Mechanistic Studies on Tryptophan Lyase (NosL): Identification of Cyanide as a Reaction Product
Author:
Affiliation:
1. Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States
Funder
Welch Foundation
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.7b09000
Reference20 articles.
1. Radical-mediated enzymatic carbon chain fragmentation-recombination
2. Radical S-Adenosylmethionine (SAM) Enzymes in Cofactor Biosynthesis: A Treasure Trove of Complex Organic Radical Rearrangement Reactions
3. Crystal Structure of Tryptophan Lyase (NosL): Evidence for Radical Formation at the Amino Group of Tryptophan
4. Tryptophan Lyase (NosL): Mechanistic Insights from Substrate Analogues and Mutagenesis
5. Substrate-Tuned Catalysis of the RadicalS-Adenosyl-L-Methionine Enzyme NosL Involved in Nosiheptide Biosynthesis
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