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Transient inactivation of almond mandelonitrile lyase by 3-methyleneoxindole: a photooxidation product of the natural plant hormone indole-3-acetic acid.
TLDR
It is determined that MOI is a competitive inhibitor of MNL with a Ki of 23 +/- 3 microM under steady-state turnover conditions, in reasonable agreement with the value obtained from the inactivation data. Expand
A Spectrophotometric Assay for α-Ketoaldehydes Using Horse Liver Alcohol Dehydrogenase
Abstract α-Ketoaldehydes have been extensively employed as reagents for the chemical modification of arginine residues in proteins, and to probe for putative anion recognition sites. A majorExpand
A spectrophotometric assay for alpha-ketoaldehydes using horse liver alcohol dehydrogenase.
TLDR
It is discovered that phenylglyoxal and several related alpha-ketoaldehydes are good substrates for horse liver alcohol dehydrogenase (HLADH), and the enzymatic reduction reaction is stoichiometric with the oxidation of NADH, resulting in a rapid, convenient, and sensitive method for the spectrophotometric quantitation of alpha- ketoaldeHydes. Expand
Equilibrium constants for the formation of glyoxylate thiohemiacetals and kinetic constants for their oxidation by O2 catalyzed by l-hydroxy acid oxidase☆
Abstract Glyoxylate thiohemiacetal formation constants (defined as the concentration of thiohemiacetal divided by the concentration of thiol and the total concentration of hydrated and unhydratedExpand
Isomerization of (R)- and (S)-glutathiolactaldehydes by glyoxalase I: the case for dichotomous stereochemical behavior in a single active site.
TLDR
Glutathiohydroxyacetone was found to be a good competitive inhibitor of the normal glyoxalase I reaction, suggesting that the slow processing rate of these compounds with respect to the normal thiohemiacetals is not due to poor binding. Expand
Peroxisomal Oxidases and Their Probable Role in Controlling Animal Metabolism
TLDR
It has been found that the S-oxalyl derivatives of biological thiols (glutathione and coenzyme A) inhibit metabolically important enzymes (including phosphorylase phosphatase, malic enzyme and succinyl-CoA transferase) when present at physiological concentrations. Expand
THIOL‐GLYOXYLATE ADDUCTS AS SUBSTRATES FOR RAT KIDNEY L‐α‐HYDROXY ACID OXIDASE *
Peroxisomes are small organelles that characteristically contain catalase and several oxidative enzymes, including the flavoprotein oxidases, L-a-hydroxy acid oxidase (L-HAO) and D-aminO acid oxidaseExpand
Thiol-glyoxylate adducts as substrates for rat kidney L-α-hydroxy acid oxidase
Abstract Rat kidney L-α-hydroxy acid oxidase (EC 1.1.3.15) catalyzes a rapid O2 uptake at pH 7.5 when both glyoxylate and one of a number of various thiols are present. Thiols which are reactive inExpand
Inactivation of Escherichia coli pyruvate formate-lyase by hypophosphite: evidence for a rate-limiting phosphorus-hydrogen bond cleavage.
TLDR
It is reported here that the inactivation of both the free and acetylated forms of the lyase is subject to a primary kinetic isotope effect using [2H2]hypophosphite, which suggests that phosphorus-hydrogen bond cleavage is at least partially rate limiting during inactivation. Expand
3-Methyleneoxindole: an affinity label of glutathione S-transferase pi which targets tryptophan 38.
TLDR
Results show that MOI reacts preferentially with GST pi, which may be useful in novel combination chemotherapy to enhance the efficacy of alkylating cancer drugs while minimizing toxic side effects. Expand
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