Biosynthesis of dicarboxylic acids by carbon dioxide fixation. II. Further study of the properties of the "malic" enzyme of pigeon liver.

نویسندگان

  • J B VEIGA SALLES
  • S OCHOA
چکیده

This enzyme is provisionally referred to as “malic” enzyme. The present paper deals with further observations on the kinetics and other properties of the purified enzyme.’ The enzyme is totally inactive in the absence of Mn++. Mg++ can replace Mn++ but is less effective. Further evidence has been obtained indicating that free oxalacetate is not an intermediate in Reaction 1 and that both Reactions 1 and 2 are catalyzed by one and the same enzyme. Additional evidence has also been obtained showing that the dismutation between malate and pyruvate (2,3), represented by Reaction 3, is catalyzed

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منابع مشابه

Biosynthesis of dicarboxylic acids by carbon dioxide fixation; isolation and properties of an enzyme from pigeon liver catalyzing the reversible oxidative decarboxylation of 1-malic acid.

followed spectrophotometrically. The spectrophotometric method could not be applied to the determination of the equilibrium constant of Reaction 1 owing to interference by lactic dehydrogenase which contaminated the best preparations of the pigeon liver enzyme available (1). However, through coupling with the isocitric dehydrogenase system (Reaction 2), Reaction 3 was obtained (3). The equilibr...

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Biosynthesis of dicarboxylic acids by carbon dioxide fixation. IV. Isolation and properties of an adaptive "malic" enzyme from Lactobacillus arabinosus.

Reaction 1 requires DPN and manganous ions. It is specific for Imalic acid; d-malic acid is inactive. TPN cannot replace DPN. Reaction 2 requires the presence of manganous ions. The evidence presented below supports the view that Reaction 1 is a DPN-linked dismutation between Z-malate and pyruvate, resulting from the interaction of lactic dehydrogenase with a DPN-specific “malic” enzyme as show...

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Biosynthesis of dicarboxylic acids by carbon dioxide fixation. III. Enzymatic synthesis of iota-malic acid by reductive carboxylation of pyruvic acid.

A complete chemical balance which demonstrates the occurrence of Reaction 3 has now been obtained. There is no reaction in the absence of either TPN, .Zwischenferment, or “malic” enzyme. The rate of reaction is proportional to the concentration of “malic” enzyme and to the CO* tension. It is also possible to couple the isocitric dehydrogenase-oxalosuccinic carboxylase system (2) with “malic” en...

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Interrelationships of oxalacetic and l-malic acids in carbon dioxide fixation.

Reaction 1 requires TPN,’ as shown, while the incorporation of COZ into oxalacetate during Reaction 2 is catalyzed by ATP in pigeon liver extracts (4, 5), although not in bacterial preparations (6). The relationship between the two reactions has been obscure, although some information is available. It has been reported that ATP has no effect on Reaction 1 (1) and that TPN cannot replace ATP in ...

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Carbon dioxide fixation in the brain.

Upon intracarotid administration of ammonia to cats, there is a significant increase of cerebral glutamine without a corresponding decrease in the level of cerebral glutamic acid (3). Similar observations in dogs have been reported by others (4). Since the supply of glutamic acid from the circulating blood is insufficient for the formation of the additional amount of glutamine, the dicarboxylic...

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 187 2  شماره 

صفحات  -

تاریخ انتشار 1950