The Enzyme Database

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EC 1.1.1.8     
Accepted name: glycerol-3-phosphate dehydrogenase (NAD+)
Reaction: sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): α-glycerol phosphate dehydrogenase (NAD+); α-glycerophosphate dehydrogenase (NAD+); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrogenase (NAD+); glycerophosphate dehydrogenase (NAD+); hydroglycerophosphate dehydrogenase; L-α-glycerol phosphate dehydrogenase; L-α-glycerophosphate dehydrogenase; L-glycerol phosphate dehydrogenase; L-glycerophosphate dehydrogenase (ambiguous); NAD+-α-glycerophosphate dehydrogenase; NAD+-dependent glycerol phosphate dehydrogenase; NAD+-dependent glycerol-3-phosphate dehydrogenase; NAD+-L-glycerol-3-phosphate dehydrogenase; NAD+-linked glycerol 3-phosphate dehydrogenase; NADH-dihydroxyacetone phosphate reductase; glycerol-3-phosphate dehydrogenase (NAD+); L-glycerol-3-phosphate dehydrogenase (ambiguous)
Systematic name: sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase
Comments: Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9075-65-4
References:
1.  Baranowski, T. α-Glycerophosphate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 85–96.
2.  Brosemer, R.W. and Kuhn, R.W. Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenases. Biochemistry 8 (1969) 2095–2105. [PMID: 4307630]
3.  O'Brien, S.J. and MacIntyre, R.J. The α-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Biochem. Genet. 7 (1972) 141–161. [PMID: 4340553]
4.  Warkentin, K.L. and Fondy, T.P. Isolation and characterization of cytoplasmic L-glycerol-3-phosphate dehydrogenase from rabbit-renal-adipose tissue and its comparison with the skeletal-muscle enzyme. Eur. J. Biochem. 36 (1973) 97–109. [DOI] [PMID: 4200180]
5.  Albertyn, J., van Tonder, A. and Prior, B.A. Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae. FEBS Lett. 308 (1992) 130–132. [DOI] [PMID: 1499720]
6.  Koekemoer, T.C., Litthauer, D. and Oelofsen, W. Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase. Int. J. Biochem. Cell Biol. 27 (1995) 625–632. [DOI] [PMID: 7671141]
[EC 1.1.1.8 created 1961, modified 2005]
 
 
EC 1.1.1.94     
Accepted name: glycerol-3-phosphate dehydrogenase [NAD(P)+]
Reaction: sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): L-glycerol-3-phosphate:NAD(P) oxidoreductase; glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); glycerol 3-phosphate dehydrogenase (NADP); glycerol-3-phosphate dehydrogenase [NAD(P)]
Systematic name: sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase
Comments: The enzyme from Escherichia coli shows specificity for the B side of NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-30-9
References:
1.  Kito, M. and Pizer, L.I. Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli. J. Biol. Chem. 244 (1969) 3316–3323. [PMID: 4389388]
2.  Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. J. Biol. Chem. 253 (1978) 6348–6353. [PMID: 355254]
3.  Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. Kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. J. Biol. Chem. 253 (1978) 6354–6363. [PMID: 28326]
4.  Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol-3-phosphate, a precursor of phospholipid. Further kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. J. Biol. Chem. 255 (1980) 3492–3497. [PMID: 6767719]
[EC 1.1.1.94 created 1972, modified 2005]
 
 
EC 1.1.1.101     
Accepted name: acylglycerone-phosphate reductase
Reaction: 1-palmitoylglycerol 3-phosphate + NADP+ = palmitoylglycerone phosphate + NADPH + H+
Other name(s): palmitoyldihydroxyacetone-phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase; palmitoyl-dihydroxyacetone-phosphate reductase; acyldihydroxyacetone phosphate reductase; palmitoyl dihydroxyacetone phosphate reductase
Systematic name: 1-palmitoylglycerol-3-phosphate:NADP+ oxidoreductase
Comments: Also acts on alkylglycerone 3-phosphate and alkylglycerol 3-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-35-4
References:
1.  LaBelle, E.F., Jr. and Hajira, A.K. Enzymatic reduction of alkyl and acyl derivatives of dihydroxyacetone phosphate by reduced pyridine nucleotides. J. Biol. Chem. 247 (1972) 5825–5834. [PMID: 4403490]
[EC 1.1.1.101 created 1972, modified 1976]
 
 
EC 1.1.1.261     
Accepted name: sn-glycerol-1-phosphate dehydrogenase
Reaction: sn-glycerol 1-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
For diagram of archaetidylserine biosynthesis, click here and for diagram of archaetidylserine biosynthesis, click here
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): glycerol-1-phosphate dehydrogenase [NAD(P)+]; sn-glycerol-1-phosphate:NAD+ oxidoreductase; G-1-P dehydrogenase; Gro1PDH; AraM
Systematic name: sn-glycerol-1-phosphate:NAD(P)+ 2-oxidoreductase
Comments: This enzyme is found primarily as a Zn2+-dependent form in archaea but a Ni2+-dependent form has been found in Gram-positive bacteria [6]. The Zn2+-dependent metalloenzyme is responsible for the formation of archaea-specific sn-glycerol-1-phosphate, the first step in the biosynthesis of polar lipids in archaea. It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes. The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 (phosphoglycerol geranylgeranyltransferase) and EC 2.5.1.42 (geranylgeranylglycerol-phosphate geranylgeranyltransferase), which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 (CDP-archaeol 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 [4]. Activity of the enzyme is stimulated by K+ [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 204594-18-3
References:
1.  Nishihara, M. and Koga, Y. sn-Glycerol-1-phosphate dehydrogenase in Methanobacterium thermoautotrophicum: key enzyme in biosynthesis of the enantiomeric glycerophosphate backbone of ether phospholipids of archaebacteria. J. Biochem. 117 (1995) 933–935. [PMID: 8586635]
2.  Nishihara, M. and Koga, Y. Purification and properties of sn-glycerol-1-phosphate dehydrogenase from Methanobacterium thermoautotrophicum: characterization of the biosynthetic enzyme for the enantiomeric glycerophosphate backbone of ether polar lipids of Archaea. J. Biochem. 122 (1997) 572–576. [PMID: 9348086]
3.  Koga, Y., Kyuragi, T., Nishihara, M. and Sone, N. Did archaeal and bacterial cells arise independently from noncellular precursors? A hypothesis stating that the advent of membrane phospholipid with enantiomeric glycerophosphate backbones caused the separation of the two lines of descent. J. Mol. Evol. 46 (1998) 54–63. [PMID: 9419225]
4.  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]
5.  Han, J.S. and Ishikawa, K. Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1. Archaea 1 (2005) 311–317. [PMID: 15876564]
6.  Guldan, H., Sterner, R. and Babinger, P. Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis. Biochemistry 47 (2008) 7376–7384. [DOI] [PMID: 18558723]
[EC 1.1.1.261 created 2000, modified 2009]
 
 
EC 1.1.1.408     
Accepted name: 4-phospho-D-threonate 3-dehydrogenase
Reaction: 4-phospho-D-threonate + NAD+ = glycerone phosphate + CO2 + NADH + H+ (overall reaction)
(1a) 4-phospho-D-threonate + NAD+ = 3-dehydro-4-phospho-D-erythronate + NADH + H+
(1b) 3-dehydro-4-phospho-D-erythronate = glycerone phosphate + CO2 (spontaneous)
For diagram of erythronate and threonate catabolism, click here
Glossary: D-threonate = (2S,3R)-2,3,4-trihydroxybutanoate
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): pdxA2 (gene name) (ambiguous)
Systematic name: 4-phospho-D-threonate:NAD+ 3-oxidoreductase
Comments: The enzyme, characterized from bacteria, is involved in a pathway for D-threonate catabolism.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl. Acad. Sci. USA 113 (2016) E4161–E4169. [DOI] [PMID: 27402745]
[EC 1.1.1.408 created 2017]
 
 
EC 1.1.1.409     
Accepted name: 4-phospho-D-erythronate 3-dehydrogenase
Reaction: 4-phospho-D-erythronate + NAD+ = glycerone phosphate + CO2 + NADH + H+ (overall reaction)
(1a) 4-phospho-D-erythronate + NAD+ = 3-dehydro-4-phospho-L-threonate + NADH + H+
(1b) 3-dehydro-4-phospho-L-threonate = glycerone phosphate + CO2 (spontaneous)
For diagram of erythronate and threonate catabolism, click here
Glossary: D-erythronate = (2R,3R)-2,3,4-trihydroxybutanoate
Other name(s): pdxA2 (gene name) (ambiguous)
Systematic name: 4-phospho-D-erythronate:NAD+ 3-oxidoreductase
Comments: The enzyme, characterized from bacteria, is involved in a pathway for D-erythronate catabolism.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl. Acad. Sci. USA 113 (2016) E4161–E4169. [DOI] [PMID: 27402745]
[EC 1.1.1.409 created 2017]
 
 
EC 1.1.3.21     
Accepted name: glycerol-3-phosphate oxidase
Reaction: sn-glycerol 3-phosphate + O2 = glycerone phosphate + H2O2
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-α-glycerophosphate oxidase; α-glycerophosphate oxidase; L-α-glycerol-3-phosphate oxidase
Systematic name: sn-glycerol-3-phosphate:oxygen 2-oxidoreductase
Comments: A flavoprotein (FAD).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9046-28-0
References:
1.  Gancedo, C., Gancedo, J.M. and Sols, A. Glycerol metabolism in yeasts. Pathways of utilization and production. Eur. J. Biochem. 5 (1968) 165–172. [DOI] [PMID: 5667352]
2.  Koditschek, L.K. and Umbreit, W.W. α-Glycerophosphate oxidase in Streptococcus faecium F 24. J. Bacteriol. 93 (1969) 1063–1068. [PMID: 5788698]
[EC 1.1.3.21 created 1984]
 
 
EC 1.1.5.3     
Accepted name: glycerol-3-phosphate dehydrogenase
Reaction: sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): α-glycerophosphate dehydrogenase; α-glycerophosphate dehydrogenase (acceptor); anaerobic glycerol-3-phosphate dehydrogenase; DL-glycerol 3-phosphate oxidase (misleading); FAD-dependent glycerol-3-phosphate dehydrogenase; FAD-dependent sn-glycerol-3-phosphate dehydrogenase; FAD-GPDH; FAD-linked glycerol 3-phosphate dehydrogenase; FAD-linked L-glycerol-3-phosphate dehydrogenase; flavin-linked glycerol-3-phosphate dehydrogenase; flavoprotein-linked L-glycerol 3-phosphate dehydrogenase; glycerol 3-phosphate cytochrome c reductase (misleading); glycerol phosphate dehydrogenase; glycerol phosphate dehydrogenase (acceptor); glycerol phosphate dehydrogenase (FAD); glycerol-3-phosphate CoQ reductase; glycerol-3-phosphate dehydrogenase (flavin-linked); glycerol-3-phosphate:CoQ reductase; glycerophosphate dehydrogenase; L-3-glycerophosphate-ubiquinone oxidoreductase; L-glycerol-3-phosphate dehydrogenase (ambiguous); L-glycerophosphate dehydrogenase; mGPD; mitochondrial glycerol phosphate dehydrogenase; NAD+-independent glycerol phosphate dehydrogenase; pyridine nucleotide-independent L-glycerol 3-phosphate dehydrogenase; sn-glycerol 3-phosphate oxidase (misleading); sn-glycerol-3-phosphate dehydrogenase; sn-glycerol-3-phosphate:(acceptor) 2-oxidoreductase; sn-glycerol-3-phosphate:acceptor 2-oxidoreductase
Systematic name: sn-glycerol 3-phosphate:quinone oxidoreductase
Comments: This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane [6], while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane [2]. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain [3]. This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix [7,8]. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9 [4]. The enzyme is activated by calcium [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9001-49-4
References:
1.  Ringler, R.L. Studies on the mitochondrial α-glycerophosphate dehydrogenase. II. Extraction and partial purification of the dehydrogenase from pig brain. J. Biol. Chem. 236 (1961) 1192–1198. [PMID: 13741763]
2.  Schryvers, A., Lohmeier, E. and Weiner, J.H. Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli. J. Biol. Chem. 253 (1978) 783–788. [PMID: 340460]
3.  MacDonald, M.J. and Brown, L.J. Calcium activation of mitochondrial glycerol phosphate dehydrogenase restudied. Arch. Biochem. Biophys. 326 (1996) 79–84. [DOI] [PMID: 8579375]
4.  Rauchová, H., Fato, R., Drahota, Z. and Lenaz, G. Steady-state kinetics of reduction of coenzyme Q analogs by glycerol-3-phosphate dehydrogenase in brown adipose tissue mitochondria. Arch. Biochem. Biophys. 344 (1997) 235–241. [DOI] [PMID: 9244403]
5.  Shen, W., Wei, Y., Dauk, M., Zheng, Z. and Zou, J. Identification of a mitochondrial glycerol-3-phosphate dehydrogenase from Arabidopsis thaliana: evidence for a mitochondrial glycerol-3-phosphate shuttle in plants. FEBS Lett. 536 (2003) 92–96. [DOI] [PMID: 12586344]
6.  Walz, A.C., Demel, R.A., de Kruijff, B. and Mutzel, R. Aerobic sn-glycerol-3-phosphate dehydrogenase from Escherichia coli binds to the cytoplasmic membrane through an amphipathic α-helix. Biochem. J. 365 (2002) 471–479. [DOI] [PMID: 11955283]
7.  Ansell, R., Granath, K., Hohmann, S., Thevelein, J.M. and Adler, L. The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation. EMBO J. 16 (1997) 2179–2187. [DOI] [PMID: 9171333]
8.  Larsson, C., Påhlman, I.L., Ansell, R., Rigoulet, M., Adler, L. and Gustafsson, L. The importance of the glycerol 3-phosphate shuttle during aerobic growth of Saccharomyces cerevisiae. Yeast 14 (1998) 347–357. [DOI] [PMID: 9559543]
[EC 1.1.5.3 created 1961 as EC 1.1.2.1, transferred 1965 to EC 1.1.99.5, transferred 2009 to EC 1.1.5.3]
 
 
EC 1.1.99.5      
Transferred entry: glycerol-3-phosphate dehydrogenase. As the acceptor is now known, the enzyme has been transferred to EC 1.1.5.3, glycerol-3-phosphate dehydrogenase.
[EC 1.1.99.5 created 1961 as EC 1.1.2.1, transferred 1965 to EC 1.1.99.5, deleted 2009]
 
 
EC 2.3.1.42     
Accepted name: glycerone-phosphate O-acyltransferase
Reaction: acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): dihydroxyacetone phosphate acyltransferase (ambiguous)
Systematic name: acyl-CoA:glycerone-phosphate O-acyltransferase
Comments: A membrane protein. Uses CoA derivatives of palmitate, stearate and oleate, with highest activity on palmitoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37257-19-5
References:
1.  Ballas, L.M. and Bell, R.M. Topography of glycerolipid synthetic enzymes. Synthesis of phosphatidylserine, phosphatidylinositol and glycerolipid intermediates occurs on the cytoplasmic surface of rat liver microsomal vesicles. Biochim. Biophys. Acta 665 (1981) 586–595. [DOI] [PMID: 6271231]
2.  Declercq, P.E., Haagsman, H.P., Van Veldhoven, P., Debeer, L.J., Van Golde, L.M.G. and Mannaerts, G.P. Rat liver dihydroxyacetone-phosphate acyltransferases and their contribution to glycerolipid synthesis. J. Biol. Chem. 259 (1984) 9064–9075. [PMID: 6746639]
3.  Hajra, A.K. Biosynthesis of acyl dihydroxyacetone phosphate in guinea pig liver mitochondria. J. Biol. Chem. 243 (1968) 3458–3465. [PMID: 5656381]
[EC 2.3.1.42 created 1972]
 
 
EC 2.3.1.245     
Accepted name: 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
Reaction: glycerone phosphate + acetyl-CoA = 3-hydroxy-5-phosphooxypentane-2,4-dione + CoA
Glossary: (4S)-4,5-dihydroxypentane-2,3-dione = autoinducer 2 = AI-2
Other name(s): lsrF (gene name)
Systematic name: acetyl-CoA:glycerone phosphate C-acetyltransferase
Comments: The enzyme participates in a degradation pathway of the bacterial quorum-sensing autoinducer molecule AI-2.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Diaz, Z., Xavier, K.B. and Miller, S.T. The crystal structure of the Escherichia coli autoinducer-2 processing protein LsrF. PLoS One 4:e6820 (2009). [DOI] [PMID: 19714241]
2.  Marques, J.C., Oh, I.K., Ly, D.C., Lamosa, P., Ventura, M.R., Miller, S.T. and Xavier, K.B. LsrF, a coenzyme A-dependent thiolase, catalyzes the terminal step in processing the quorum sensing signal autoinducer-2. Proc. Natl. Acad. Sci. USA 111 (2014) 14235–14240. [DOI] [PMID: 25225400]
[EC 2.3.1.245 created 2015]
 
 
EC 2.3.1.277     
Accepted name: 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate synthase
Reaction: a medium-chain 3-oxoacyl-[acyl-carrier protein] + glycerone phosphate = 2-oxo-3-(phosphooxy)propyl 3-oxoalkanoate + a holo-[acyl-carrier protein]
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): afsA (gene name); scbA (gene name); barX (gene name)
Systematic name: 3-oxoacyl-[acyl-carrier protein]:glycerone phosphate 3-oxonacylltransferase
Comments: The enzyme catalyses the first committed step in the biosynthesis of γ-butyrolactone autoregulators that control secondary metabolism and morphological development in Streptomyces bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Horinouchi, S., Suzuki, H., Nishiyama, M. and Beppu, T. Nucleotide sequence and transcriptional analysis of the Streptomyces griseus gene (afsA) responsible for A-factor biosynthesis. J. Bacteriol. 171 (1989) 1206–1210. [PMID: 2492509]
2.  Kato, J.Y., Funa, N., Watanabe, H., Ohnishi, Y. and Horinouchi, S. Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces. Proc. Natl. Acad. Sci. USA 104 (2007) 2378–2383. [DOI] [PMID: 17277085]
3.  Hsiao, N.H., Soding, J., Linke, D., Lange, C., Hertweck, C., Wohlleben, W. and Takano, E. ScbA from Streptomyces coelicolor A3(2) has homology to fatty acid synthases and is able to synthesize γ-butyrolactones. Microbiology 153 (2007) 1394–1404. [PMID: 17464053]
4.  Lee, Y.J., Kitani, S. and Nihira, T. Null mutation analysis of an afsA-family gene, barX, that is involved in biosynthesis of the γ-butyrolactone autoregulator in Streptomyces virginiae. Microbiology 156 (2010) 206–210. [PMID: 19778967]
[EC 2.3.1.277 created 2018]
 
 
EC 2.5.1.72     
Accepted name: quinolinate synthase
Reaction: glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate
For diagram of quinolinate biosynthesis, click here
Glossary: quinolinate = pyridine-2,3-dicarboxylate
glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): NadA; QS; quinolinate synthetase
Systematic name: glycerone phosphate:iminosuccinate alkyltransferase (cyclizing)
Comments: An iron-sulfur protein that requires a [4Fe-4S] cluster for activity [1]. Quinolinate synthase catalyses the second step in the de novo biosynthesis of NAD+ from aspartate in some bacteria, with EC 1.4.3.16 (L-aspartate oxidase) catalysing the first step and EC 2.4.2.19 [nicotinate-nucleotide diphosphorylase (carboxylating)] the third step. In Escherichia coli, two of the residues that are involved in the [4Fe-4S] cluster binding appear to undergo reversible disulfide-bond formation that regulates the activity of the enzyme [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ollagnier-de Choudens, S., Loiseau, L., Sanakis, Y., Barras, F. and Fontecave, M. Quinolinate synthetase, an iron-sulfur enzyme in NAD biosynthesis. FEBS Lett. 579 (2005) 3737–3743. [DOI] [PMID: 15967443]
2.  Katoh, A., Uenohara, K., Akita, M. and Hashimoto, T. Early steps in the biosynthesis of NAD in Arabidopsis start with aspartate and occur in the plastid. Plant Physiol. 141 (2006) 851–857. [DOI] [PMID: 16698895]
3.  Sakuraba, H., Tsuge, H., Yoneda, K., Katunuma, N. and Ohshima, T. Crystal structure of the NAD biosynthetic enzyme quinolinate synthase. J. Biol. Chem. 280 (2005) 26645–26648. [DOI] [PMID: 15937336]
4.  Rousset, C., Fontecave, M. and Ollagnier de Choudens, S. The [4Fe-4S] cluster of quinolinate synthase from Escherichia coli: Investigation of cluster ligands. FEBS Lett. 582 (2008) 2937–2944. [DOI] [PMID: 18674537]
5.  Saunders, A.H. and Booker, S.J. Regulation of the activity of Escherichia coli quinolinate synthase by reversible disulfide-bond formation. Biochemistry 47 (2008) 8467–8469. [DOI] [PMID: 18651751]
[EC 2.5.1.72 created 2008]
 
 
EC 2.7.1.29     
Accepted name: glycerone kinase
Reaction: ATP + glycerone = ADP + glycerone phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): dihydroxyacetone kinase; acetol kinase; acetol kinase (phosphorylating)
Systematic name: ATP:glycerone phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 57657-66-6
References:
1.  Sellinger, O.Z. and Miller, O.N. Phosphorylation of acetol by homogenates of rat liver. Fed. Proc. 16 (1957) 245–246.
[EC 2.7.1.29 created 1961]
 
 
EC 2.7.1.84     
Accepted name: alkylglycerone kinase
Reaction: ATP + O-alkylglycerone = ADP + O-alkylglycerone phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): alkyldihydroxyacetone kinase (phosphorylating); alkyldihydroxyacetone kinase
Systematic name: ATP:O-alkylglycerone phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52227-80-2
References:
1.  Chae, K., Piantadosi, C. and Snyder, F. Reductase, phosphatase, and kinase activities in the metabolism of alkyldihydroxyacetone phosphate and alkyldihydroxyacetone. J. Biol. Chem. 248 (1973) 6718–6723. [PMID: 4147653]
[EC 2.7.1.84 created 1976]
 
 
EC 2.7.1.121     
Accepted name: phosphoenolpyruvate—glycerone phosphotransferase
Reaction: phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Systematic name: phosphoenolpyruvate:glycerone phosphotransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 91755-81-6
References:
1.  Jin, R.Z. and Lin, E.C.C. An inducible phosphoenolpyruvate: dihydroxyacetone phosphotransferase system in Escherichia coli. J. Gen. Microbiol. 130 (1984) 83–88. [DOI] [PMID: 6368745]
[EC 2.7.1.121 created 1989]
 
 
EC 4.1.1.104     
Accepted name: 3-dehydro-4-phosphotetronate decarboxylase
Reaction: (1) 3-dehydro-4-phospho-L-erythronate = glycerone phosphate + CO2
(2) 3-dehydro-4-phospho-D-erythronate = glycerone phosphate + CO2
For diagram of erythronate and threonate catabolism, click here
Glossary: L-erythronate = (2S,3S)-2,3,4-trihydroxybutanoate
D-erythronate = (2R,3R)-2,3,4-trihydroxybutanoate
Other name(s): otnC (gene name)
Systematic name: 3-dehydro-4-phosphotetronate carboxy-lyase
Comments: The enzyme, characterized from bacteria, is involved in D-erythronate and L-threonate catabolism.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zhang, X., Carter, M.S., Vetting, M.W., San Francisco, B., Zhao, S., Al-Obaidi, N.F., Solbiati, J.O., Thiaville, J.J., de Crecy-Lagard, V., Jacobson, M.P., Almo, S.C. and Gerlt, J.A. Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars. Proc. Natl. Acad. Sci. USA 113 (2016) E4161–E4169. [DOI] [PMID: 27402745]
[EC 4.1.1.104 created 2017]
 
 
EC 4.1.2.2     
Accepted name: ketotetrose-phosphate aldolase
Reaction: erythrulose 1-phosphate = glycerone phosphate + formaldehyde
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): phosphoketotetrose aldolase; erythrulose-1-phosphate synthetase; erythrose-1-phosphate synthase; erythrulose-1-phosphate formaldehyde-lyase
Systematic name: erythrulose-1-phosphate formaldehyde-lyase (glycerone-phosphate-forming)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9024-45-7
References:
1.  Charalampous, F.C. and Mueller, G.C. Synthesis of erythrulose phosphate by a soluble enzyme from rat tissue. J. Biol. Chem. 201 (1953) 161–173. [PMID: 13044785]
[EC 4.1.2.2 created 1961]
 
 
EC 4.1.2.13     
Accepted name: fructose-bisphosphate aldolase
Reaction: D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
For diagram of the pentose phosphate pathway (later stages), click here and for mechanism, click here; for diagrams of the Calvin cycle, click here and glycolysis, click here
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; fructose diphosphate aldolase; diphosphofructose aldolase; fructose 1,6-diphosphate aldolase; ketose 1-phosphate aldolase; phosphofructoaldolase; zymohexase; fructoaldolase; fructose 1-phosphate aldolase; fructose 1-monophosphate aldolase; 1,6-diphosphofructose aldolase; SMALDO; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase
Systematic name: D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Comments: Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-52-6
References:
1.  Horecker, B.L., Tsolas, O. and Lai, C.Y. Aldolases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 7, Academic Press, New York, 1972, pp. 213–258.
2.  Alefounder, P.R., Baldwin, S.A., Perham, R.N., Short, N.J. Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli. Biochem. J. 257 (1989) 529–534. [PMID: 2649077]
[EC 4.1.2.13 created 1965, modified 1999 (EC 4.1.2.7 created 1961, incorporated 1972)]
 
 
EC 4.1.2.17     
Accepted name: L-fuculose-phosphate aldolase
Reaction: L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): L-fuculose 1-phosphate aldolase; fuculose aldolase; L-fuculose-1-phosphate lactaldehyde-lyase
Systematic name: L-fuculose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-54-8
References:
1.  Ghalambor, M.A. and Heath, E.C. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. IV. Purification and properties of cytidine monophosphate 3-deoxy-D-manno-octulosonate synthetase. J. Biol. Chem. 241 (1966) 3216–3221. [PMID: 5330266]
2.  Dreyer, M.K. and Schulz, G.E. The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli. J. Mol. Biol. 231 (1993) 549–553. [DOI] [PMID: 8515438]
3.  Dreyer, M.K. and Schulz, G.E. Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. J. Mol. Biol. 259 (1996) 458–466. [DOI] [PMID: 8676381]
[EC 4.1.2.17 created 1965]
 
 
EC 4.1.2.19     
Accepted name: rhamnulose-1-phosphate aldolase
Reaction: L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
For diagram of L-Rhamnose metabolism, click here
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): rhamnulose phosphate aldolase; L-rhamnulose 1-phosphate aldolase; L-rhamnulose-phosphate aldolase; L-rhamnulose-1-phosphate lactaldehyde-lyase
Systematic name: L-rhamnulose-1-phosphate (S)-lactaldehyde-lyase (glycerone-phosphate-forming)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9054-58-4
References:
1.  Chiu, T.-H. and Feingold, D.S. L-Rhamnulose 1-phosphate aldolase from Escherichia coli. Crystallization and properties. Biochemistry 8 (1969) 98–108. [PMID: 4975916]
2.  Sawada, H. and Takagi, Y. The metabolism of L-rhamnose in Escherichia coli. 3. L-Rhamulose-phosphate aldolase. Biochim. Biophys. Acta 92 (1964) 26–32. [PMID: 14243785]
[EC 4.1.2.19 created 1972]
 
 
EC 4.1.2.29     
Accepted name: 5-dehydro-2-deoxyphosphogluconate aldolase
Reaction: 5-dehydro-2-deoxy-D-gluconate 6-phosphate = glycerone phosphate + malonate semialdehyde
For diagram of inositol catabolism, click here
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): phospho-5-keto-2-deoxygluconate aldolase; 5-dehydro-2-deoxy-D-gluconate-6-phosphate malonate-semialdehyde-lyase
Systematic name: 5-dehydro-2-deoxy-D-gluconate-6-phosphate malonate-semialdehyde-lyase (glycerone-phosphate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-25-6
References:
1.  Anderson, W.A. and Magasanik, B. The pathway of myo-inositol degradation in Aerobacter aerogenes. Conversion of 2-deoxy-5-keto-D-gluconic acid to glycolytic intermediates. J. Biol. Chem. 246 (1971) 5662–5675. [PMID: 4328832]
[EC 4.1.2.29 created 1976]
 
 
EC 4.1.2.40     
Accepted name: tagatose-bisphosphate aldolase
Reaction: D-tagatose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): D-tagatose-1,6-bisphosphate triosephosphate lyase
Systematic name: D-tagatose 1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Comments: Enzyme activity is stimulated by certain divalent cations. It is involved in the tagatose 6-phosphate pathway of lactose catabolism in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39433-95-9
References:
1.  Anderson, R.L., Markwell, J.P. D-Tagatose-1,6-bisphosphate aldolase (Class II) from Klebsiella pneumoniae. Methods Enzymol. 90 (1982) 323–324.
2.  Van Rooijen, R.J., Van Schalkwijk, S., De Vos, W.M. Molecular cloning, characterization, and nucleotide sequence of the tagatose 6-phosphate pathway gene cluster of the lactose operon of Lactococcus lactis. J. Biol. Chem. 266 (1991) 7176–7181. [PMID: 1901863]
[EC 4.1.2.40 created 1999]
 
 
EC 4.1.2.56     
Accepted name: 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate synthase
Reaction: 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate = glycerone phosphate + L-aspartate 4-semialdehyde
For diagram of 3-amino-4-hydroxybenzoate biosynthesis, click here
Other name(s): griI (gene name)
Systematic name: 2-amino-4,5-dihydroxy-6-oxo-7-(phosphooxy)heptanoate L-aspartate 4-semialdehyde-lyase (glycerone phosphate-forming)
Comments: Part of the pathway for the biosynthesis of grixazone, a mixture of yellow pigments produced by the bacterium Streptomyces griseus.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Suzuki, H., Ohnishi, Y., Furusho, Y., Sakuda, S. and Horinouchi, S. Novel benzene ring biosynthesis from C3 and C4 primary metabolites by two enzymes. J. Biol. Chem. 281 (2006) 36944–36951. [DOI] [PMID: 17003031]
[EC 4.1.2.56 created 2014]
 
 
EC 4.1.2.57     
Accepted name: sulfofructosephosphate aldolase
Reaction: 6-deoxy-6-sulfo-D-fructose 1-phosphate = glycerone phosphate + 2-hydroxy-3-oxopropane-1-sulfonate
For diagram of sulphoglycolysis of sulfoquinovose, click here
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
2-hydroxy-3-oxopropane-1-sulfonate = 3-sulfolactaldehyde
Other name(s): yihT (gene name)
Systematic name: 6-deoxy-6-sulfofructose-1-phosphate 2-hydroxy-3-oxopropane-1-sulfonate-lyase (glycerone-phosphate-forming)
Comments: The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Denger, K., Weiss, M., Felux, A.K., Schneider, A., Mayer, C., Spiteller, D., Huhn, T., Cook, A.M. and Schleheck, D. Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle. Nature 507 (2014) 114–117. [DOI] [PMID: 24463506]
[EC 4.1.2.57 created 2014]
 
 
EC 4.2.3.3     
Accepted name: methylglyoxal synthase
Reaction: glycerone phosphate = 2-oxopropanal + phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
2-oxopropanal = methylglyoxal
Other name(s): methylglyoxal synthetase; glycerone-phosphate phospho-lyase
Systematic name: glycerone-phosphate phosphate-lyase (methylglyoxal-forming)
Comments: Does not act on D-glyceraldehyde 3-phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37279-01-9
References:
1.  Cooper, R.A. and Anderson, A. The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli. FEBS Lett. 11 (1970) 273–276. [DOI] [PMID: 11945504]
2.  Hopper, D.J. and Cooper, R.A. The regulation of Escherichia coli methylglyoxal synthase; a new control site in glycolysis? FEBS Lett. 13 (1971) 213–216. [DOI] [PMID: 11945670]
3.  Ray, S. and Ray, M. Isolation of methylglyoxal synthase from goat liver. J. Biol. Chem. 256 (1981) 6230–6233. [PMID: 7240200]
[EC 4.2.3.3 created 1972 as EC 4.2.99.11, transferred 2000 to EC 4.2.3.3]
 
 
EC 5.3.1.1     
Accepted name: triose-phosphate isomerase
Reaction: D-glyceraldehyde 3-phosphate = glycerone phosphate
Glossary: glycerone phosphate = dihydroxyacetone phosphate = 3-hydroxy-2-oxopropyl phosphate
Other name(s): phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase
Systematic name: D-glyceraldehyde-3-phosphate aldose-ketose-isomerase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-78-3
References:
1.  Meyer-Arendt, E., Beisenherz, G. and Bücher, T. Triosephosphate isomerase. Naturwissenschaften 40 (1953) 59.
2.  Meyerhof, O. and Beck, L.V. Triosephosphate isomerase. J. Biol. Chem. 156 (1944) 109–120.
[EC 5.3.1.1 created 1961]
 
 


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