Kinetics of suicide substrates
- 1 March 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 185 (3), 771-773
- https://doi.org/10.1042/bj1850771
Abstract
When suicide substrates inactivate enzymes during catalysis, formation of product and inactivation of enzyme proceed concurrently. The steady-state hypothesis is applicable when catalytic quantities of enzyme are used. Equations for the rate of inactivation have been derived and integrated to obtain equations describing progress curves.This publication has 7 references indexed in Scilit:
- β-Elimination of β-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of a key intermediate in the reactionBiochemistry, 1978
- Suicide substrates for the alanine racemase of Escherichia coli BBiochemistry, 1978
- Estimation of Michaelis constant and maximum velocity from the direct linear plotBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- [45] Suicide substrates for flavoprotein enzymesMethods in Enzymology, 1978
- [3] Mechanism-based irreversible enzyme inhibitorsMethods in Enzymology, 1977
- The substrate analog, bromopyruvate, as both a substrate and alkylating agent for 2-keto-3-deoxy-6-phosphogluconic aldolase. Kinetic and stereochemical studies.1972
- Mode of inhibition of beta-hydroxydecanoyl thioester dehydrase by 3-decynoyl-N-acetylcysteamine.1970