Title of article :
The Malonyl Transferase Activity of Type II Polyketide Synthase Acyl Carrier Proteins Original Research Article
Author/Authors :
Christopher J. Arthur، نويسنده , , Anna E. Szafranska، نويسنده , , Jed Long، نويسنده , , Jane Mills، نويسنده , , Russell J. Cox، نويسنده , , Stuart C. Findlow، نويسنده , , Thomas J. Simpson، نويسنده , , Matthew P. Crump، نويسنده , , John Crosby and Matthew P. Crump، نويسنده ,
Issue Information :
ماهنامه با شماره پیاپی سال 2006
Pages :
10
From page :
587
To page :
596
Abstract :
Acyl carrier proteins (ACPs) play a fundamental role in directing intermediates among the enzyme active sites of fatty acid and polyketide synthases (PKSs). In this paper, we demonstrate that the Streptomyces coelicolor (S. coelicolor) actinorhodin (act) PKS ACP can catalyze transfer of malonate to type II S. coelicolor fatty acid synthase (FAS) and other PKS ACPs in vitro. The reciprocal transfer from S. coelicolor FAS ACP to a PKS ACP was not observed. Several mutations in both act ACP and S. coelicolor FAS ACP could be classified by their participation in either donation or acceptance of this malonyl group. These mutations indicated that self-malonylation and malonyl transfer could be completely decoupled, implying that they were separate processes and that a FAS ACP could be converted from a non-malonyl-transferring protein to one with malonyl transferase activity.
Journal title :
Chemistry and Biology
Serial Year :
2006
Journal title :
Chemistry and Biology
Record number :
1159212
Link To Document :
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