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


Two glutamate dehydrogenases, NADH-linked (EC and NADPH-linked (EC 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.


Apr 1, 1994·Journal of Bioenergetics and Biomembranes·Juan J Cazzulo
Jan 1, 1981·Transactions of the Royal Society of Tropical Medicine and Hygiene·W E Gutteridge
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Related Concepts

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

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