Type II thioesterase restores activity of a NRPS module stalled with an aminoacyl-S-enzyme that cannot be elongated

ChemBioChem

Volumn 5, Issue 9, 2004, Pages 1290-1293

  Yeh, Ellen ^a   Kohli, Rahul M ^a   Bruner, Steven D ^b   Walsh, Christopher T ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b BOSTON COLLEGE   (United States)

Author keywords

Biosynthesis; Natural products; Nonribosomal peptide synthetases; Type II thioeterase

Indexed keywords

AMINO ACID; NATURAL PRODUCT; NONRIBOSOMAL PEPTIDE SYNTHETASE; PEPTIDE; PEPTIDE SYNTHASE; THIOL ESTER HYDROLASE; UNCLASSIFIED DRUG;

ARTICLE; BIOSYNTHESIS; CHEMICAL MODIFICATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME ENGINEERING; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; THIOLATION;

AMINO ACIDS; AMINOHYDROLASES; CYSTEAMINE; FATTY ACID SYNTHETASE COMPLEX; HYDROLYSIS; PEPTIDE SYNTHASES; THIOLESTER HYDROLASES;

EID: 4644278719     PISSN: 14394227     EISSN: None     Source Type: Journal    
DOI: 10.1002/cbic.200400077     Document Type: Article

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