The Enzyme Database

Displaying entries 51-69 of 69.

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EC 2.7.8.27     
Accepted name: sphingomyelin synthase
Reaction: a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol
For diagram of reaction, click here
Glossary: sphingomyelin = a ceramide-1-phosphocholine
ceramide = an N-acylsphingoid. The fatty acids of naturally occurring ceramides range in chain length from about C16 to about C26 and may contain one or more double bonds and/or hydroxy substituents at C-2
sphingoid = sphinganine, i.e. D-erythro-2-aminooctadecane-1,3-diol, and its homologues and stereoisomers (see also Lip-1.4)
Other name(s): SM synthase; SMS1; SMS2
Systematic name: ceramide:phosphatidylcholine cholinephosphotransferase
Comments: The reaction can occur in both directions [3]. This enzyme occupies a central position in sphingolipid and glycerophospholipid metabolism [4]. Up- and down-regulation of its activity has been linked to mitogenic and pro-apoptotic signalling in a variety of mammalian cell types [4]. Unlike EC 2.7.8.3, ceramide cholinephosphotransferase, CDP-choline cannot replace phosphatidylcholine as the donor of the phosphocholine moiety of sphingomyelin [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 58703-97-2
References:
1.  Ullman, M.D. and Radin, N.S. The enzymatic formation of sphingomyelin from ceramide and lecithin in mouse liver. J. Biol. Chem. 249 (1974) 1506–1512. [PMID: 4817756]
2.  Voelker, D.R. and Kennedy, E.P. Cellular and enzymic synthesis of sphingomyelin. Biochemistry 21 (1982) 2753–2759. [PMID: 7093220]
3.  Huitema, K., van den Dikkenberg, J., Brouwers, J.F. and Holthuis, J.C. Identification of a family of animal sphingomyelin synthases. EMBO J. 23 (2004) 33–44. [DOI] [PMID: 14685263]
4.  Tafesse, F.G., Ternes, P. and Holthuis, J.C. The multigenic sphingomyelin synthase family. J. Biol. Chem. 281 (2006) 29421–29425. [DOI] [PMID: 16905542]
5.  Yamaoka, S., Miyaji, M., Kitano, T., Umehara, H. and Okazaki, T. Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J. Biol. Chem. 279 (2004) 18688–18693. [DOI] [PMID: 14976195]
[EC 2.7.8.27 created 2006]
 
 
EC 2.7.8.34     
Accepted name: CDP-L-myo-inositol myo-inositolphosphotransferase
Reaction: CDP-1L-myo-inositol + 1L-myo-inositol 1-phosphate = CMP + bis(1L-myo-inositol) 3,1′-phosphate 1-phosphate
For diagram of bis(1L-myo-inositol) 1,3′-phosphate biosynthesis, click here
Glossary: 1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate
Other name(s): CDP-inositol:inositol-1-phosphate transferase (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS)); DIPPS (bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase (IPCT/DIPPS))
Systematic name: CDP-1L-myo-inositol:1L-myo-inositol 1-phosphate myo-inositolphosphotransferase
Comments: In many organisms this activity is catalysed by a bifunctional enzyme. The di-myo-inositol-1,3′-phosphate-1′-phosphate synthase domain of the bifunctional EC 2.7.7.74/EC 2.7.8.34 (CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase) uses only 1L-myo-inositol 1-phosphate as an alcohol acceptor, but CDP-glycerol, as well as CDP-1L-myo-inositol and CDP-D-myo-inositol, are recognized as alcohol donors. The enzyme is involved in biosynthesis of bis(1L-myo-inositol) 1,3-phosphate, a widespread organic solute in microorganisms adapted to hot environments.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Rodrigues, M.V., Borges, N., Henriques, M., Lamosa, P., Ventura, R., Fernandes, C., Empadinhas, N., Maycock, C., da Costa, M.S. and Santos, H. Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol:inositol-1-phosphate transferase, the key enzyme for di-myo-inositol-phosphate synthesis in several (hyper)thermophiles. J. Bacteriol. 189 (2007) 5405–5412. [DOI] [PMID: 17526717]
[EC 2.7.8.34 created 2011]
 
 
EC 2.7.8.38     
Accepted name: archaetidylserine synthase
Reaction: (1) CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol + L-serine = CMP + 2,3-bis-(O-geranylgeranyl)-sn-glycero-1-phospho-L-serine
(2) CDP-2,3-bis-(O-phytanyl)-sn-glycerol + L-serine = CMP + 2,3-bis-(O-phytanyl)-sn-glycero-1-phospho-L-serine
For diagram of archaetidylserine biosynthesis, click here
Glossary: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol = CDP-unsaturated archaeol
2,3-bis-(O-geranylgeranyl)-sn-glycero-1-phospho-L-serine = unsaturated archaetidylserine
CDP-2,3-bis-(O-phytanyl)-sn-glycerol = CDP archaeol
2,3-bis-(O-phytanyl)-sn-glycero-1-phospho-L-serine = archaetidylserine
Systematic name: CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol:L-serine 2,3-bis-(O-geranylgeranyl)-sn-glycerol phosphotransferase
Comments: Requires Mn2+. Isolated from the archaeon Methanothermobacter thermautotrophicus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Morii, H. and Koga, Y. CDP-2,3-di-O-geranylgeranyl-sn-glycerol:L-serine O-archaetidyltransferase (archaetidylserine synthase) in the methanogenic archaeon Methanothermobacter thermautotrophicus. J. Bacteriol. 185 (2003) 1181–1189. [DOI] [PMID: 12562787]
[EC 2.7.8.38 created 2013, modified 2013]
 
 
EC 2.7.8.39     
Accepted name: archaetidylinositol phosphate synthase
Reaction: CDP-2,3-bis-(O-phytanyl)-sn-glycerol + 1L-myo-inositol 1-phosphate = CMP + 1-archaetidyl-1D-myo-inositol 3-phosphate
Glossary: 1L-myo-inositol 1-phosphate = 1D-myo-inositol 3-phosphate
CDP-2,3-bis-(O-phytanyl)-sn-glycerol = CDP-2,3-di-(O-phytanyl)-sn-glycerol = CDP-archaeol
1-archaetidyl-1D-myo-inositol 3-phosphate = archaetidyl-myo-inositol 1-phosphate
Other name(s): AIP synthase
Systematic name: CDP-2,3-bis-(O-phytanyl)-sn-glycerol:1L-myo-inositol 1-phosphate 1-sn-archaetidyltransferase
Comments: Requires Mg2+ or Mn2+ for activity. The enzyme is involved in biosynthesis of archaetidyl-myo-inositol, a compound essential for glycolipid biosynthesis in archaea.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Morii, H., Kiyonari, S., Ishino, Y. and Koga, Y. A novel biosynthetic pathway of archaetidyl-myo-inositol via archaetidyl-myo-inositol phosphate from CDP-archaeol and D-glucose 6-phosphate in methanoarchaeon Methanothermobacter thermautotrophicus cells. J. Biol. Chem. 284 (2009) 30766–30774. [DOI] [PMID: 19740749]
[EC 2.7.8.39 created 2013]
 
 
EC 2.7.8.41     
Accepted name: cardiolipin synthase (CMP-forming)
Reaction: a CDP-diacylglycerol + a phosphatidylglycerol = a cardiolipin + CMP
Systematic name: CDP-diacylglycerol:phosphatidylglycerol diacylglycerolphosphotransferase (CMP-forming)
Comments: The eukaryotic enzyme is involved in the biosynthesis of the mitochondrial phospholipid cardiolipin. It requires divalent cations for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schlame, M. and Hostetler, K.Y. Solubilization, purification, and characterization of cardiolipin synthase from rat liver mitochondria. Demonstration of its phospholipid requirement. J. Biol. Chem. 266 (1991) 22398–22403. [PMID: 1657995]
2.  Nowicki, M., Muller, F. and Frentzen, M. Cardiolipin synthase of Arabidopsis thaliana. FEBS Lett. 579 (2005) 2161–2165. [DOI] [PMID: 15811335]
3.  Houtkooper, R.H., Akbari, H., van Lenthe, H., Kulik, W., Wanders, R.J., Frentzen, M. and Vaz, F.M. Identification and characterization of human cardiolipin synthase. FEBS Lett. 580 (2006) 3059–3064. [DOI] [PMID: 16678169]
4.  Sandoval-Calderon, M., Geiger, O., Guan, Z., Barona-Gomez, F. and Sohlenkamp, C. A eukaryote-like cardiolipin synthase is present in Streptomyces coelicolor and in most actinobacteria. J. Biol. Chem. 284 (2009) 17383–17390. [DOI] [PMID: 19439403]
[EC 2.7.8.41 created 2014]
 
 
EC 2.7.8.44     
Accepted name: teichoic acid glycerol-phosphate primase
Reaction: CDP-glycerol + N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = CDP + 4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): Tag primase; CDP-glycerol:glycerophosphate glycerophosphotransferase; tagB (gene name); tarB (gene name)
Systematic name: CDP-glycerol:N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase
Comments: Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls. This enzyme adds the first glycerol unit to the disaccharide linker of the teichoic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bhavsar, A.P., Truant, R. and Brown, E.D. The TagB protein in Bacillus subtilis 168 is an intracellular peripheral membrane protein that can incorporate glycerol phosphate onto a membrane-bound acceptor in vitro. J. Biol. Chem. 280 (2005) 36691–36700. [DOI] [PMID: 16150696]
2.  Ginsberg, C., Zhang, Y.H., Yuan, Y. and Walker, S. In vitro reconstitution of two essential steps in wall teichoic acid biosynthesis. ACS Chem. Biol. 1 (2006) 25–28. [DOI] [PMID: 17163636]
3.  Brown, S., Zhang, Y.H. and Walker, S. A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps. Chem. Biol. 15 (2008) 12–21. [DOI] [PMID: 18215769]
[EC 2.7.8.44 created 2016]
 
 
EC 2.7.8.45     
Accepted name: teichoic acid glycerol-phosphate transferase
Reaction: CDP-glycerol + 4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = CDP + 4-O-di[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): tarF (gene name) (ambiguous); teichoic acid glycerol-phosphate primase
Systematic name: CDP-glycerol:4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase
Comments: Involved in the biosynthesis of teichoic acid linkage units in the cell walls of some bacteria such as Staphylococcus aureus. This enzyme adds a second glycerol unit to the disaccharide linker of the teichoic acid. cf. EC 2.7.8.12, teichoic acid poly(glycerol phosphate) polymerase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brown, S., Zhang, Y.H. and Walker, S. A revised pathway proposed for Staphylococcus aureus wall teichoic acid biosynthesis based on in vitro reconstitution of the intracellular steps. Chem. Biol. 15 (2008) 12–21. [DOI] [PMID: 18215769]
2.  Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101–1110. [DOI] [PMID: 21035733]
[EC 2.7.8.45 created 2017]
 
 
EC 2.7.8.46     
Accepted name: teichoic acid ribitol-phosphate primase
Reaction: CDP-ribitol + 4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = CMP + 4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): Tar primase; tarK (gene name)
Systematic name: CDP-ribitol:4-O-[(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol ribitylphosphotransferase
Comments: Involved in the biosynthesis of teichoic acid linkage units in the cell wall of Bacillus subtilis W23. This enzyme adds the first ribitol unit to the disaccharide linker of the teichoic acid.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101–1110. [DOI] [PMID: 21035733]
[EC 2.7.8.46 created 2017]
 
 
EC 2.7.8.47     
Accepted name: teichoic acid ribitol-phosphate polymerase
Reaction: n CDP-ribitol + 4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-[(1-D-ribitylphospho)n-(1-D-ribitylphospho)-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
Other name(s): Tar polymerase (ambiguous); tarL (gene name) (ambiguous)
Systematic name: CDP-ribitol:4-O-[1-D-ribitylphospho-(2R)-1-glycerophospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol ribitolphosphotransferase
Comments: Involved in the biosynthesis of teichoic acid linkage units in the cell wall of Bacillus subtilis W23. This enzyme adds the 25-35 ribitol units to the linker molecule.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Brown, S., Meredith, T., Swoboda, J. and Walker, S. Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways. Chem. Biol. 17 (2010) 1101–1110. [DOI] [PMID: 21035733]
[EC 2.7.8.47 created 2017]
 
 
EC 2.7.8.48     
Accepted name: ceramide phosphoethanolamine synthase
Reaction: CDP-ethanolamine + a ceramide = a ceramide phosphorylethanolamine + CMP
Other name(s): Cpes (gene name); CPE synthase
Systematic name: CDP-ethanolamine:ceramide phosphoethanolaminyltransferase
Comments: The enzyme, studied from the fly Drosophila melanogaster, has homologues among the invertebrates, but not in other animal phyla. Its product, ceramide phosphoethanolamine, is synthesized as the main sphingolipid in cell membranes of arthropods, such as Drosophila and Musca, and is common in worms, bees, spiders, and scorpions. It has also been reported in deep-sea mussels and some sea snails, as well as protozoans and oomycetes. The enzyme requires a Mn(II) cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Vacaru, A.M., Tafesse, F.G., Ternes, P., Kondylis, V., Hermansson, M., Brouwers, J.F., Somerharju, P., Rabouille, C. and Holthuis, J.C. Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER. J. Cell Biol. 185 (2009) 1013–1027. [DOI] [PMID: 19506037]
2.  Vacaru, A.M., van den Dikkenberg, J., Ternes, P. and Holthuis, J.C. Ceramide phosphoethanolamine biosynthesis in Drosophila is mediated by a unique ethanolamine phosphotransferase in the Golgi lumen. J. Biol. Chem. 288 (2013) 11520–11530. [DOI] [PMID: 23449981]
[EC 2.7.8.48 created 2022]
 
 
EC 3.5.4.30     
Accepted name: dCTP deaminase (dUMP-forming)
Reaction: dCTP + 2 H2O = dUMP + diphosphate + NH3
Systematic name: dCTP aminohydrolase (dUMP-forming)
Comments: Requires Mg2+. Is highly specific for dCTP as substrate as dCMP, CTP, CDP, CMP, cytosine or deoxycytosine are not deaminated. While most bacteria require two enzymes to form dUMP from dCTP (EC 3.5.4.13, dCTP deaminase and EC 3.6.1.23, dUTP diphosphatase), the archaeon Methanocaldococcus jannaschii uses a single enzyme to carry out both functions. This enzyme can also act as a dUTP diphosphatase, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Li, H., Xu, H., Graham, D.E. and White, R.H. The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase. J. Biol. Chem. 278 (2003) 11100–11106. [DOI] [PMID: 12538648]
[EC 3.5.4.30 created 2003]
 
 
EC 3.6.1.6     
Accepted name: nucleoside diphosphate phosphatase
Reaction: a nucleoside diphosphate + H2O = a nucleoside phosphate + phosphate
Other name(s): nucleoside-diphosphatase; thiaminpyrophosphatase; UDPase; inosine diphosphatase; adenosine diphosphatase; IDPase; ADPase; adenosinepyrophosphatase; guanosine diphosphatase; guanosine 5′-diphosphatase; inosine 5′-diphosphatase; uridine diphosphatase; uridine 5′-diphosphatase; type B nucleoside diphosphatase; GDPase; CDPase; nucleoside 5′-diphosphatase; type L nucleoside diphosphatase; NDPase; nucleoside diphosphate phosphohydrolase
Systematic name: nucleoside-diphosphate phosphohydrolase
Comments: The enzyme, which appears to be limited to metazoa, acts on multiple nucleoside diphosphates as well as on D-ribose 5-diphosphate. Specificity depends on species and isoform.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-69-4
References:
1.  Gibson, D.M., Ayengar, P. and Sanadi, D.R. A phosphatase specific for nucleoside diphosphates. Biochim. Biophys. Acta 16 (1955) 536–538. [DOI] [PMID: 14389272]
2.  Horecker, B.L., Hurwitz, J. and Heppel, L.A. The synthesis of ribose 5-pyrophosphate and ribose 5-triphosphate. J. Am. Chem. Soc. 79 (1957) 701–702.
3.  Yeung, G., Mulero, J.J., McGowan, D.W., Bajwa, S.S. and Ford, J.E. CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry 39 (2000) 12916–12923. [DOI] [PMID: 11041856]
4.  Failer, B.U., Braun, N. and Zimmermann, H. Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J. Biol. Chem. 277 (2002) 36978–36986. [DOI] [PMID: 12167635]
5.  Uccelletti, D., O'Callaghan, C., Berninsone, P., Zemtseva, I., Abeijon, C. and Hirschberg, C.B. ire-1-dependent transcriptional up-regulation of a lumenal uridine diphosphatase from Caenorhabditis elegans. J. Biol. Chem. 279 (2004) 27390–27398. [DOI] [PMID: 15102851]
[EC 3.6.1.6 created 1961]
 
 
EC 3.6.1.16     
Accepted name: CDP-glycerol diphosphatase
Reaction: CDP-glycerol + H2O = CMP + sn-glycerol 3-phosphate
Other name(s): CDP-glycerol pyrophosphatase; cytidine diphosphoglycerol pyrophosphatase
Systematic name: CDP-glycerol phosphoglycerohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-28-4
References:
1.  Glaser, L. The synthesis of teichoic acid. IV. On the regulation of cytidine 5′-diphosphateglycerol concentration. Biochim. Biophys. Acta 101 (1965) 6–15. [PMID: 14329291]
[EC 3.6.1.16 created 1972]
 
 
EC 3.6.1.26     
Accepted name: CDP-diacylglycerol diphosphatase
Reaction: CDP-diacylglycerol + H2O = CMP + phosphatidate
Other name(s): cytidine diphosphodiacylglycerol pyrophosphatase; CDP diacylglycerol hydrolase
Systematic name: CDP-diacylglycerol phosphatidylhydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-20-1
References:
1.  Raetz, C.R.H., Hirschberg, B., Dowhan, W., Wickner, W.T. and Kennedy, E.P. A membrane-bound pyrophosphatase in Escherichia coli catalyzing the hydrolysis of cytidine diphosphate-diglyceride. J. Biol. Chem. 247 (1972) 2245–2247. [PMID: 4335869]
[EC 3.6.1.26 created 1976]
 
 
EC 3.6.1.53     
Accepted name: Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase
Reaction: (1) CDP-choline + H2O = CMP + phosphocholine
(2) ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate
Other name(s): Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase; ADPRibase-Mn
Systematic name: CDP-choline phosphohydrolase
Comments: Requires Mn2+. Unlike EC 3.6.1.13, ADP-ribose diphosphatase, it cannot utilize Mg2+. ADP-D-ribose, CDP-choline, CDP-ethanolamine and ADP are substrates for this enzyme but ADP-D-glucose, UDP-D-glucose, CDP-D-glucose, CDP, CMP and AMP are not hydrolysed [2]. The mammalian enzyme hydrolyses cyclic ADP-ribose to 1-(5-phospho-β-D-ribosyl)-AMP with ~100-fold lower efficiency than ADP-D-ribose [3]. In rat, the enzyme is found predominantly in thymus and spleen.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Canales, J., Pinto, R.M., Costas, M.J., Hernández, M.T., Miró, A., Bernet, D., Fernández, A. and Cameselle, J.C. Rat liver nucleoside diphosphosugar or diphosphoalcohol pyrophosphatases different from nucleotide pyrophosphatase or phosphodiesterase I: substrate specificities of Mg2+-and/or Mn2+-dependent hydrolases acting on ADP-ribose. Biochim. Biophys. Acta 1246 (1995) 167–177. [DOI] [PMID: 7819284]
2.  Canales, J., Fernández, A., Ribeiro, J.M., Cabezas, A., Rodrigues, J.R., Cameselle, J.C. and Costas, M.J. Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase: a novel metallophosphoesterase family preferentially expressed in rodent immune cells. Biochem. J. 413 (2008) 103–113. [DOI] [PMID: 18352857]
3.  Canales, J., Fernandez, A., Rodrigues, J.R., Ferreira, R., Ribeiro, J.M., Cabezas, A., Costas, M.J. and Cameselle, J.C. Hydrolysis of the phosphoanhydride linkage of cyclic ADP-ribose by the Mn(2+)-dependent ADP-ribose/CDP-alcohol pyrophosphatase. FEBS Lett. 583 (2009) 1593–1598. [DOI] [PMID: 19379742]
4.  Rodrigues, J.R., Fernandez, A., Canales, J., Cabezas, A., Ribeiro, J.M., Costas, M.J. and Cameselle, J.C. Characterization of Danio rerio Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase, the structural prototype of the ADPRibase-Mn-like protein family. PLoS One 7:e42249 (2012). [DOI] [PMID: 22848751]
[EC 3.6.1.53 created 2008]
 
 
EC 4.2.1.45     
Accepted name: CDP-glucose 4,6-dehydratase
Reaction: CDP-glucose = CDP-4-dehydro-6-deoxy-D-glucose + H2O
For diagram of CDP-abequose, CDP-ascarylose, CDP-paratose and CDP-tyrelose biosynthesis, click here
Other name(s): cytidine diphosphoglucose oxidoreductase; CDP-glucose 4,6-hydro-lyase
Systematic name: CDP-glucose 4,6-hydro-lyase (CDP-4-dehydro-6-deoxy-D-glucose-forming)
Comments: Requires bound NAD+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37259-55-5
References:
1.  Hey, A.E. and Elbein, A.D. Biosynthesis of tyvelose. The purification and properties of cytidine diphosphate D-glucose oxidoreductase. J. Biol. Chem. 241 (1966) 5473–5478. [PMID: 4380946]
2.  Matsuhashi, S., Matsuhashi, M., Brown, J.G. and Strominger, J.L. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. 3. Cytidine diphosphate D-glucose oxidoreductase. J. Biol. Chem. 241 (1966) 4283–4287. [PMID: 4288651]
3.  Melo, A., Elliott, H. and Glaser, L. The mechanism of 6-deoxyhexose synthesis. I. Intramolecular hydrogen transfer catalyzed by deoxythymidine diphosphate D-glucose oxidoreductase. J. Biol. Chem. 243 (1968) 1467–1474. [PMID: 4869560]
[EC 4.2.1.45 created 1972]
 
 
EC 4.6.1.12     
Accepted name: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Reaction: 2-phospho-4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP
For diagram of non-mevalonate terpenoid biosynthesis, click here
Other name(s): MECDP-synthase; 2-phospho-4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol CMP-lyase (cyclizing)
Systematic name: 2-phospho-4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol CMP-lyase (cyclizing; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate-forming)
Comments: The enzyme from Escherichia coli requires Mg2+ or Mn2+. Forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis (for diagram, click here).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 287480-92-6
References:
1.  Herz, S., Wungsintaweekul, J., Schuhr, C.A., Hecht, S., Lüttgen, H., Sagner, S., Fellermeier, M., Eisenreich, W., Zenk, M.H., Bacher, A. and Rohdich, F. Biosynthesis of terpenoids: YgbB protein converts 4-diphosphocytidyl-2C-methyl-D-erithritol 2-phosphate to 2-C-methyl-D-erithritol 2,4-cyclodiphosphate. Proc. Natl. Acad. Sci. USA 97 (2000) 2486–2490. [DOI] [PMID: 10694574]
2.  Takagi, M., Kuzuyama, T., Kaneda, K., Watanabe, H., Dairi, T. and Seto, H. Studies on the nonmevalonate pathway: Formation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate from 2-phospho-4-(cytidine 5′-diphospho)-2-C-methyl-D-erythritol. Tetrahedron Lett. 41 (2000) 3395–3398.
[EC 4.6.1.12 created 2001]
 
 
EC 5.1.3.10     
Accepted name: CDP-paratose 2-epimerase
Reaction: CDP-α-D-paratose = CDP-α-D-tyvelose
For diagram of CDP-abequose, CDP-ascarylose, CDP-paratose and CDP-tyrelose biosynthesis, click here
Glossary: CDP-α-D-tyvelose = CDP-3,6-dideoxy-α-D-mannose = CDP-3,6-dideoxy-α-D-arabino-hexose
CDP-α-D-paratose = CDP-3,6-dideoxy-α-D-glucose = CDP-3,6-dideoxy-α-D-ribo-hexose
Other name(s): CDP-paratose epimerase; cytidine diphosphoabequose epimerase; cytidine diphosphodideoxyglucose epimerase; cytidine diphosphoparatose epimerase; cytidine diphosphate paratose-2-epimerase; CDP-abequose epimerase (incorrect); CDP-D-abequose 2-epimerase (incorrect); CDP-tyvelose 2-epimerase,
Systematic name: CDP-3,6-dideoxy-D-glucose 2-epimerase
Comments: Requires NAD+.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37318-36-8
References:
1.  Matsuhashi, S. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. II. Reversible 2-epimerization of cytidine diphosphate paratose. J. Biol. Chem. 241 (1966) 4275–4282. [PMID: 5924649]
2.  Liu, H.-W. and Thorson, J.S. Pathways and mechanisms in the biogenesis of novel deoxysugars by bacteria. Annu. Rev. Microbiol. 48 (1994) 223–256. [DOI] [PMID: 7826006]
3.  Koropatkin, N.M., Liu, H.W. and Holden, H.M. High resolution x-ray structure of tyvelose epimerase from Salmonella typhi. J. Biol. Chem. 278 (2003) 20874–20881. [DOI] [PMID: 12642575]
[EC 5.1.3.10 created 1972, modified 2005]
 
 
EC 5.5.1.13     
Accepted name: ent-copalyl diphosphate synthase
Reaction: geranylgeranyl diphosphate = ent-copalyl diphosphate
For diagram of biosynthesis of diterpenoids from ent-copalyl diphosphate, click here
Other name(s): ent-kaurene synthase A; ent-kaurene synthetase A; ent-CDP synthase; ent-copalyl-diphosphate lyase (decyclizing)
Systematic name: ent-copalyl-diphosphate lyase (ring-opening)
Comments: Part of a bifunctional enzyme involved in the biosynthesis of kaurene. See also EC 4.2.3.19 (ent-kaurene synthase)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9055-64-5
References:
1.  Fall, R.R., West, C.A. Purification and properties of kaurene synthetase from Fusarium moniliforme. J. Biol. Chem. 246 (1971) 6913–6928. [PMID: 4331199]
2.  Sun, T.P. and Kamiya, Y. The Arabidopsis GA1 locus encodes the cyclase ent-kaurene synthetase A of gibberellin biosynthesis. Plant Cell 6 (1994) 1509–1518. [PMID: 7994182]
3.  Kawaide, H., Imai, R., Sassa, T. and Kamiya, Y. Ent-kaurene synthase from the fungus Phaeosphaeria sp. L487. cDNA isolation, characterization, and bacterial expression of a bifunctional diterpene cyclase in fungal gibberellin biosynthesis. J. Biol. Chem. 272 (1997) 21706–21712. [DOI] [PMID: 9268298]
4.  Toyomasu, T., Kawaide, H., Ishizaki, A., Shinoda, S., Otsuka, M., Mitsuhashi, W. and Sassa, T. Cloning of a full-length cDNA encoding ent-kaurene synthase from Gibberella fujikuroi: functional analysis of a bifunctional diterpene cyclase. Biosci. Biotechnol. Biochem. 64 (2000) 660–664. [DOI] [PMID: 10803977]
[EC 5.5.1.13 created 2002]
 
 


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