KEGG   ENZYME: 2.3.1.111Help
Entry
EC 2.3.1.111                Enzyme                                 

Name
mycocerosate synthase;
mas (gene name);
mycocerosic acid synthase;
acyl-CoA:methylmalonyl-CoA C-acyltransferase (decarboxylating, oxoacyl- and enoyl-reducing);
long-chain acyl-CoA:methylmalonyl-CoA C-acyltransferase (mycocerosate-forming)
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy
Sysname
long-chain acyl-[mycocerosic acid synthase]:methylmalonyl-CoA C-acyltransferase (mycocerosate-forming)
Reaction(IUBMB)
(1) a long-chain acyl-[mycocerosic acid synthase] + 3 methylmalonyl-CoA + 6 NADPH + 6 H+ = a trimethylated-mycocerosoyl-[mycocerosate synthase] + 3 CoA + 3 CO2 + 6 NADP+ + 3 H2O;
(2) a long-chain acyl-[mycocerosic acid synthase] + 4 methylmalonyl-CoA + 8 NADPH + 8 H+ = a tetramethylated-mycocerosoyl-[mycocerosate synthase] + 4 CoA + 4 CO2 + 8 NADP+ + 4 H2O
Reaction(KEGG)
(other) R05189 R11450
Show
Substrate
long-chain acyl-[mycocerosic acid synthase];
methylmalonyl-CoA [CPD:C02557];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Product
trimethylated-mycocerosoyl-[mycocerosate synthase];
CoA [CPD:C00010];
CO2 [CPD:C00011];
NADP+ [CPD:C00006];
H2O [CPD:C00001];
tetramethylated-mycocerosoyl-[mycocerosate synthase]
Comment
The enzyme, characterized from mycobacteria, is loaded with a long-chain acyl moiety by EC 6.2.1.49, 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.
History
EC 2.3.1.111 created 1989, modified 2016, modified 2017
Orthology
K11628  
mycocerosic acid synthase
Genes
MTU: 
Rv2940c(mas)
MTV: 
MTC: 
MT3010(mas-2)
MRA: 
MTF: 
MTB: 
MTK: 
MTZ: 
MTG: 
MTE: 
MTUR: 
MTL: 
MTO: 
MTD: 
MTN: 
MTJ: 
MTUB: 
MTUE: 
MTX: 
MTUL: 
MTUT: 
MTUU: 
MTQ: 
MBO: 
Mb2965c(mas)
MBB: 
MBT: 
MBM: 
MBK: 
MBX: 
MBZ: 
MAF: 
MCE: 
MCQ: 
MCV: 
MCX: 
MCZ: 
MMIC: 
MLE: 
ML0139(mas)
MLB: 
MUL: 
MMI: 
MMAE: 
MLI: 
MKN: 
MKS: 
MKI: 
MHAD: 
SLE: 
sle_14460(sle_14460)
KPHY: 
 » show all
Taxonomy
Reference
1  [PMID:3880746]
  Authors
Rainwater DL, Kolattukudy PE.
  Title
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.
  Journal
J. Biol. Chem. 260 (1985) 616-23.
  Sequence
[mbo:Mb2965c]
Reference
2  [PMID:1527058]
  Authors
Mathur M, Kolattukudy PE
  Title
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.
  Journal
J. Biol. Chem. 267 (1992) 19388-95.
  Sequence
[mbo:Mb2965c]
Reference
3  [PMID:15749014]
  Authors
Trivedi OA, Arora P, Vats A, Ansari MZ, Tickoo R, Sridharan V, Mohanty D, Gokhale RS
  Title
Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid.
  Journal
Mol. Cell. 17 (2005) 631-43.
Reference
4  [PMID:24831705]
  Authors
Menendez-Bravo S, Comba S, Sabatini M, Arabolaza A, Gramajo H
  Title
Expanding the chemical diversity of natural esters by engineering a polyketide-derived pathway into Escherichia coli.
  Journal
Metab. Eng. 24 (2014) 97-106.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
95229-19-9

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