EC - Mycocerosate synthase

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IntEnz Enzyme Nomenclature


Accepted name:
mycocerosate synthase
Other names:
mycocerosic acid synthase
mas (gene name)
acyl-CoA:methylmalonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing)
long-chain acyl-CoA:methylmalonyl-CoA C-acyltransferase (mycocerosate-forming)
Systematic name:
long-chain acyl-[mycocerosic acid synthase]:methylmalonyl-CoA C-acyltransferase (mycocerosate-forming)



The enzyme, characterized from mycobacteria, is loaded with a long-chain acyl moiety by EC, long-chain fatty acid adenylyltransferase FadD28, and elongates it by incorporation of three or four methylmalonyl (but not malonyl) residues, to form tri- or tetramethyl-branched fatty-acids, respectively, such as 2,4,6,8-tetramethyloctacosanoate (C32-mycocerosate). Since the enzyme lacks a thioesterase domain, the product remains bound and requires additional enzyme(s) for removal. Even though the enzyme can accept C6 to C20 substrates in vitro, it prefers to act on C14-C20 substrates in vivo.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00529
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050111
CAS Registry Number: 95229-19-9


  1. Rainwater, D.L. and Kollattukudy, P.E.
    Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA.
    J. Biol. Chem. 260 : 616-623 (1985). [PMID: 3880746]
  2. Mathur, M., Kolattukudy, P. E.
    Molecular cloning and sequencing of the gene for mycocerosic acid synthase, a novel fatty acid elongating multifunctional enzyme, from Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin.
    J. Biol. Chem. 267 : 19388-19395 (1992). [PMID: 1527058]
  3. Trivedi, O. A., Arora, P., Vats, A., Ansari, M. Z., Tickoo, R., Sridharan, V., Mohanty, D., Gokhale, R. S.
    Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid.
    Mol. Cell 17 : 631-643 (2005). [PMID: 15749014]
  4. Menendez-Bravo, S., Comba, S., Sabatini, M., Arabolaza, A., Gramajo, H.
    Expanding the chemical diversity of natural esters by engineering a polyketide-derived pathway into Escherichia coli.
    Metab. Eng. 24 : 97-106 (2014). [PMID: 24831705]

[EC created 1989, modified 2016, modified 2017]