PMID: 3754770Jun 23, 1986Paper

Inhibition of aspartate aminotransferase by D-hydrazinosuccinate: comparison with L-hydrazinosuccinate

Biochimica Et Biophysica Acta
R H YamadaT Hasegawa

Abstract

L-Hydrazinosuccinate has been reported to be a slow- and tight-binding inhibitor of aspartate aminotransferase (L-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) and to interact with the enzyme via a reaction of two consecutive steps. The present work examined the effects of D-hydrazinosuccinate on the same enzyme for comparison. D-Hydrazinosuccinate showed a potent inhibition in a slow-binding manner: transamination became slower with time when the reaction was initiated by the addition of enzyme to a mixture of the assay components and D-hydrazinosuccinate, while the reaction was initially very slow and became faster with time when the enzyme was preincubated with the inhibitor before the initiation of reaction. Analysis of the time-course of interaction of the enzyme with D-hydrazinosuccinate suggested a reversible single-step reaction mechanism and gave an inhibition constant of approx. 3 nM, in contrast to the two-step mechanism, and a much lower inhibition constant of 0.2 nM for L-hydrazinosuccinate. Comparison of the rate constants for the reaction steps in the interaction of the enzyme with D- and L-enantiomers confirmed that the difference in the reaction mechanism was mainly responsible for the stronger inhibi...Continue Reading

References

Jan 1, 1979·Methods in Enzymology·J W Williams, J F Morrison
Sep 20, 1985·Biochimica Et Biophysica Acta·R H YamadaT Hasegawa
Aug 24, 1970·Biochemical and Biophysical Research Communications·N Feliss, M Martinez-Carrion
Sep 7, 1984·Biochimica Et Biophysica Acta·R H YamadaT Hasegawa

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Citations

May 1, 1995·Bioorganic & Medicinal Chemistry·E S LightcapR B Silverman
Feb 25, 1987·Biochimica Et Biophysica Acta·R YamadaT Hasegawa

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