The mechanism of action of ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. Evidence that the hydrogen transfer mechanism involves a second intermediate hydrogen carrier in addition to the cofactor.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Ethanolamine Deaminase, a Cobamide Coenzyme-dependent Enzyme
2. The Mechanism of Action of Ethanolamine Ammonia-Lyase, a B12-dependent Enzyme
3. The Substrate-Dependent Steric Course of the Ethanolamine Ammonia-Lyase Reaction
4. The mechanism of action of ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. Studies with isopropanolamine, a true substrate.
5. Interaction of N-substituted ethanolamine analogs with ethanolamine ammonia-lyase, an adenosylcobalamin-requiring enzyme.
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1. The ammonia-lyases: enzymes that use a wide range of approaches to catalyze the same type of reaction;Critical Reviews in Biochemistry and Molecular Biology;2019-11-02
2. Crystal Structures of Ethanolamine Ammonia-lyase Complexed with Coenzyme B12 Analogs and Substrates;Journal of Biological Chemistry;2010-08
3. A Mechanistic Overview of B12-dependent Processes;Vitamin B12and B12-Proteins;2007-12-21
4. L-Aspartase: New Tricks from an Old Enzyme;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
5. Computational Study on Mechanistic Details of the Aminoethanol Rearrangement Catalyzed by the Vitamin B12-Dependent Ethanolamine Ammonia Lyase: His and Asp/Glu Acting Simultaneously as Catalytic Auxiliaries;The Journal of Organic Chemistry;2003-08-12
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