tailieunhanh - Báo cáo khoa học: Biochemical characterization of the minimal polyketide synthase domains in the lovastatin nonaketide synthase LovB

The biosynthesis of lovastatin inAspergillus terreusrequires two mega-synthases. The lovastatin nonaketide synthase, LovB, synthesizes the inter-mediate dihydromonacolin L using nine malonyl-coenzyme A molecules, and is a reducing, iterative type I polyketide synthase. | ễFEBS Journal Biochemical characterization of the minimal polyketide synthase domains in the lovastatin nonaketide synthase LovB Suzanne M. Ma and Yi Tang Department of Chemicaland Biomolecular Engineering University of California Los Angeles CA USA Keywords filamentous fungi ketosynthase lovastatin megasynthase polyketide Correspondence Y. Tang Department of Chemicaland Biomolecular Engineering 5531 Boelter Hall 420 Westwood Plaza UCLA Los Angeles CA 90095 USA Fax 1 310 206 4107 Tel 1 310 825 0375 E-mail yitang@ Received 1 March 2007 revised 29 March 2007 accepted 2 April 2007 doi The biosynthesis of lovastatin in Aspergillus terreus requires two megasynthases. The lovastatin nonaketide synthase LovB synthesizes the intermediate dihydromonacolin L using nine malonyl-coenzyme A molecules and is a reducing iterative type I polyketide synthase. The iterative type I poly-ketide synthase is mechanistically different from bacterial type I polyketide synthases and animal fatty acid synthases. We have cloned the minimal polyketide synthase domains of LovB as standalone proteins and assayed their activities and substrate specificities. The didomain proteins ketosyn-thase-malonyl-coenzyme A acyl carrier protein acyltransferase KS-MAT and acyl carrier protein-condensation ACP-CON domain were expressed solubly in Escherichia coli. The monodomains MAT ACP and CON were also obtained as soluble proteins. The MAT domain can be readily labeled by 1 2-14C malonyl-coenzyme A and can transfer the acyl group to both the cognate LovB ACP and heterologous ACPs from bacterial type I and type II polyketide synthases. Using the LovB ACP-CON didomain as an acyl acceptor LovB MAT transferred malonyl and acetyl groups with kcat Km values of min-1 iM-1 and min-1 iM-1 respectively. The LovB MAT domain was able to substitute the Streptomyces coelicolor FabD in supporting product turnover in a bacterial type II minimal poly-ketide synthase .

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