EC |
3.1.2.30 |
Accepted name: |
(3S)-malyl-CoA thioesterase |
Reaction: |
(S)-malyl-CoA + H2O = (S)-malate + CoA |
Glossary: |
(S)-malate = (2S)-2-hydroxybutanedioate
(S)-malyl-CoA = (3S)-3-carboxy-3-hydroxypropanoyl-CoA |
Other name(s): |
mcl2 (gene name) |
Systematic name: |
(S)-malyl-CoA hydrolase |
Comments: |
Stimulated by Mg2+ or Mn2+. The enzyme has no activity with (2R,3S)-2-methylmalyl-CoA (cf. EC 4.1.3.24, malyl-CoA lyase) or other CoA esters. |
References: |
1. |
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. [PMID: 20047909] |
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[EC 3.1.2.30 created 2014] |
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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 |
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]. |
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. [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. [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. [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. [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. [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) . [PMID: 27920298] |
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[EC 4.1.3.24 created 1972, modified 2014] |
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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 |
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
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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. |
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. [PMID: 18065535] |
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[EC 4.2.1.148 created 2014] |
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