Conserved Amino Acid Residues Correlating With Ketoreductase Stereospecificity in Modular Polyketide Synthases | Zendy

Caffrey Patrick | Zendy

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Conserved Amino Acid Residues Correlating With Ketoreductase Stereospecificity in Modular Polyketide Synthases

Author(s) -

Caffrey Patrick

Publication year - 2003

Publication title -

chembiochem

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.05

H-Index - 126

eISSN - 1439-7633

pISSN - 1439-4227

DOI - 10.1002/cbic.200300581

Subject(s) - polyketide , stereospecificity , stereochemistry , chemistry , amino acid residue , biochemistry , amino acid , modular design , computational biology , biology , peptide sequence , biosynthesis , enzyme , catalysis , computer science , operating system , gene

Getting down to specifics : Key amino acid residues were found to correlate with ketoreductase domain stereospecificity in modular polyketide synthases. These residues may allow alcohol stereochemistry (see scheme; ACP, acyl carrier protein) in polyketides to be predicted from ketoreductase sequences. The results also suggest that polyketide synthase dehydratase domains have a preference for 3hydroxyacyl substrates with the same alcohol stereochemistry as the (3 R )‐hydroxyacyl chains used by dehydratases in fatty acid synthases.

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