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Theory of the process of amino-acid metabolism, catalysed by pyridoxal enzymes.
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This article is published in Biokhimiya.The article was published on 1953-01-01 and is currently open access. It has received 106 citations till now. The article focuses on the topics: Pyridoxal.read more
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An appreciation of Professor Alexander E. Braunstein. The discovery and scope of enzymatic transamination.
Arthur J.L. Cooper,Alton Meister +1 more
TL;DR: This review outlines the events leading to the discovery of enzymatic transamination, how the discovery was made, the findings that led to the recognition by the mid-1950s of the very wide scope and biological importance of aminotransferase reactions, and the elucidation of the primary amino acid sequence and three-dimensional structure of aspartate aminotsferases.
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Catalytic function of a histidyl residue in cytosolic aspartate aminotransferase-catalyzed reactions.
TL;DR: Results indicates that the histidyl residue does not function as a base abstracting the α-hydrogen atom of these substrates but acts as a catalytic residue involved in the interaction with the distal carboxylate of a natural dicarboxylic substrate as proposed previously.
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The L-cysteine desulfhydrase of Escherichia coli.
M. A. Metaxas,E. A. Delwiche +1 more
TL;DR: The present communication describes the isolation and characterization of an L-cysteine desulfhydrase from a strain of E. coli and achievesvirtually complete resolution for pyridoxal-phosphate.
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Design, Synthesis and Anti-tuberculosis Activity of Hydrazones and N-acylhydrazones Containing Vitamin B6 and Different Heteroaromatic Nucleus
Thais Cristina Mendonça Nogueira,Lucas dos Santos Cruz,Cristina Lourenço,Marcus V. N. de Souza +3 more
TL;DR: In this paper, a series of hydrazones 1a-g and N-acylhydrazones 2a-f containing vitamin B6 have been synthesized from commercial pyridoxal hydrochloride and the appropriate aromatic or heteroaromatic hydrazine or NacylHydrazine.
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The pyridoxal-phosphate-dependent enzymes exclusively catalyzing reactions of β-replacement
TL;DR: It appears highly improbable that transient formation of an alphabeta-unsaturated, coenzyme-substrate imine, considered as an obligatory step in the action of lyases in the alphabeta -eliminating and other subgroups, should occur in the sequences of reaction intermediates in the case of beta-replacing lyases.