A mechanism for substrate-Induced formation of 6-Hydroxyflavin mononucleotide catalyzed by C30A trimethylamine dehydrogenase-Reference-Cited by-同舟云学术

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A mechanism for substrate-Induced formation of 6-Hydroxyflavin mononucleotide catalyzed by C30A trimethylamine dehydrogenase

Published:2003-11 Issue:22 Volume:13 Page:4129-4132
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Lu Xingliang,Nikolic Dejan,Mitchell Deanna J.,van Breemen Richard B.,Mersfelder John A.,Hille Russ,Silverman Richard B.

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference16 articles.

1. Identification of the iron-sulfur center in trimethylamine dehydrogenase.

2. Structure of the covalently bound coenzyme of trimethylamine dehydrogenase. Evidence for a 6-substituted flavin.

3. Trimethylamine dehydrogenase from a methylotrophic bacterium I. Isolation and steady-state kinetics

4. The natural flavorprotein electron acceptor of trimethylamine dehydrogenase.

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1. Natural Flavins: Occurrence, Role, and Noncanonical Chemistry;Flavin‐Based Catalysis;2021-06-11

2. Total volatile basic nitrogen and trimethylamine in muscle foods: Potential formation pathways and effects on human health;Comprehensive Reviews in Food Science and Food Safety;2021-05-30

3. A Single-Point Mutation in d-Arginine Dehydrogenase Unlocks a Transient Conformational State Resulting in Altered Cofactor Reactivity;Biochemistry;2021-02-25

4. Pleiotropic Impact of a Single Lysine Mutation on Biosynthesis of and Catalysis by N-Methyltryptophan Oxidase;Biochemistry;2011-05-12

5. Flavin-Dependent Enzymes;Comprehensive Natural Products II;2010

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