Active-Site Structure of a β-Hydroxylase in Antibiotic Biosynthesis-Reference-Cited by-同舟云学术

Active-Site Structure of a β-Hydroxylase in Antibiotic Biosynthesis

Published:2011-04-20 Issue:18 Volume:133 Page:6938-6941
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Vu Van V.¹,Makris Thomas M.¹,Lipscomb John D.¹,Que Lawrence¹

Affiliation:

1. Department of Chemistry, §Department of Biochemistry, Molecular Biology and Biophysics, and ⊥Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, Minnesota 55455, United States

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja201822v

Reference45 articles.

1. Aminoacyl-S-Enzyme Intermediates in β-Hydroxylations and α,β-Desaturations of Amino Acids in Peptide Antibiotics

2. Ramoplanin (A-16686), a new glycolipodepsipeptide antibiotic. III. Structure elucidation.

3. The biosynthetic gene cluster for the antitumor drug bleomycin from Streptomyces verticillus ATCC15003 supporting functional interactions between nonribosomal peptide synthetases and a polyketide synthase

4. Assembling the glycopeptide antibiotic scaffold: The biosynthesis of from Streptomyces toyocaensis NRRL15009

5. Coumarin formation in novobiocin biosynthesis: β-hydroxylation of the aminoacyl enzyme tyrosyl-S-NovH by a cytochrome P450 NovI

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