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Literature DB >> 7387634

Kinetics of suicide substrates.

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.

Mesh：

Substances：
Enzyme Inhibitors

Year: 1980 PMID： 7387634 PMCID： PMC1161457 DOI： 10.1042/bj1850771

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

7 in total

1. Mechanism-based irreversible enzyme inhibitors.

Authors: R R Rando
Journal: Methods Enzymol Date: 1977 Impact factor: 1.600

2. Suicide substrates for the alanine racemase of Escherichia coli B.

Authors: E Wang; C Walsh
Journal: Biochemistry Date: 1978-04-04 Impact factor: 3.162

3. The substrate analog, bromopyruvate, as both a substrate and alkylating agent for 2-keto-3-deoxy-6-phosphogluconic aldolase. Kinetic and stereochemical studies.

Authors: H P Meloche; M A Luczak; J M Wurster
Journal: J Biol Chem Date: 1972-07-10 Impact factor: 5.157

4. Mode of inhibition of beta-hydroxydecanoyl thioester dehydrase by 3-decynoyl-N-acetylcysteamine.

Authors: K Endo; G M Helmkamp; K Bloch
Journal: J Biol Chem Date: 1970-09-10 Impact factor: 5.157

5. beta-elimination of beta-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of a key intermediate in the reaction.

Authors: T S Soper; J M Manning
Journal: Biochemistry Date: 1978-08-08 Impact factor: 3.162

6. Suicide substrates for flavoprotein enzymes.

Authors: C Walsh; T Cromartie; P Marcotte; R Spencer
Journal: Methods Enzymol Date: 1978 Impact factor: 1.600

7. Estimation of Michaelis constant and maximum velocity from the direct linear plot.

Authors: A Cornish-Bowden; R Eisenthal
Journal: Biochim Biophys Acta Date: 1978-03-14

7 in total

32 in total

1. A novel approach to distinguish between enzyme mechanisms: quasi-steady-state kinetic analysis of the prostaglandin H synthase peroxidase reaction.

Authors: Peter V Vrzheshch; Elena A Batanova; Alevtina T Mevkh; Sergei D Varfolomeev; Irina G Gazaryan; Roger N F Thorneley
Journal: Biochem J Date: 2003-06-15 Impact factor: 3.857

2. The kinetics of substrate-induced inactivation.

Authors: S G Waley
Journal: Biochem J Date: 1991-10-01 Impact factor: 3.857

3. The average enzyme principle.

Authors: Ed Reznik; Osman Chaudhary; Daniel Segrè
Journal: FEBS Lett Date: 2013-07-23 Impact factor: 4.124

4. Ribozymes: analytical solution of the one-substrate, two-intermediate reversible scheme for enzyme reactions.

Authors: Paolo Toti; Ludovico Sbordone; Carolina Sbordone; Carlo Bauer
Journal: J Biol Phys Date: 2007-01-27 Impact factor: 1.365

Review 5. The anomalous kinetics of sulphatase A.

Authors: A B Roy; T J Mantle
Journal: Biochem J Date: 1989-08-01 Impact factor: 3.857

6. Inhibition of class C beta-lactamases by (1'R,6R)-6-(1'-hydroxy)benzylpenicillanic acid SS-dioxide.

Authors: G C Knight; S G Waley
Journal: Biochem J Date: 1985-01-15 Impact factor: 3.857

7. A kinetic study of the suicide inactivation of an enzyme measured through coupling reactions. Application to the suicide inactivation of tyrosinase.

Authors: J Escribano; J Tudela; F Garcia-Carmona; F Garcia-Canovas
Journal: Biochem J Date: 1989-09-01 Impact factor: 3.857