PMID: 44525Nov 1, 1979

Evidence for NADH- and NADPH-linked glutamate dehydrogenases in Trypanosoma cruzi epimastigotes

The Journal of protozoology
R D Walter, F Ebert

Abstract

Two glutamate dehydrogenases, NADH-linked (EC 1.2.1.2) and NADPH-linked (EC 1.2.1.4) were isolated from the epimastigote forms of Trypanosoma cruzi and purified. Both enzymes exist as hexamers. The molecular weights of the native NADH-and NADPH-linked glutamate dehydrogenases were estimated to be 360,000 and 265,000, respectively, and those of the subunits to be 58,000 and 43,000, respectively. The isoelectric point of the NADH-linked dehydrogenase is at pH 5.25 and that of the NADPH-linked enzyme at pH 5.1. The activities of both enzymes are regulated by product inhibition. In addition, purine nucleotides were shown to be potent inhibitors of the NADH-linked glutamate dehydrogenase.

References

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Citations

May 3, 1977·Molecular and Cellular Biochemistry·V R Shatilov, W L Kretovich
Jan 1, 1978·The International Journal of Biochemistry·S M JuanJuan J Cazzulo
Feb 19, 1975·Biochimica Et Biophysica Acta·F M VeroneseL Conventi
Nov 1, 1975·Journal of Bacteriology·N SakamotoM A Savageau
Jan 1, 1977·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·Juan J CazzuloE L Segura
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Related Concepts

Enzymes, antithrombotic
Purine Nucleotides
NADH
LXN
Substrate Specificity
Enzymes for Treatment of Wounds and Ulcers
Metabolic Inhibition
Trypanosoma cruzi
NADP
QPCT

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