Purification and properties of L-erythro-3,5-diaminohexanoate dehydrogenase from Clostridium sticklandii
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00699a010
Reference12 articles.
1. The gel-filtration behaviour of proteins related to their molecular weights over a wide range
2. Purification and Properties of l-erythro-3,5-Diaminohexanoate Dehydrogenase from a Lysine-fermenting Clostridium
3. Purification and properties of β-lysine mutase, a pyridoxal phosphate and B12 coenzyme dependent enzyme
4. The kinetics of enzyme-catalyzed reactions with two or more substrates or products
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1. Crystal Structures and Catalytic Mechanism of l ‐ erythro ‐3,5‐Diaminohexanoate Dehydrogenase and Rational Engineering for Asymmetric Synthesis of β‐Amino Acids;Angewandte Chemie International Edition;2021-03-24
2. Crystal Structures and Catalytic Mechanism of l ‐ erythro ‐3,5‐Diaminohexanoate Dehydrogenase and Rational Engineering for Asymmetric Synthesis of β‐Amino Acids;Angewandte Chemie;2021-03-24
3. Development of β-Amino Acid Dehydrogenase for the Synthesis of β-Amino Acids via Reductive Amination of β-Keto Acids;ACS Catalysis;2015-03-06
4. Identification of the Last Unknown Genes in the Fermentation Pathway of Lysine;Journal of Biological Chemistry;2007-03
5. The Biochemistry and Enzymology of Amino Acid Dehydrogenases;Critical Reviews in Biochemistry and Molecular Biology;1994-01
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