111 created 2013]
 
 
EC 2.5.1.112     
Accepted name: adenylate dimethylallyltransferase (ADP/ATP-dependent)
Reaction: (1) prenyl diphosphate + ADP = diphosphate + N6-prenyladenosine 5′-diphosphate
(2) prenyl diphosphate + ATP = diphosphate + N6-prenyladenosine 5′-triphosphate
For diagram of N6-(Dimethylallyl)adenosine phosphates biosynthesis, click here
Other name(s): cytokinin synthase (ambiguous); isopentenyltransferase (ambiguous); 2-isopentenyl-diphosphate:ADP/ATP Δ2-isopentenyltransferase; adenylate isopentenyltransferase (ambiguous); dimethylallyl diphosphate:ATP/ADP isopentenyltransferase: IPT; dimethylallyl-diphosphate:ADP/ATP dimethylallyltransferase
Systematic name: prenyl-diphosphate:ADP/ATP prenyltransferase
Comments: Involved in the biosynthesis of cytokinins in plants. The IPT4 isoform from the plant Arabidopsis thaliana is specific for ADP and ATP [1]. Other isoforms, such as IPT1 from Arabidopsis thaliana [1,2] and the enzyme from the common hop, Humulus lupulus [3], also have a lower activity with AMP (cf. EC 2.5.1.27, adenylate dimethylallyltransferase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kakimoto, T. Identification of plant cytokinin biosynthetic enzymes as dimethylallyl diphosphate:ATP/ADP isopentenyltransferases. Plant Cell Physiol. 42 (2001) 677–685. [PMID: 11479373]
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 2.5.1.112 created 2013]
 
 
EC 2.5.1.121     
Accepted name: 5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
Reaction: prenyl diphosphate + 5,10-dihydrophenazine-1-carboxylate = diphosphate + 9-prenyl-5,10-dihydrophenazine-1-carboxylate
Glossary: 9-prenyl-5,10-dihydrophenazine-1-carboxylate = 9-(3-methylbut-2-en-1-yl)-5,10-dihydrophenazine-1-carboxylate
Other name(s): PpzP; dihydrophenazine-1-carboxylate dimethylallyltransferase; 5,10-dihydrophenazine 1-carboxylate dimethylallyltransferase; dimethylallyl diphosphate:5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase
Systematic name: prenyl-diphosphate:5,10-dihydrophenazine-1-carboxylate 9-prenyltransferase
Comments: The enzyme is involved in the biosynthesis of prenylated phenazines by the bacterium Streptomyces anulatus. It is specific for both prenyl diphosphate and 5,10-dihydrophenazine-1-carboxylate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Saleh, O., Gust, B., Boll, B., Fiedler, H.P. and Heide, L. Aromatic prenylation in phenazine biosynthesis: dihydrophenazine-1-carboxylate dimethylallyltransferase from Streptomyces anulatus. J. Biol. Chem. 284 (2009) 14439–14447. [DOI] [PMID: 19339241]
[EC 2.5.1.121 created 2014]
 
 
EC 2.5.1.122     
Accepted name: 4-O-dimethylallyl-L-tyrosine synthase
Reaction: prenyl diphosphate + L-tyrosine = diphosphate + 4-O-prenyl-L-tyrosine
Other name(s): SirD; dimethylallyl diphosphate:L-tyrosine 4-O-dimethylallyltransferase
Systematic name: prenyl-diphosphate:L-tyrosine 4-O-prenyltransferase
Comments: The enzyme is involved in biosynthesis of the phytotoxin sirodesmin PL by the phytopathogenic ascomycete Leptosphaeria maculans.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kremer, A. and Li, S.M. A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL. Microbiology 156 (2010) 278–286. [DOI] [PMID: 19762440]
2.  Zou, H.X., Xie, X., Zheng, X.D. and Li, S.M. The tyrosine O-prenyltransferase SirD catalyzes O-, N-, and C-prenylations. Appl. Microbiol. Biotechnol. 89 (2011) 1443–1451. [DOI] [PMID: 21038099]
[EC 2.5.1.122 created 2014]
 
 
EC 2.5.1.158     
Accepted name: hexaprenyl diphosphate synthase (prenyl-diphosphate specific)
Reaction: prenyl diphosphate + 5 3-methylbut-3-en-1-yl diphosphate = all-trans-hexaprenyl diphosphate + 5 diphosphate
Glossary: prenyl diphosphate = dimethylallyl diphosphate
3-methylbut-3-en-1-yl diphosphate = isopentenyl diphosphate
Other name(s): HexPPS
Systematic name: prenyl-diphosphate:3-methylbut-3-en-1-yl-diphosphate transferase (adding 5 units of 3-methylbut-3-en-1-yl)
Comments: This activity has been characterized from a number of fungal bifunctional enzymes. Following the formation of hexaprenyl diphosphate, a different domain in the enzymes catalyses its cyclization into a triterpene (see EC 4.2.3.221, macrophomene synthase and EC 4.2.3.220, talaropentaene synthase). cf. EC 2.5.1.82, hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Tao, H., Lauterbach, L., Bian, G., Chen, R., Hou, A., Mori, T., Cheng, S., Hu, B., Lu, L., Mu, X., Li, M., Adachi, N., Kawasaki, M., Moriya, T., Senda, T., Wang, X., Deng, Z., Abe, I., Dickschat, J.S. and Liu, T. Discovery of non-squalene triterpenes. Nature 606 (2022) 414–419. [DOI] [PMID: 35650436]
[EC 2.5.1.158 created 2024]
 
 
EC 2.5.1.159     
Accepted name: hapalindole G dimethylallyltransferase
Reaction: (1) prenyl diphosphate + hapalindole G = ambiguine A + diphosphate
(2) prenyl diphosphate + hapalindole U = ambiguine H + diphosphate
For diagram of hapalindole/fischerindole biosynthesis, click here
Glossary: prenyl diphosphate = dimethylallyl diphosphate
hapalindole G = (6aS,8R,9R,10R,10aS)-8-chloro-10-isocyano-6,6,9-trimethyl-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
ambiguine A = (6aS,8R,9R,10R,10aS)-8-chloro-10-isocyano-6,6,9-trimethyl-1-(2-methylbut-3-en-2-yl)-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
hapalindole U = (6aS,9R,10R,10aS)-10-isocyano-6,6,9-trimethyl-9-vinyl-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
ambiguine H = (6aS,9R,10R,10aS)-9-ethenyl-10-isocyano-6,6,9-trimethyl-1-(2-methylbut-3-en-2-yl)-2,6,6a,7,8,9,10,10a-octahydronaphtho[1,2,3-cd]indole
Other name(s): ambP3 (gene name); famD1 (gene name)
Systematic name: prenyl-diphosphate:hapalindole G prenyltransferase (ambiguine A-forming)
Comments: Requires Mg2+. The enzyme, characterized from the cyanobacterium Fischerella ambigua UTEX 1903, is involved in the biosynthesis of hapalindole-type alkaloids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hillwig, M.L., Zhu, Q. and Liu, X. Biosynthesis of ambiguine indole alkaloids in cyanobacterium Fischerella ambigua. ACS Chem. Biol. 9 (2014) 372–377. [DOI] [PMID: 24180436]
[EC 2.5.1.159 created 2024]
 
 
EC 3.6.1.76     
Accepted name: prenyl-diphosphate phosphatase
Reaction: (1) prenyl diphosphate + H2O = prenyl phosphate + phosphate
(2) 3-methylbut-3-en-1-yl diphosphate + H2O = 3-methylbut-3-en-1-yl phosphate + phosphate
Glossary: isopentenyl = 3-methylbut-3-en-1-yl
prenyl = 3-methylbut-2-en-1-yl = dimethylallyl
dimethylallyl diphosphate = DMAPP
isopentenyl diphosphate = IPP
Systematic name: prenyl diphosphate/3-methylbut-3-en-1-yl diphosphate phosphohydrolase
Comments: The enzyme, characterized from the methanogenic archaeon Methanosarcina mazei, belongs to the Nudix hydrolase family (a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to a moiety). Its main purpose is to provide the substrate for EC 2.5.1.129, flavin prenyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ishibashi, Y., Matsushima, N., Ito, T. and Hemmi, H. Isopentenyl diphosphate/dimethylallyl diphosphate-specific Nudix hydrolase from the methanogenic archaeon Methanosarcina mazei. Biosci. Biotechnol. Biochem. 86 (2022) 246–253. [DOI] [PMID: 34864834]
[EC 3.6.1.76 created 2022]
 
 
EC 4.2.3.27     
Accepted name: isoprene synthase
Reaction: prenyl diphosphate = isoprene + diphosphate
For diagram of isoprene biosynthesis and metabolism, click here
Glossary: isoprene = 2-methylbuta-1,3-diene
Other name(s): ISPC; ISPS; dimethylallyl-diphosphate diphosphate-lyase (isoprene-forming)
Systematic name: prenyl-diphosphate diphosphate-lyase (isoprene-forming)
Comments: Requires Mg2+ or Mn2+ for activity. This enzyme is located in the chloroplast of isoprene-emitting plants, such as poplar and aspen, and may be activitated by light-dependent changes in chloroplast pH and Mg2+ concentration [2,8].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 139172-14-8
References:
1.  Silver, G.M. and Fall, R. Enzymatic synthesis of isoprene from dimethylallyl diphosphate in aspen leaf extracts. Plant Physiol. 97 (1991) 1588–1591. [PMID: 16668590]
2.  Silver, G.M. and Fall, R. Characterization of aspen isoprene synthase, an enzyme responsible for leaf isoprene emission to the atmosphere. J. Biol. Chem. 270 (1995) 13010–13016. [DOI] [PMID: 7768893]
3.  Wildermuth, M.C. and Fall, R. Light-dependent isoprene emission (characterization of a thylakoid-bound isoprene synthase in Salix discolor chloroplasts). Plant Physiol. 112 (1996) 171–182. [PMID: 12226383]
4.  Schnitzler, J.P., Arenz, R., Steinbrecher, R. and Lehming, A. Characterization of an isoprene synthase from leaves of Quercus petraea. Bot. Acta 109 (1996) 216–221.
5.  Miller, B., Oschinski, C. and Zimmer, W. First isolation of an isoprene synthase gene from poplar and successful expression of the gene in Escherichia coli. Planta 213 (2001) 483–487. [PMID: 11506373]
6.  Sivy, T.L., Shirk, M.C. and Fall, R. Isoprene synthase activity parallels fluctuations of isoprene release during growth of Bacillus subtilis. Biochem. Biophys. Res. Commun. 294 (2002) 71–75. [DOI] [PMID: 12054742]
7.  Sasaki, K., Ohara, K. and Yazaki, K. Gene expression and characterization of isoprene synthase from Populus alba. FEBS Lett. 579 (2005) 2514–2518. [DOI] [PMID: 15848197]
8.  Schnitzler, J.-P., Zimmer, I., Bachl, A., Arend, M., Fromm, J. and Fischbach, R.J. Biochemical properties of isoprene synthase in poplar (Populus x canescens). Planta 222 (2005) 777–786. [DOI] [PMID: 16052321]
[EC 4.2.3.27 created 2007]
 
 


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