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] |
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|
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] |
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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] |
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[EC 1.1.1.157 created 1976] |
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|
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] |
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[EC 1.1.1.298 created 2009] |
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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] |
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|
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] |
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[EC 1.2.1.76 created 2009] |
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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] |
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[EC 1.2.7.1 created 1972, modified 2003, modified 2013] |
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|
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] |
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[EC 1.3.1.84 created 2009, modified 2014] |
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EC
|
1.3.99.1
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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] |
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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] |
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[EC 2.3.1.9 created 1961, modified 2019] |
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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. |
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[EC 2.7.9.2 created 1976] |
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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] |
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[EC 2.8.3.22 created 2014] |
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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] |
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[EC 4.1.1.31 created 1961, modified 2011] |
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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] |
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|
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] |
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[EC 4.1.3.25 created 1972, modified 2014] |
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|
|
|
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] |
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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 Δ3-Δ2-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 Δ3-Δ2-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] |
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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] |
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[EC 4.2.1.148 created 2014] |
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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] |
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[EC 4.2.1.153 created 2014] |
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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] |
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[EC 5.1.99.1 created 1965, modified 1981] |
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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] |
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[EC 5.4.1.3 created 2014] |
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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. |
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[EC 5.4.99.2 created 1961, modified 1983] |
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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] |
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[EC 6.2.1.5 created 1961] |
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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] |
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[EC 6.2.1.36 created 2009] |
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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] |
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[EC 6.2.1.40 created 2014, modified 2019] |
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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] |
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[EC 6.2.1.56 created 2019] |
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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] |
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[EC 6.4.1.2 created 1961, modified 2018] |
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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. |
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[EC 6.4.1.3 created 1961, modified 1983] |
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