Kinetics of coupled reactions catalyzed by aspartate aminotransferase and glutamate dehydrogenase.

C. Salerno, J. Ovádi, T. Keleti, P. Fasella

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Liver mitochondrial aspartate aminotransferase and glutamate dehydrogenase catalyze following sequence of reactions: see formula in text. In the presence of a slight excess of dehydrogenase, the time course of NADPH oxidation resulting from the overall reaction goes through a lag phase and reaches a linear phase. The slopes of the linear part of this curve is a linear function of transaminase concentration. At high concentration (approximately or equal to 10 microM) of both enzymes the lag phase, as observed after rapid mixing of the two enzymes in a Durrum stopped-flow spectrophotometer, is shorter, than that predicted from the kinetic parameters determined for the separate reactions catalyzed by each enzyme.

Original languageEnglish
Pages (from-to)511-517
Number of pages7
JournalEuropean Journal of Biochemistry
Volume121
Issue number3
Publication statusPublished - Jan 1982

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Glutamate Dehydrogenase
Aspartate Aminotransferases
Kinetics
Mitochondrial Aspartate Aminotransferase
Enzymes
Spectrophotometers
Transaminases
NADP
Kinetic parameters
Liver
Oxidoreductases
Oxidation
aspartate dehydrogenase

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kinetics of coupled reactions catalyzed by aspartate aminotransferase and glutamate dehydrogenase. / Salerno, C.; Ovádi, J.; Keleti, T.; Fasella, P.

In: European Journal of Biochemistry, Vol. 121, No. 3, 01.1982, p. 511-517.

Research output: Contribution to journalArticle

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