Post-translational modification of polyketide and nonribosomal peptide synthases

The past year has witnessed a major advance in the study of polyketide and nonribosomal peptide biosynthesis with the identification of the phosphopantetheinyl transferase enzyme family, enzymes required to produce active, post-translationally modified polyketide and peptide synthases. Phosphopantet...

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Veröffentlicht in:Current opinion in chemical biology 1997-10, Vol.1 (3), p.309-315
Hauptverfasser: Walsh, Christopher T, Gehring, Amy M, Weinreb, Paul H, Quadri, Luis EN, Flugel, Roger S
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Sprache:eng
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Zusammenfassung:The past year has witnessed a major advance in the study of polyketide and nonribosomal peptide biosynthesis with the identification of the phosphopantetheinyl transferase enzyme family, enzymes required to produce active, post-translationally modified polyketide and peptide synthases. Phosphopantetheinyl transferases required for fatty acid, peptide and siderophore biosynthesis have been characterized and a consensus sequence noted in order to facilitate future identification of additional proteins catalyzing phosphopantetheinyl transfer.
ISSN:1367-5931
1879-0402
DOI:10.1016/S1367-5931(97)80067-1