Emergence of oxygen‐ and pyridoxal phosphate‐dependent reactions
نویسندگان
چکیده
منابع مشابه
Oxygen-sensitive Reactions of Proteins and Peptides
In the previous paper (l), an oxygen-sensitive thermochromic system was described which involved reactions of anoxic liquid ammonia at 25” with peptides and proteins containing fully combined cystine. Few proteins are very soluble in liquid ammonia, and the question arose whether the reaction in such instances went to completion, the blue color produced representing the reaction product of all ...
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The geometry about oxygen in the transition-state structures for oxygen transfers from a nitrone to phosphorous, from a percarboxylic acid to a carbon–carbon double bond, and from an N-sulfonyl oxaziridine to a carbon–carbon double bond have been evaluated by the endocyclic restriction test. The former can proceed at an oblique angle, while the latter two require a large angle between the enter...
متن کاملCarbon 13 NMR study of nonenzymatic reactions of pyridoxal 5'-phosphate with selected amino acids and of related reactions.
Carbon 13 nuclear magnetic resonance spectroscopy has been used to monitor the nonenzymatic reactions of pyridoxal 5'-phosphate with glycine, alanine, valine, serine, and with several other model compounds. Isotopically enriched amino acids were employed so that low concentrations could be utilized while still allowing relatively rapid acquisition of spectral data. The results for alanine and s...
متن کاملEmergence of pyridoxal phosphorylation through a promiscuous ancestor during the evolution of hydroxymethyl pyrimidine kinases.
In the family of ATP-dependent vitamin kinases, several bifunctional enzymes that phosphorylate hydroxymethyl pyrimidine (HMP) and pyridoxal (PL) have been described besides enzymes specific towards HMP. To determine how bifunctionality emerged, we reconstructed the sequence of three ancestors of HMP kinases, experimentally resurrected, and assayed the enzymatic activity of their last common an...
متن کاملDual role of oxygen during lipoxygenase reactions.
Studying the oxygenation kinetics of (19R/S,5Z,8Z,11Z,14Z)-19-hydroxyeicosa-5,8,11,14-tetraenoic acid (19-OH-AA) by rabbit 15-lipoxygenase-1 we observed a pronounced oxygen dependence of the reaction rate, which was not apparent with arachidonic acid as substrate. Moreover, we found that peroxide-dependent activation of the lipoxygenase depended strongly on the oxygen concentration. These data ...
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ژورنال
عنوان ژورنال: The FEBS Journal
سال: 2020
ISSN: 1742-464X,1742-4658
DOI: 10.1111/febs.15277