(Acil-nosilac-protein) S-maloniltransferaza

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(Acil-nosilac-protein) S-maloniltransferaza
EC broj
CAS broj 37257-17-3
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures

(Acil-nosilac-protein) S-maloniltransferaza (EC, (acil nosilac protein)maloniltransferaza, FabD, malonil koenzim A-acil nosilac protein transacilaza, malonilna transacilaza, malonil transferaza, malonil-KoA-acil nosilac protein transacilaza, malonil-KoA:(acil-nosilac-protein) S-maloniltransferaza, malonil-KoA:ACP transacilaza, malonil-KoA:ACP-SH transacilaza, malonil-KoA:AcpM transacilaza, malonil-KoA:acil nosilac protein transacilaza, malonil-KoA:acil-nosilac-protein transacilaza, malonil-KoA/defosfo-KoA aciltransferaza, MAT, MCAT, MdcH) je enzim sa sistematskim imenom malonil-KoA:(acil-nosilac protein) S-maloniltransferaza.[1][2][3][4][5][6][7][8][9][10][11][12] Ovaj enzim katalizuje sledeću hemijsku reakciju

malonil-KoA + [acil-nosilac protein] KoA + malonil-[acil-nosilac protein]

Ovaj enzim, zajedno sa EC, [acil-nosilac-protein] S-acetiltransferazom, je esencijalan za inicijaciju biosinteze masnih kiselina kod bakterija.


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  2. Prescott, D.J. and Vagelos, P.R. (1972). „Acyl carrier protein”. Adv. Enzymol. Relat. Areas Mol. Biol. 36: 269—311. PMID 4561013. 
  3. Williamson, I.P. and Wakil, S.J. (1966). „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. PMID 5330116. 
  4. Joshi, V.C. and Wakil, S.J. (1971). „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. 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. (2001). „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. PMID 11373295. 
  6. Keatinge-Clay, A.T., Shelat, A.A., Savage, D.F., Tsai, S.C., Miercke, L.J., O'Connell, J.D., 3rd, Khosla, C. and Stroud, R.M. (2003). „Catalysis, specificity, and ACP docking site of Streptomyces coelicolor malonyl-CoA:ACP transacylase”. Structure. 11: 147—154. PMID 12575934. 
  7. Szafranska, A.E., Hitchman, T.S., Cox, R.J., Crosby, J. and Simpson, T.J. (2002). „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. PMID 11814333. 
  8. Hoenke, S., Schmid, M. and Dimroth, P. (1997). „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. PMID 9208947. 
  9. Koo, J.H. and Kim, Y.S. (1999). „Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus”. Eur. J. Biochem. 266: 683—690. PMID 10561613. 
  10. Hoenke, S. and Dimroth, P. (1999). „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. PMID 9914491. 
  11. Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y. (1998). „Malonate decarboxylase of Pseudomonas putida is composed of five subunits”. FEMS Microbiol. Lett. 169: 37—43. PMID 9851033. 
  12. Dimroth, P. and Hilbi, H. (1997). „Enzymic and genetic basis for bacterial growth on malonate”. Mol. Microbiol. 25: 3—10. PMID 11902724. 


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