EC - Malyl-CoA lyase

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IntEnz Enzyme Nomenclature


Accepted name:
malyl-CoA lyase
Other names:
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)



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, (3S)-citramalyl-CoA lyase [2,4].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050083
CAS Registry Number: 37290-67-8
UniProtKB/Swiss-Prot: (10) [show] [UniProt]


  1. Tuboi, S. and Kikuchi, G.
    Enzymic cleavage of malyl-Coenzyme A into acetyl-Coenzyme A and glyoxylic acid.
    Biochim. Biophys. Acta 96: 148-153 (1965). [PMID: 14285256]
  2. Herter, S., Busch, A., Fuchs, G.
    L-Malyl-coenzyme A lyase/beta-methylmalyl-coenzyme A lyase from Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic CO(2) fixation.
    J. Bacteriol. 184: 5999-6006 (2002). [PMID: 12374834]
  3. Meister, M., Saum, S., Alber, B. E., Fuchs, G.
    L-malyl-coenzyme A/beta-methylmalyl-coenzyme A lyase is involved in acetate assimilation of the isocitrate lyase-negative bacterium Rhodobacter capsulatus.
    J. Bacteriol. 187: 1415-1425 (2005). [PMID: 15687206]
  4. Friedmann, S., Alber, B. E., Fuchs, G.
    Properties of R-citramalyl-coenzyme A lyase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus.
    J. Bacteriol. 189: 2906-2914 (2007). [PMID: 17259315]
  5. Erb, T. J., Frerichs-Revermann, L., Fuchs, G., Alber, B. E.
    The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and (3S)- Malyl-CoA thioesterase.
    J. Bacteriol. 192: 1249-1258 (2010). [PMID: 20047909]
  6. Borjian, F., Han, J., Hou, J., Xiang, H., Zarzycki, J. and Berg, I.A.
    Malate Synthase and beta-Methylmalyl Coenzyme A Lyase Reactions in the Methylaspartate Cycle in Haloarcula hispanica
    J. Bacteriol. 199 (2017). [PMID: 27920298]

[EC created 1972, modified 2014]