Molecular Rationale for Partitioning between C–H and C–F Bond Activation in Heme-Dependent Tyrosine Hydroxylase
Author:
Affiliation:
1. Department of Chemistry, The University of Texas at San Antonio, One UTSA Circle, Texas 78249, United States
Funder
National Institute of General Medical Sciences
Lutcher Brown Endowment fund
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.1c00175
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1. The genes lmbB1 and lmbB2 of Streptomyces lincolnensis encode enzymes involved in the conversion of l -tyrosine to propylproline during the biosynthesis of the antibiotic lincomycin A
2. Molecular characterization of the lincomycin-production gene cluster of Streptomyces lincolnensis 78-11
3. Biocatalytic Carbon–Hydrogen and Carbon–Fluorine Bond Cleavage through Hydroxylation Promoted by a Histidyl-Ligated Heme Enzyme
4. Sequence analysis of porothramycin biosynthetic gene cluster
5. Benzodiazepine Biosynthesis in Streptomyces refuineus
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