Malyl-CoA formation in the NAD-, CoASH-, and alpha-ketoglutarate dehydrogenase-dependent oxidation of 2-keto-4-hydroxyglutarate. Possible coupled role of this reaction with 2-keto-4-hydroxyglutarate aldolase activity in a pyruvate-catalyzed cyclic oxidation of glyoxylate.-Reference-Cited by-同舟云学术

Malyl-CoA formation in the NAD-, CoASH-, and alpha-ketoglutarate dehydrogenase-dependent oxidation of 2-keto-4-hydroxyglutarate. Possible coupled role of this reaction with 2-keto-4-hydroxyglutarate aldolase activity in a pyruvate-catalyzed cyclic oxidation of glyoxylate.

Published:1984-08 Issue:16 Volume:259 Page:10012-10019
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Gupta S C,Dekker E E

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference55 articles.

1. The enzymatic conversion of γ-OH-α-ketoglutarate (HKG) to malate: (A postulated step in the cyclic oxidation of glyoxylate)

2. Evidence for the identity and some comparative properties of alpha-ketoglutarate and 2-keto-4-hydroxyglutarate dehydrogenase activity.

3. [46] 2-keto-4-hydroxyglutarate aldolase from Escherichia coli

4. Steady-state kinetics and inhibition studies of the aldol condensation reaction catalyzed by bovine liver and Escherichia coli 2-keto-4-hydroxyglutarate aldolase

5. [45] 2-Keto-4-hydroxyglutarate aldolase from bovine liver

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