Reaction: (S)-methylmalonyl-CoA + pyruvate = propanoyl-CoA + oxaloacetate
Other name(s): transcarboxylase; methylmalonyl coenzyme A carboxyltransferase; methylmalonyl-CoA transcarboxylase; oxalacetic transcarboxylase; methylmalonyl-CoA carboxyltransferase; (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase; (S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase [incorrect]
Systematic name: (S)-methylmalonyl-CoA:pyruvate carboxytransferase
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: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9029-86-1
References:
1. Swick, R.W. and Wood, H.G. The role of transcarboxylation in propionic acid fermentation. Proc. Natl. Acad. Sci. USA 46 (1960) 28-41. [PMID: 16590594]
2. Wood, H.G. and 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 (1985) 1-22. [PMID: 3893281]
3. Peikert, C., Seeger, K., Bhat, R.K. and Berger, S. Determination of the binding specificity of the 12S subunit of the transcarboxylase by saturation transfer difference NMR. Org. Biomol. Chem. 2 (2004) 1777-1781. [PMID: 15188046]
4. Kumar Bhat, R. and 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 (2007) 13-26. [PMID: 17134979]
5. Carey, P.R., Sonnichsen, F.D. and Yee, V.C. Transcarboxylase: one of nature's early nanomachines. IUBMB Life 56 (2004) 575-583. [PMID: 15814455]