EC 2.1.3.1 - Methylmalonyl-CoA carboxytransferase

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IntEnz Enzyme Nomenclature
EC 2.1.3.1

Names

Accepted name:
methylmalonyl-CoA carboxytransferase
Other names:
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase
(S)-methylmalonyl-CoA:pyruvate carboxyltransferase
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate [incorrect]
methylmalonyl coenzyme A carboxyltransferase
methylmalonyl-CoA carboxyltransferase
methylmalonyl-CoA transcarboxylase
oxalacetic transcarboxylase
transcarboxylase
Systematic name:
(S)-methylmalonyl-CoA:pyruvate carboxytransferase

Reaction

Cofactors

Comments:

A biotinyl-protein, containing cobalt and zinc. The enzyme, described from the bacterium Propionibacterium shermanii, is unique among the biotin-dependent enzymes in that it catalyses carboxyl transfer between two organic molecules, utilizing two separate carboxyltransferase domains. The enzyme is a very large complex, consisting of a hexameric central core of 12S subunits surrounded by six 5S subunit dimers, each connected to the central core by twelve 1.3S biotin carrier subunits.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00167
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047154
CAS Registry Number: 9029-86-1
UniProtKB/Swiss-Prot:

References

  1. Swick, R.W. and Wood, H.G.
    The role of transcarboxylation in propionic acid fermentation.
    Proc. Natl. Acad. Sci. USA 46 : 28-41 (1960). [PMID: 16590594]
  2. Wood, H. G., Kumar, G. K.
    Transcarboxylase: its quaternary structure and the role of the biotinyl subunit in the assembly of the enzyme and in catalysis.
    Ann N Y Acad Sci 447 : 1-22 (1985). [PMID: 3893281]
  3. Peikert, C., Seeger, K., Bhat, R. K., Berger, S.
    Determination of the binding specificity of the 12S subunit of the transcarboxylase by saturation transfer difference NMR.
    Org Biomol Chem 2 : 1777-1781 (2004). [PMID: 15188046]
  4. Kumar Bhat, R., Berger, S.
    New and easy strategy for cloning, expression, purification, and characterization of the 5S subunit of transcarboxylase from Propionibacterium f. shermanii.
    Prep Biochem Biotechnol 37 : 13-26 (2007). [PMID: 17134979]
  5. Carey, P. R., Sonnichsen, F. D., Yee, V. C.
    Transcarboxylase: one of nature's early nanomachines.
    IUBMB Life 56 : 575-583 (2004). [PMID: 15814455]

[EC 2.1.3.1 created 1961, modified 2004]