Enzymic transformation of L-CYSTEINESULFINIC ACID (cas 1115-65-7)☆

Add time:08/14/2019    Source:sciencedirect.com

1.1. A soluble enzyme preparation, obtained from Proteus vulgaris by ultrasonic disintegration, in the presence of suitable cofactors, catalyzes the rapid oxidation of L-cysteinesulfinic acid. The metabolism of the latter compound is shown to proceed by two simultaneous and competing pathways. In pathway A it is oxidized to cysteic acid and the latter is transaminated with α-ketoglutarate. Pathway B is initiated by transamination of cysteinesulfinate with α-ketoglutarate (or oxaloacetate). The resulting β-sulfinylpyruvic acid is desulfinated to pyruvate and SO3= and the latter is oxidized to SO4=, while α-ketoglutarate is regenerated under the influenceof a TPN-specific glutamic dehydrogenase.2.2. Three new enzymes are described: L-cysteinesulfinic dehydrogenase (the enzyme responsible for the formation of cysteic acid), oxaloacetic-cysteinesulfinic and α-ketoglutaric-cysteinesulfinic transaminases. The properties of the latter are discussed in some detail.3.3. β-Sulfinylpyruvic acid, an analogue of oxaloacetic acid, which has not hitherto been implicated in intermediary metabolism, has been accumulated by transaminase action. This compound is desulfinated to SO3= and pyruvate, under the influence of Mn++, analogously to the β-decarboxylation of oxaloacetic acid by Mn++. The desulfination is a rapid, non-enzymic reaction, as is the oxidation of SO3= to SO4= by Mn++.4.4. The possibility is discussed that enzymes may exist for the desulfination reaction and that the reversal of their action (SO2 fixation into pyruvate) may be a mechanism for the incorporation of inorganic sulfur into organic linkages.5.5. L-Cysteinesulfinic dehydrogenase requires a previously unrecognized, pyridine nucleotide coenzyme.6.6. The applicability of the metabolic scheme to intact bacterial cells and to animal tissues is discussed.

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