Diiron monooxygenases in natural product biosynthesis
Author:
Affiliation:
1. Department of Chemistry
2. University of Minnesota
3. Minneapolis
4. USA
5. Department of Biochemistry, Molecular Biology and Biophysics
Abstract
Two new families of diiron cluster-containing oxygenases serve as tailoring enzymes for NRPS and PKS biosynthetic systems.
Funder
National Institutes of Health
Publisher
Royal Society of Chemistry (RSC)
Subject
Organic Chemistry,Drug Discovery,Biochemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2018/NP/C7NP00061H
Reference76 articles.
1. Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines
2. Assembly-Line Enzymology for Polyketide and Nonribosomal Peptide Antibiotics: Logic, Machinery, and Mechanisms
3. Coumarin formation in novobiocin biosynthesis: β-hydroxylation of the aminoacyl enzyme tyrosyl-S-NovH by a cytochrome P450 NovI
4. An asparagine oxygenase (AsnO) and a 3-hydroxyasparaginyl phosphotransferase (HasP) are involved in the biosynthesis of calcium-dependent lipopeptide antibiotics
5. The Nonribosomal Peptide Synthetase Enzyme DdaD Tethers Nβ-Fumaramoyl-l-2,3-diaminopropionate for Fe(II)/α-Ketoglutarate-Dependent Epoxidation by DdaC during Dapdiamide Antibiotic Biosynthesis
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