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Biochemical characterization of a malonyl-specific acyltransferase domain of FK506 biosynthetic polyketide synthase
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نویسنده
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wang y.-y. ,bai l.f. ,ran x.-x. ,jiang x.-h. ,wu h. ,zhang w. ,jin m.-y. ,li y.-q. ,jiang h.
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منبع
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protein and peptide letters - 2015 - دوره : 22 - شماره : 1 - صفحه:2 -7
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چکیده
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Acyltransferases (ats) play an essential role in the polyketide biosynthesis through transferring acyl units into acyl carrier proteins (acps) via a self-acylation reaction and a transacylation reaction. here we used at10fkba of fk506 biosynthetic polyketide synthase (pks) from streptomyces tsukubaensis yn06 as a model to study the specificity of ats for acyl units. our results show that at10fkba can form both malonyl-o-at10fkba and methylmalonyl-o-at10fkba in the self-acylation reaction,however,only malonyl-o-at10fkba but not methylmalonyl-o-at10fkba can transfer the acyl unit into acps in the transacylation reaction. unlike some ats that are known to control the acyl specificity in self-acylation reactions,at10fkba controls the acyl specificity in transacylation reactions. © 2015 bentham science publishers.
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کلیدواژه
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Acyltransferase; FK506; Malonyl-CoA; Methylmalonyl-CoA; Polyketide synthase
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آدرس
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college of life sciences,zhejiang university,hangzhou, China, college of life sciences,zhejiang university,hangzhou, China, college of life sciences,zhejiang university,hangzhou, China, college of life sciences,zhejiang university,hangzhou, China, hangzhou zhongmei huadong pharmaceutical co. ltd,hangzhou, China, hangzhou zhongmei huadong pharmaceutical co. ltd,hangzhou, China, hangzhou zhongmei huadong pharmaceutical co. ltd,hangzhou, China, college of life sciences,zhejiang university,hangzhou,zhejiang,china,key laboratory of microbial biochemistry and metabolism engineering of zhejiang province,hangzhou, China, college of life sciences,zhejiang university,hangzhou,zhejiang,china,key laboratory of microbial biochemistry and metabolism engineering of zhejiang province,hangzhou, China
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Authors
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