EC 2.3.1.39 - [acyl-carrier-protein] S-malonyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.1.39

Names

Accepted name:
[acyl-carrier-protein] S-malonyltransferase
Other names:
[acyl carrier protein]malonyltransferase
malonyl coenzyme A-acyl carrier protein transacylase
malonyl transacylase
malonyl transferase
malonyl-CoA-acyl carrier protein transacylase
MAT
FabD
malonyl-CoA:acyl carrier protein transacylase
malonyl-CoA:ACP transacylase
MCAT
malonyl-CoA:AcpM transacylase
acyl carrier protein malonyltransferase
malonyl-CoA:[acyl-carrier-protein] S-malonyltransferase
malonyl-CoA:ACP-SH transacylase
malonyl-CoA:acyl-carrier-protein transacylase
malonyl-CoA/dephospho-CoA acyltransferase
MdcH
Systematic name:
malonyl-CoA:[acyl-carrier protein] S-malonyltransferase

Reaction

Comments:

This enzyme, along with EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, is essential for the initiation of fatty-acid biosynthesis in bacteria. This enzyme also provides the malonyl groups for polyketide biosynthesis [7]. The product of the reaction, malonyl-ACP, is an elongation substrate in fatty-acid biosynthesis. In Mycobacterium tuberculosis, holo-ACP (the product of EC 2.7.8.7, holo-[acyl-carrier-protein] synthase) is the preferred substrate [5]. This enzyme also forms part of the multienzyme complexes EC 4.1.1.88 (biotin-independent malonate decarboxylase) and EC 4.1.1.89 (biotin-dependent malonate decarboxylase). Malonylation of ACP is immediately followed by decarboxylation within the malonate-decarboxylase complex to yield acetyl-ACP, the catalytically active species of the decarboxylase [12]. In the enzyme from Klebsiella pneumoniae, methylmalonyl-CoA can also act as a substrate but acetyl-CoA cannot [10] whereas the enzyme from Pseudomonas putida can use both as substrates [11]. The ACP subunit found in fatty-acid biosynthesis contains a pantetheine-4'-phosphate prosthetic group; that from malonate decarboxylase also contains pantetheine-4'-phosphate but in the form of a 2'-(5-triphosphoribosyl)-3'-dephospho-CoA prosthetic group.

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:0016419 , GO:0004314
CAS Registry Number: 37257-17-3
UniProtKB/Swiss-Prot: (43) [show] [UniProt]

References

  1. Alberts, A.W., Majerus, P.W. and Vagelos, P.R.
    Acetyl-CoA acyl carrier protein transacylase.
    Methods Enzymol. 14: 50-53 (1969).
  2. Prescott, D.J. and Vagelos, P.R.
    Acyl carrier protein.
    Adv. Enzymol. Relat. Areas Mol. Biol. 36: 269-311 (1972). [PMID: 4561013]
  3. Williamson, I.P. and Wakil, S.J.
    Studies on the mechanism of fatty acid synthesis. XVII. Preparation and general properties of acetyl coenzyme A and malonyl coenzyme A-acyl carrier protein transacylases.
    J. Biol. Chem. 241: 2326-2332 (1966). [PMID: 5330116]
  4. Joshi, V.C. and Wakil, S.J.
    Studies on the mechanism of fatty acid synthesis. XXVI. Purification and properties of malonyl-coenzyme A--acyl carrier protein transacylase of Escherichia coli.
    Arch. Biochem. Biophys. 143: 493-505 (1971). [PMID: 4934182]
  5. Kremer, L., Nampoothiri, K.M., Lesjean, S., Dover, L.G., Graham, S., Betts, J., Brennan, P.J., Minnikin, D.E., Locht, C. and Besra, G.S.
    Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA:AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II.
    J. Biol. Chem. 276: 27967-27974 (2001). [PMID: 11373295]
  6. Keatinge-Clay, A.T., Shelat, A.A., Savage, D.F., Tsai, S.-C., Miercke, L.J.W., O'Connell, J.D., 3rd, Khosla, C. and Stroud, R.M.
    Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase.
    Structure 11: 147-154 (2003). [PMID: 12575934]
  7. Szafranska, A.E., Hitchman, T.S., Cox, R.J., Crosby, J. and Simpson, T.J.
    Kinetic and mechanistic analysis of the malonyl CoA:ACP transacylase from Streptomyces coelicolor indicates a single catalytically competent serine nucleophile at the active site.
    Biochemistry 41: 1421-1427 (2002). [PMID: 11814333]
  8. Hoenke, S., Schmid, M. and Dimroth, P.
    Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli.
    Eur. J. Biochem. 246: 530-538 (1997). [PMID: 9208947]
  9. Koo, J.H. and Kim, Y.S.
    Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus.
    Eur. J. Biochem. 266: 683-690 (1999). [PMID: 10561613]
  10. Hoenke, S. and Dimroth, P.
    Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzyme
    Eur. J. Biochem. 259: 181-187 (1999). [PMID: 9914491]
  11. Hoenke, S. and Dimroth, P.
    Erratum report: Formation of catalytically active acetyl-S-malonate decarboxylase requires malonyl-coenzyme A:acyl carrier protein transacylase as auxiliary enzyme
    Eur. J. Biochem. 259: 259 (1999).
  12. Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y.
    Malonate decarboxylase of Pseudomonas putida is composed of five subunits.
    FEMS Microbiol. Lett. 169: 37-43 (1998). [PMID: 9851033]
  13. Dimroth, P. and Hilbi, H.
    Enzymic and genetic basis for bacterial growth on malonate.
    Mol. Microbiol. 25: 3-10 (1997). [PMID: 11902724]

[EC 2.3.1.39 created 1972, modified 2006, modified 2008]