A type III polyketide synthase from Rhizobium etli condenses malonyl CoAs to a heptaketide pyrone with unusually high catalytic efficiency.
A novel type III polyketide synthase (RePKS) from Rhizobium etli produced a heptaketide pyrone using acetyl-CoA and six molecules of malonyl-CoA. Its catalytic efficiency (k(cat)/K(m) = 5230 mM(-1) min(-1)) for malonyl CoA was found to be the highest ever reported. Molecular dynamics studies revealed the unique features of RePKS.
Department of Chemical Engineering, Konkuk University, Seoul 143-701, Korea.
Marimuthu
M
Jeya
Tae-Su
TS
Kim
Manish
M
Kumar Tiwari
Jinglin
J
Li
Huimin
H
Zhao
Jung-Kul
JK
Lee
D000105:Acetyl Coenzyme A / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D008316:Malonyl Coenzyme A / Q000737:chemistry / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D048630:Polyketide Synthases / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D011753:Pyrones / Q000737:chemistry / Q000378:metabolism*; D042163:Rhizobium etli / Q000201:enzymology* / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity
D011753:Pyrones; D008316:Malonyl Coenzyme A; D000105:Acetyl Coenzyme A; D048630:Polyketide Synthases