Open AccessJournal Article
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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Journal ArticleDOI
Kinetics and Mechanism of the Condensation of Pyridoxal with Amino Acids
TL;DR: The kinetics and mechanism of the condensation of amino acids with pyridoxal were studied in relation to the amino acid structure, solvent, pH, and temperature and several kinetically discernible reaction steps were revealed.
Journal ArticleDOI
Stereochemistry of reactions of the inhibitor/substrates L- and D-beta-chloroalanine with beta-mercaptoethanol catalysed by L-aspartate aminotransferase and D-amino acid aminotransferase respectively.
TL;DR: Two members of the alpha-family of PLP-dependent enzymes have been shown to catalyse beta-substitution of L- and D-beta-chloroalanine respectively with beta-mercaptoethanol, reactions typical of the beta- family ofPLP- dependent enzymes.
Book ChapterDOI
Hypothalamic control of anterior pituitary hormone secretion--characterized hypothalamic-hypophysiotropic peptides.
Geoffrey F. Grant,Wylie Vale +1 more
TL;DR: The chapter discusses the various identified releasing factors with respect to their effects upon the anterior pituitary, the structure activity relationships of each, and their interrelation with the feedback control exhibited by the peripheral endocrine hormones.
Journal ArticleDOI
Chemical transformations of pyridoxal and pyridoxal 5′-phosphate condensation products with amino acids
TL;DR: In this article, the mechanism of chemical transformations of pyridoxal and pyrinoxal 5′-phosphate condensation products with amino acids is studied by kinetic measurements.
Journal ArticleDOI
Spectroscopic characterization of true enzyme‐substrate intermediates of aspartate aminotransferase trapped at subzero temperatures
Michael Sterk,Heinz Gehring +1 more
TL;DR: The finding that the external aldimine can probably be accumulated in the conversion of the pyridoxal to the pyrsidoxamine form with the natural substrates would confirm the proton abstraction at C alpha to be the rate-limiting step in the tautomerization, although with cysteine sulfinate, the formation of the externalAldimines might contribute to the rate limitation.