The Enzyme Database

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EC 1.1.1.59     
Accepted name: 3-hydroxypropionate dehydrogenase
Reaction: 3-hydroxypropanoate + NAD+ = 3-oxopropanoate + NADH + H+
Systematic name: 3-hydroxypropanoate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-59-5
References:
1.  Den, H., Robinson, W.G. and Coon, M.J. Enzymatic conversion of β-hydroxypropionate to malonic semialdehyde. J. Biol. Chem. 234 (1959) 1666–1671. [PMID: 13672942]
[EC 1.1.1.59 created 1965]
 
 
EC 1.1.1.61     
Accepted name: 4-hydroxybutyrate dehydrogenase
Reaction: 4-hydroxybutanoate + NAD+ = succinate semialdehyde + NADH + H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): γ-hydroxybutyrate dehydrogenase
Systematic name: 4-hydroxybutanoate:NAD+ oxidoreductase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9028-60-8
References:
1.  Nirenberg, M.W. and Jakoby, W.B. Enzymatic utilization of γ-hydroxybutyric acid. J. Biol. Chem. 235 (1960) 954–960. [PMID: 14427301]
[EC 1.1.1.61 created 1965]
 
 
EC 1.1.1.157     
Accepted name: 3-hydroxybutyryl-CoA dehydrogenase
Reaction: (S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): β-hydroxybutyryl coenzyme A dehydrogenase; L(+)-3-hydroxybutyryl-CoA dehydrogenase; BHBD; dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate); L-(+)-3-hydroxybutyryl-CoA dehydrogenase; β-hydroxybutyryl-CoA dehydrogenase
Systematic name: (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39319-78-3
References:
1.  Madan, V.K., Hillmer, P. and Gottschalk, G. Purification and properties of NADP-dependent L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 32 (1973) 51–56. [DOI] [PMID: 4405720]
[EC 1.1.1.157 created 1976]
 
 
EC 1.1.1.298     
Accepted name: 3-hydroxypropionate dehydrogenase (NADP+)
Reaction: 3-hydroxypropanoate + NADP+ = malonate semialdehyde + NADPH + H+
For diagram of the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Glossary: 3-hydroxypropanoate = 3-hydroxypropionate
Other name(s): 3-hydroxypropanoate dehydrogenase (NADP+); 3-hydroxypropionate:NADP+ oxidoreductase
Systematic name: 3-hydroxypropanoate:NADP+ oxidoreductase
Comments: Catalyses the reduction of malonate semialdehyde to 3-hydroxypropanoate, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and archaea, respectively [1,2]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the upstream reaction in the pathway, EC 1.2.1.75 [3]. Different from EC 1.1.1.59 [3-hydroxypropionate dehydrogenase (NAD+)] by cofactor preference.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Strauss, G. and Fuchs, G. Enzymes of a novel autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur. J. Biochem. 215 (1993) 633–643. [DOI] [PMID: 8354269]
2.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
3.  Hugler, M., Menendez, C., Schagger, H. and Fuchs, G. Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation. J. Bacteriol. 184 (2002) 2404–2410. [DOI] [PMID: 11948153]
[EC 1.1.1.298 created 2009]
 
 
EC 1.2.1.75     
Accepted name: malonyl-CoA reductase (malonate semialdehyde-forming)
Reaction: malonate semialdehyde + CoA + NADP+ = malonyl-CoA + NADPH + H+
For diagram of the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): NADP-dependent malonyl CoA reductase; malonyl CoA reductase (NADP); malonyl CoA reductase (malonate semialdehyde-forming)
Systematic name: malonate semialdehyde:NADP+ oxidoreductase (malonate semialdehyde-forming)
Comments: Requires Mg2+. Catalyses the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutanoate cycles, autotrophic CO2 fixation pathways found in some green non-sulfur phototrophic bacteria and some thermoacidophilic archaea, respectively [1,2]. The enzyme from Sulfolobus tokodaii has been purified, and found to contain one RNA molecule per two subunits [3]. The enzyme from Chloroflexus aurantiacus is bifunctional, and also catalyses the next reaction in the pathway, EC 1.1.1.298 [3-hydroxypropionate dehydrogenase (NADP+)] [4].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Strauss, G. and Fuchs, G. Enzymes of a novel autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus, the 3-hydroxypropionate cycle. Eur. J. Biochem. 215 (1993) 633–643. [DOI] [PMID: 8354269]
2.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
3.  Alber, B., Olinger, M., Rieder, A., Kockelkorn, D., Jobst, B., Hugler, M. and Fuchs, G. Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp. J. Bacteriol. 188 (2006) 8551–8559. [DOI] [PMID: 17041055]
4.  Hugler, M., Menendez, C., Schagger, H. and Fuchs, G. Malonyl-coenzyme A reductase from Chloroflexus aurantiacus, a key enzyme of the 3-hydroxypropionate cycle for autotrophic CO2 fixation. J. Bacteriol. 184 (2002) 2404–2410. [DOI] [PMID: 11948153]
[EC 1.2.1.75 created 2009]
 
 
EC 1.2.1.76     
Accepted name: succinate-semialdehyde dehydrogenase (acylating)
Reaction: succinate semialdehyde + CoA + NADP+ = succinyl-CoA + NADPH + H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): succinyl-coA reductase; coenzyme-A-dependent succinate-semialdehyde dehydrogenase
Systematic name: succinate semialdehyde:NADP+ oxidoreductase (CoA-acylating)
Comments: Catalyses the NADPH-dependent reduction of succinyl-CoA to succinate semialdehyde. The enzyme has been described in Clostridium kluyveri, where it participates in succinate fermentation [1], and in Metallosphaera sedula, where it participates in the 3-hydroxypropanonate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [2,3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Sohling, B. and Gottschalk, G. Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 212 (1993) 121–127. [DOI] [PMID: 8444151]
2.  Alber, B., Olinger, M., Rieder, A., Kockelkorn, D., Jobst, B., Hugler, M. and Fuchs, G. Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp. J. Bacteriol. 188 (2006) 8551–8559. [DOI] [PMID: 17041055]
3.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
[EC 1.2.1.76 created 2009]
 
 
EC 1.2.7.1     
Accepted name: pyruvate synthase
Reaction: pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): pyruvate oxidoreductase; pyruvate synthetase; pyruvate:ferredoxin oxidoreductase; pyruvic-ferredoxin oxidoreductase; 2-oxobutyrate synthase; α-ketobutyrate-ferredoxin oxidoreductase; 2-ketobutyrate synthase; α-ketobutyrate synthase; 2-oxobutyrate-ferredoxin oxidoreductase; 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propionylating); 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating)
Systematic name: pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9082-51-3
References:
1.  Evans, M.C.W. and Buchanan, B.B. Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA 53 (1965) 1420–1425. [DOI] [PMID: 5217644]
2.  Gehring, U. and Arnon, D.I. Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium. J. Biol. Chem. 247 (1972) 6963–6969. [PMID: 4628267]
3.  Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties of the enzyme. J. Biol. Chem. 246 (1971) 3111–3119. [PMID: 5574389]
4.  Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism. J. Biol. Chem. 246 (1971) 3120–3125. [PMID: 4324891]
5.  Charon, M.-H., Volbeda, A., Chabriere, E., Pieulle, L. and Fontecilla-Camps, J.C. Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase. Curr. Opin. Struct. Biol. 9 (1999) 663–669. [DOI] [PMID: 10607667]
[EC 1.2.7.1 created 1972, modified 2003, modified 2013]
 
 
EC 1.3.1.84     
Accepted name: acrylyl-CoA reductase (NADPH)
Reaction: propanoyl-CoA + NADP+ = acryloyl-CoA + NADPH + H+
For diagram of the 3-hydroxypropanoate cycle, click here, for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here and for diagram of 3-(dimethylsulfonio)propanoate met
Glossary: propanoyl-CoA = propionyl-CoA
acryloyl-CoA = acrylyl-CoA = propenoyl-CoA
Systematic name: propanoyl-CoA:NADP+ oxidoreductase
Comments: Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1]. The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA [2]. Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16. Contains Zn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
2.  Teufel, R., Kung, J.W., Kockelkorn, D., Alber, B.E. and Fuchs, G. 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales. J. Bacteriol. 191 (2009) 4572–4581. [DOI] [PMID: 19429610]
[EC 1.3.1.84 created 2009, modified 2014]
 
 
EC 1.3.99.1      
Deleted entry: succinate dehydrogenase. The activity is included in EC 1.3.5.1, succinate dehydrogenase (quinone).
[EC 1.3.99.1 created 1961, deleted 2014]
 
 
EC 2.3.1.9     
Accepted name: acetyl-CoA C-acetyltransferase
Reaction: 2 acetyl-CoA = CoA + acetoacetyl-CoA (overall reaction)
(1a) acetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine = [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + CoA
(1b) [acetyl-CoA C-acetyltransferase]-S-acetyl-L-cysteine + acetyl-CoA = acetoacetyl-CoA + [acetyl-CoA C-acetyltransferase]-L-cysteine
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here and for diagram of mevalonate biosynthesis, click here
Other name(s): acetoacetyl-CoA thiolase; β-acetoacetyl coenzyme A thiolase; 2-methylacetoacetyl-CoA thiolase [misleading]; 3-oxothiolase; acetyl coenzyme A thiolase; acetyl-CoA acetyltransferase; acetyl-CoA:N-acetyltransferase; thiolase II; type II thiolase
Systematic name: acetyl-CoA:acetyl-CoA C-acetyltransferase
Comments: The enzyme, found in both eukaryotes and prokaryotes, catalyses the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. In the second step the acyl group is transferred to an acetyl-CoA molecule. cf. EC 2.3.1.16, acetyl-CoA C-acyltransferase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-46-7
References:
1.  Lynen, F. and Ochoa, S. Enzymes of fatty acid metabolism. Biochim. Biophys. Acta 12 (1953) 299–314. [DOI] [PMID: 13115439]
2.  Stern, J.R., Drummond, G.I., Coon, M.J. and del Campillo, A. Enzymes of ketone body metabolism. I. Purification of an acetoacetate-synthesizing enzyme from ox liver. J. Biol. Chem. 235 (1960) 313–317. [PMID: 13834445]
[EC 2.3.1.9 created 1961, modified 2019]
 
 
EC 2.7.9.2     
Accepted name: pyruvate, water dikinase
Reaction: ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): phosphoenolpyruvate synthase; pyruvate-water dikinase (phosphorylating); PEP synthetase; phosphoenolpyruvate synthase; phoephoenolpyruvate synthetase; phosphoenolpyruvic synthase; phosphopyruvate synthetase
Systematic name: ATP:pyruvate, water phosphotransferase
Comments: A manganese protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-09-6
References:
1.  Berman, K.M. and Cohn, M. Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions. J. Biol. Chem. 245 (1970) 5309–5318. [PMID: 4319237]
2.  Berman, K.M. and Cohn, M. Phosphoenolpyruvate synthetase. Partial reactions studied with adenosine triphosphate analogues and the inorganic phosphate-H218O exchange reaction. J. Biol. Chem. 245 (1970) 5319–5325. [PMID: 4319238]
3.  Cooper, R.A. and Kornberg, H.L. Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli. Biochim. Biophys. Acta 104 (1965) 618–620. [DOI] [PMID: 5322808]
4.  Cooper, R.A. and Kornberg, H.L. Phosphoenolpyruvate synthetase. Methods Enzymol. 13 (1969) 309–314.
[EC 2.7.9.2 created 1976]
 
 
EC 2.8.3.22     
Accepted name: succinyl-CoA—L-malate CoA-transferase
Reaction: (1) succinyl-CoA + (S)-malate = succinate + (S)-malyl-CoA
(2) succinyl-CoA + (S)-citramalate = succinate + (S)-citramalyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Glossary: (S)-citramalate = (2S)-2-hydroxy-2-methylbutanedioate
(S)-malate = (2S)-2-hydroxybutanedioate
(S)-malyl-CoA = (3S)-3-carboxy-3-hydroxypropanoyl-CoA
Other name(s): SmtAB
Systematic name: succinyl-CoA:(S)-malate CoA-transferase
Comments: The enzyme, purified from the bacterium Chloroflexus aurantiacus, can also accept itaconate as acceptor, with lower efficiency. It is part of the 3-hydroxypropanoate cycle for carbon assimilation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Friedmann, S., Steindorf, A., Alber, B.E. and Fuchs, G. Properties of succinyl-coenzyme A:L-malate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 188 (2006) 2646–2655. [DOI] [PMID: 16547052]
[EC 2.8.3.22 created 2014]
 
 
EC 4.1.1.31     
Accepted name: phosphoenolpyruvate carboxylase
Reaction: phosphate + oxaloacetate = phosphoenolpyruvate + HCO3-
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): phosphopyruvate (phosphate) carboxylase; PEP carboxylase; phosphoenolpyruvic carboxylase; PEPC; PEPCase; phosphate:oxaloacetate carboxy-lyase (phosphorylating)
Systematic name: phosphate:oxaloacetate carboxy-lyase (adding phosphate, phosphoenolpyruvate-forming)
Comments: This enzyme replenishes oxaloacetate in the tricarboxylic acid cycle when operating in the reverse direction. The reaction proceeds in two steps: formation of carboxyphosphate and the enolate form of pyruvate, followed by carboxylation of the enolate and release of phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-77-0
References:
1.  Chen, J.H. and Jones, R.F. Multiple forms of phosphoenolpyruvate carboxylase from Chlamydomonas reeinhardtii. Biochim. Biophys. Acta 214 (1970) 318–325. [DOI] [PMID: 5501374]
2.  Mazelis, M. and Vennesland, B. Carbon dioxide fixation into oxalacetate in higher plants. Plant Physiol. 32 (1957) 591–600. [PMID: 16655053]
3.  Tovar-Mendez, A., Mujica-Jimenez, C. and Munoz-Clares, R.A. Physiological implications of the kinetics of maize leaf phosphoenolpyruvate carboxylase. Plant Physiol. 123 (2000) 149–160. [PMID: 10806233]
[EC 4.1.1.31 created 1961, modified 2011]
 
 
EC 4.1.3.24     
Accepted name: malyl-CoA lyase
Reaction: (1) (S)-malyl-CoA = acetyl-CoA + glyoxylate
(2) (2R,3S)-2-methylmalyl-CoA = propanoyl-CoA + glyoxylate
For diagram of the 3-hydroxypropanoate cycle, click here
Glossary: (S)-malyl-CoA = (3S)-3-carboxy-3-hydroxypropanoyl-CoA
(2R,3S)-2-methylmalyl-CoA = L-erythro-β-methylmalyl-CoA = (2R,3S)-2-methyl-3-carboxy-3-hydroxypropanoyl-CoA
Other name(s): malyl-coenzyme A lyase; (3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase; mclA (gene name); mcl1 (gene name); (3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase (acetyl-CoA-forming); L-malyl-CoA lyase
Systematic name: (S)-malyl-CoA glyoxylate-lyase (acetyl-CoA-forming)
Comments: The enzymes from Rhodobacter species catalyse a step in the ethylmalonyl-CoA pathway for acetate assimilation [3,5]. The enzyme from halophilic bacteria participate in the methylaspartate cycle and catalyse the reaction in the direction of malyl-CoA formation [6]. The enzyme from the bacterium Chloroflexus aurantiacus, which participates in the 3-hydroxypropanoate cycle for carbon assimilation, also has the activity of EC 4.1.3.25, (3S)-citramalyl-CoA lyase [2,4].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 37290-67-8
References:
1.  Tuboi, S. and Kikuchi, G. Enzymic cleavage of malyl-Coenzyme A into acetyl-Coenzyme A and glyoxylic acid. Biochim. Biophys. Acta 96 (1965) 148–153. [DOI] [PMID: 14285256]
2.  Herter, S., Busch, A. and Fuchs, G. L-Malyl-coenzyme A lyase/β-methylmalyl-coenzyme A lyase from Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic CO2 fixation. J. Bacteriol. 184 (2002) 5999–6006. [DOI] [PMID: 12374834]
3.  Meister, M., Saum, S., Alber, B.E. and Fuchs, G. L-Malyl-coenzyme A/β-methylmalyl-coenzyme A lyase is involved in acetate assimilation of the isocitrate lyase-negative bacterium Rhodobacter capsulatus. J. Bacteriol. 187 (2005) 1415–1425. [DOI] [PMID: 15687206]
4.  Friedmann, S., Alber, B.E. and Fuchs, G. Properties of R-citramalyl-coenzyme A lyase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 189 (2007) 2906–2914. [DOI] [PMID: 17259315]
5.  Erb, T.J., Frerichs-Revermann, L., Fuchs, G. and Alber, B.E. The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-malyl-coenzyme A (CoA)/β-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase. J. Bacteriol. 192 (2010) 1249–1258. [DOI] [PMID: 20047909]
6.  Borjian, F., Han, J., Hou, J., Xiang, H., Zarzycki, J. and Berg, I.A. Malate Synthase and β-Methylmalyl Coenzyme A Lyase Reactions in the Methylaspartate Cycle in Haloarcula hispanica. J. Bacteriol. 199 (2017) . [DOI] [PMID: 27920298]
[EC 4.1.3.24 created 1972, modified 2014]
 
 
EC 4.1.3.25     
Accepted name: (S)-citramalyl-CoA lyase
Reaction: (3S)-citramalyl-CoA = acetyl-CoA + pyruvate
For diagram of the 3-hydroxypropanoate cycle, click here
Other name(s): citramalyl coenzyme A lyase (ambiguous); (+)-CMA-CoA lyase; (3S)-citramalyl-CoA pyruvate-lyase; Mcl (ambiguous); citramalyl-CoA lyase (ambiguous)
Systematic name: (3S)-citramalyl-CoA pyruvate-lyase (acetyl-CoA-forming)
Comments: Requires Mg2+ ions for activity [3]. The enzyme from the bacterium Clostridium tetanomorphum is a component of EC 4.1.3.22, citramalate lyase [2]. It also acts on (3S)-citramalyl thioacyl-carrier protein [2]. The enzyme from the bacterium Chloroflexus aurantiacus also has the activity of EC 4.1.3.24, malyl-CoA lyase [3]. It has no activity with (3R)-citramalyl-CoA (cf. EC 4.1.3.46, (R)-citramalyl-CoA lyase) [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37290-68-9
References:
1.  Cooper, R.A. and Kornberg, H.L. The utilization of itaconate by Pseudomonas sp. Biochem. J. 91 (1964) 82–91. [PMID: 4284209]
2.  Dimroth, P., Buckel, W., Loyal, R. and Eggerer, H. Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase. Eur. J. Biochem. 80 (1977) 469–477. [DOI] [PMID: 923590]
3.  Friedmann, S., Alber, B.E. and Fuchs, G. Properties of R-citramalyl-coenzyme A lyase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 189 (2007) 2906–2914. [DOI] [PMID: 17259315]
[EC 4.1.3.25 created 1972, modified 2014]
 
 
EC 4.2.1.116     
Accepted name: 3-hydroxypropionyl-CoA dehydratase
Reaction: 3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O
For diagram of the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Glossary: acryloyl-CoA = acrylyl-CoA
3-hydroxypropanoyl-CoA = 3-hydroxypropionyl-CoA
Other name(s): 3-hydroxypropionyl-CoA hydro-lyase; 3-hydroxypropanoyl-CoA dehydratase
Systematic name: 3-hydroxypropanoyl-CoA hydro-lyase
Comments: Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1]. The enzyme from Metallosphaera sedula acts nearly equally as well on (S)-3-hydroxybutanoyl-CoA but not (R)-3-hydroxybutanoyl-CoA [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
2.  Teufel, R., Kung, J.W., Kockelkorn, D., Alber, B.E. and Fuchs, G. 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales. J. Bacteriol. 191 (2009) 4572–4581. [DOI] [PMID: 19429610]
[EC 4.2.1.116 created 2009]
 
 
EC 4.2.1.120     
Accepted name: 4-hydroxybutanoyl-CoA dehydratase
Reaction: 4-hydroxybutanoyl-CoA = (E)-but-2-enoyl-CoA + H2O
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Glossary: 4-hydroxybutanoyl-CoA = 4-hydroxybutyryl-CoA
(E)-but-2-enoyl-CoA = crotonyl-CoA
Systematic name: 4-hydroxybutanoyl-CoA hydro-lyase
Comments: Contains FAD and a [4Fe-4S] iron-sulfur cluster. The enzyme has been characterized from several microorganisms, including Clostridium kluyveri, where it participates in succinate fermentation [1,2], Clostridium aminobutyricum, where it participates in 4-aminobutyrate degradation [3,4], and Metallosphaera sedula, where it participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Bartsch, R.G. and Barker, H.A. A vinylacetyl isomerase from Clostridium kluyveri. Arch. Biochem. Biophys. 92 (1961) 122–132. [DOI] [PMID: 13687513]
2.  Scherf, U., Sohling, B., Gottschalk, G., Linder, D. and Buckel, W. Succinate-ethanol fermentation in Clostridium kluyveri: purification and characterisation of 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ32-isomerase. Arch. Microbiol. 161 (1994) 239–245. [PMID: 8161284]
3.  Scherf, U. and Buckel, W. Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ32-isomerase from Clostridium aminobutyricum. Eur. J. Biochem. 215 (1993) 421–429. [DOI] [PMID: 8344309]
4.  Muh, U., Cinkaya, I., Albracht, S.P. and Buckel, W. 4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: characterization of FAD and iron-sulfur clusters involved in an overall non-redox reaction. Biochemistry 35 (1996) 11710–11718. [DOI] [PMID: 8794752]
5.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
[EC 4.2.1.120 created 2009]
 
 
EC 4.2.1.148     
Accepted name: 2-methylfumaryl-CoA hydratase
Reaction: (2R,3S)-2-methylmalyl-CoA = 2-methylfumaryl-CoA + H2O
For diagram of the 3-hydroxypropanoate cycle, click here
Glossary: (2R,3S)-2-methylmalyl-CoA = L-erythro-β-methylmalyl-CoA = (2R,3S)-2-methyl-3-carboxy-3-hydroxypropanoyl-CoA
2-methylfumaryl-CoA = (E)-3-carboxy-2-methylprop-2-enoyl-CoA
Other name(s): Mcd; erythro-β-methylmalonyl-CoA hydrolyase; mesaconyl-coenzyme A hydratase (ambiguous); mesaconyl-C1-CoA hydratase
Systematic name: (2R,3S)-2-methylmalyl-CoA hydro-lyase (2-methylfumaryl-CoA-forming)
Comments: The enzyme from the bacterium Chloroflexus aurantiacus is part of the 3-hydroxypropanoate cycle for carbon assimilation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Zarzycki, J., Schlichting, A., Strychalsky, N., Muller, M., Alber, B.E. and Fuchs, G. Mesaconyl-coenzyme A hydratase, a new enzyme of two central carbon metabolic pathways in bacteria. J. Bacteriol. 190 (2008) 1366–1374. [DOI] [PMID: 18065535]
[EC 4.2.1.148 created 2014]
 
 
EC 4.2.1.153     
Accepted name: 3-methylfumaryl-CoA hydratase
Reaction: (S)-citramalyl-CoA = 3-methylfumaryl-CoA + H2O
For diagram of the 3-hydroxypropanoate cycle, click here
Glossary: (S)-citramalyl-CoA = (3S)-3-carboxy-3-hydroxybutanoyl-CoA
3-methylfumaryl-CoA = (E)-3-carboxybut-2-enoyl-CoA
Other name(s): Meh; mesaconyl-C4-CoA hydratase; mesaconyl-coenzyme A hydratase (ambiguous)
Systematic name: (S)-citramalyl-CoA hydro-lyase (3-methylfumaryl-CoA-forming)
Comments: The enzyme from the bacterium Chloroflexus aurantiacus is part of the 3-hydroxypropanoate cycle for carbon assimilation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zarzycki, J., Brecht, V., Muller, M. and Fuchs, G. Identifying the missing steps of the autotrophic 3-hydroxypropionate CO2 fixation cycle in Chloroflexus aurantiacus. Proc. Natl. Acad. Sci. USA 106 (2009) 21317–21322. [DOI] [PMID: 19955419]
[EC 4.2.1.153 created 2014]
 
 
EC 5.1.99.1     
Accepted name: methylmalonyl-CoA epimerase
Reaction: (R)-methylmalonyl-CoA = (S)-methylmalonyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Other name(s): methylmalonyl-CoA racemase; methylmalonyl coenzyme A racemase; DL-methylmalonyl-CoA racemase; 2-methyl-3-oxopropanoyl-CoA 2-epimerase [incorrect]
Systematic name: methylmalonyl-CoA 2-epimerase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-03-7
References:
1.  Mazumder, R., Sasakawa, T., Kaziro, Y. and Ochoa, S. Metabolism of propionic acid in animal tissues. IX. Methylmalonyl coenzyme A racemase. J. Biol. Chem. 237 (1962) 3065–3068. [PMID: 13934211]
2.  Overath, P., Kellerman, G.M., Lynen, F., Fritz, H.P. and Keller, H.J. Zum Mechanismus der Umlagerung von Methylmalonyl-CoA in Succinyl-CoA. II. Versuche zur Wirkungsweise von Methylmalonyl-CoA-Isomerase and Methylmalonyl-CoA-Racemase. Biochem. Z. 335 (1962) 500–518. [PMID: 14482843]
[EC 5.1.99.1 created 1965, modified 1981]
 
 
EC 5.4.1.3     
Accepted name: 2-methylfumaryl-CoA isomerase
Reaction: 2-methylfumaryl-CoA = 3-methylfumaryl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Glossary: 2-methylfumaryl-CoA = (E)-3-carboxy-2-methylprop-2-enoyl-CoA
3-methylfumaryl-CoA = (E)-3-carboxybut-2-enoyl-CoA
Other name(s): mesaconyl-CoA C1-C4 CoA transferase; Mct
Systematic name: 2-methylfumaryl-CoA 1,4-CoA-mutase
Comments: The enzyme, purified from the bacterium Chloroflexus aurantiacus, acts as an intramolecular CoA transferase and does not transfer CoA to free mesaconate. It is part of the 3-hydroxypropanoate cycle for carbon assimilation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Zarzycki, J., Brecht, V., Muller, M. and Fuchs, G. Identifying the missing steps of the autotrophic 3-hydroxypropionate CO2 fixation cycle in Chloroflexus aurantiacus. Proc. Natl. Acad. Sci. USA 106 (2009) 21317–21322. [DOI] [PMID: 19955419]
[EC 5.4.1.3 created 2014]
 
 
EC 5.4.99.2     
Accepted name: methylmalonyl-CoA mutase
Reaction: (R)-methylmalonyl-CoA = succinyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Other name(s): methylmalonyl-CoA CoA-carbonyl mutase; methylmalonyl coenzyme A mutase; methylmalonyl coenzyme A carbonylmutase; (S)-methylmalonyl-CoA mutase; (R)-2-methyl-3-oxopropanoyl-CoA CoA-carbonylmutase [incorrect]
Systematic name: (R)-methylmalonyl-CoA CoA-carbonylmutase
Comments: Requires a cobamide coenzyme.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-90-9
References:
1.  Barker, H.A. Coenzyme B12-dependent mutases causing carbon chain rearrangements. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 6, Academic Press, New York, 1972, pp. 509–537.
[EC 5.4.99.2 created 1961, modified 1983]
 
 
EC 6.2.1.5     
Accepted name: succinate—CoA ligase (ADP-forming)
Reaction: ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): succinyl-CoA synthetase (ADP-forming); succinic thiokinase (ambiguous); succinate thiokinase (ambiguous); succinyl-CoA synthetase (ambiguous); succinyl coenzyme A synthetase (adenosine diphosphate-forming); succinyl coenzyme A synthetase (ambiguous); A-STK (adenin nucleotide-linked succinate thiokinase); STK (ambiguous); A-SCS
Systematic name: succinate:CoA ligase (ADP-forming)
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9080-33-5
References:
1.  Hager, L.P. Succinyl CoA synthetase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 387–399.
2.  Kaufman, S. Studies on the mechanism of the reaction catalyzed by the phosphorylating enzyme. J. Biol. Chem. 216 (1955) 153–164. [PMID: 13252015]
3.  Kaufman, S. and Alivasatos, S.G.A. Purification and properties of the phosphorylating enzyme from spinach. J. Biol. Chem. 216 (1955) 141–152. [PMID: 13252014]
[EC 6.2.1.5 created 1961]
 
 
EC 6.2.1.36     
Accepted name: 3-hydroxypropionyl-CoA synthase
Reaction: 3-hydroxypropanoate + ATP + CoA = 3-hydroxypropanoyl-CoA + AMP + diphosphate
For diagram of the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Glossary: 3-hydroxypropionyl-CoA = 3-hydroxypropanoyl-CoA
Other name(s): 3-hydroxypropionyl-CoA synthetase (AMP-forming); 3-hydroxypropionate—CoA ligase
Systematic name: hydroxypropanoate:CoA ligase (AMP-forming)
Comments: Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1,2].The enzymes from Metallosphaera sedula and Sulfolobus tokodaii can also use propionate, acrylate, acetate, and butanoate as substrates [2], and are thus different from EC 6.2.1.17 (propionate—CoA ligase), which does not accept acetate or butanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
2.  Alber, B.E., Kung, J.W. and Fuchs, G. 3-Hydroxypropionyl-coenzyme A synthetase from Metallosphaera sedula, an enzyme involved in autotrophic CO2 fixation. J. Bacteriol. 190 (2008) 1383–1389. [DOI] [PMID: 18165310]
[EC 6.2.1.36 created 2009]
 
 
EC 6.2.1.40     
Accepted name: 4-hydroxybutyrate—CoA ligase (AMP-forming)
Reaction: ATP + 4-hydroxybutanoate + CoA = AMP + diphosphate + 4-hydroxybutanoyl-CoA
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): 4-hydroxybutyrate-CoA synthetase (ambiguous); 4-hydroxybutyrate:CoA ligase (ambiguous); hbs (gene name); 4-hydroxybutyrate—CoA ligase
Systematic name: 4-hydroxybutanoate:CoA ligase (AMP-forming)
Comments: Isolated from the archaeon Metallosphaera sedula. Involved in the 3-hydroxypropanoate/4-hydroxybutanoate cycle. cf. EC 6.2.1.56, 4-hydroxybutyrate—CoA ligase (ADP-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ramos-Vera, W.H., Weiss, M., Strittmatter, E., Kockelkorn, D. and Fuchs, G. Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota. J. Bacteriol. 193 (2011) 1201–1211. [DOI] [PMID: 21169482]
2.  Hawkins, A.S., Han, Y., Bennett, R.K., Adams, M.W. and Kelly, R.M. Role of 4-hydroxybutyrate-CoA synthetase in the CO2 fixation cycle in thermoacidophilic archaea. J. Biol. Chem. 288 (2013) 4012–4022. [DOI] [PMID: 23258541]
[EC 6.2.1.40 created 2014, modified 2019]
 
 
EC 6.2.1.56     
Accepted name: 4-hydroxybutyrate—CoA ligase (ADP-forming)
Reaction: ATP + 4-hydroxybutanoate + CoA = ADP + phosphate + 4-hydroxybutanoyl-CoA
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): Nmar_0206 (locus name)
Systematic name: 4-hydroxybutanoate:CoA ligase (ADP-forming)
Comments: The enzyme, characterized from the marine ammonia-oxidizing archaeon Nitrosopumilus maritimus, participates in a variant of the 3-hydroxypropanoate/4-hydroxybutanate CO2 fixation cycle. cf. EC 6.2.1.40, 4-hydroxybutyrate—CoA ligase (AMP-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Konneke, M., Schubert, D.M., Brown, P.C., Hugler, M., Standfest, S., Schwander, T., Schada von Borzyskowski, L., Erb, T.J., Stahl, D.A. and Berg, I.A. Ammonia-oxidizing archaea use the most energy-efficient aerobic pathway for CO2 fixation. Proc. Natl. Acad. Sci. USA 111 (2014) 8239–8244. [PMID: 24843170]
[EC 6.2.1.56 created 2019]
 
 
EC 6.4.1.2     
Accepted name: acetyl-CoA carboxylase
Reaction: ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): HFA1 (gene name); ACC1 (gene name); acetyl coenzyme A carboxylase; acetyl-CoA:carbon-dioxide ligase (ADP-forming)
Systematic name: acetyl-CoA:hydrogencarbonate ligase (ADP-forming)
Comments: This enzyme is a multi-domain polypeptide that catalyses three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyses the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. In some organisms these activities are catalysed by separate enzymes (see EC 6.3.4.14, biotin carboxylase, and EC 2.1.3.15, acetyl-CoA carboxytransferase). The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-93-2
References:
1.  Wakil, S.J. A malonic acid derivative as an intermediate in fatty acid synthesis. J. Am. Chem. Soc. 80 (1958) 6465.
2.  Hatch, M.D. and Stumpf, P.K. Fat metabolism in higher plants. XVI. Acetyl coenzyme A carboxylase and acyl coenzyme A-malonyl coenzyme A transcarboxylase from wheat germ. J. Biol. Chem. 236 (1961) 2879–2885. [PMID: 13905314]
3.  Matsuhashi, M., Matsuhashi, S., Numa, S. and Lynen, F. Zur Biosynthese der Fettsäuren. IV Acetyl CoA Carboxylase aus Hefe. Biochem. Z. 340 (1964) 243–262. [PMID: 14317957]
4.  Matsuhashi, M., Matsuhashi, S. and Lynen, F. Zur Biosynthese der Fettsäuren. V. Die Acetyl-CoA Carboxylase aus Rattenleber und ihre Aktivierung durch Citronsäure. Biochem. Z. 340 (1964) 263–289. [PMID: 14317958]
5.  Vagelos, P. Regulation of fatty acid biosynthesis. Curr. Top. Cell. Regul. 4 (1971) 119–166.
6.  Trumble, G.E., Smith, M.A. and Winder, W.W. Purification and characterization of rat skeletal muscle acetyl-CoA carboxylase. Eur. J. Biochem. 231 (1995) 192–198. [DOI] [PMID: 7628470]
7.  Cheng, D., Chu, C.H., Chen, L., Feder, J.N., Mintier, G.A., Wu, Y., Cook, J.W., Harpel, M.R., Locke, G.A., An, Y. and Tamura, J.K. Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes. Protein Expr. Purif. 51 (2007) 11–21. [DOI] [PMID: 16854592]
8.  Kim, K.W., Yamane, H., Zondlo, J., Busby, J. and Wang, M. Expression, purification, and characterization of human acetyl-CoA carboxylase 2. Protein Expr. Purif. 53 (2007) 16–23. [DOI] [PMID: 17223360]
[EC 6.4.1.2 created 1961, modified 2018]
 
 
EC 6.4.1.3     
Accepted name: propionyl-CoA carboxylase
Reaction: ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Other name(s): propionyl coenzyme A carboxylase
Systematic name: propanoyl-CoA:carbon-dioxide ligase (ADP-forming)
Comments: A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses transcarboxylation.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-94-3
References:
1.  Kaziro, Y., Ochoa, S., Warner, R.C. and Chen, J.-Y. Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase. J. Biol. Chem. 236 (1961) 1917–1923. [PMID: 13752080]
2.  Lane, M.D., Halenz, D.R., Kosow, D.P. and Hegre, C.S. Further studies on mitochondrial propionyl carboxylase. J. Biol. Chem. 235 (1960) 3082–3086. [PMID: 13758723]
3.  Meyer, H., Nevaldine, B. and Meyer, F. Acyl-coenzyme A carboxylase of the free-living nematode Turbatrix aceti. 1. Its isolation and molecular characteristics. Biochemistry 17 (1978) 1822–1827. [PMID: 656363]
4.  Moss, J. and Lane, M.D. The biotin-dependent enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 35 (1971) 321–442. [PMID: 4150153]
5.  Vagelos, P. Regulation of fatty acid biosynthesis. Curr. Top. Cell. Regul. 4 (1971) 119–166.
[EC 6.4.1.3 created 1961, modified 1983]
 
 


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