Kinetic mechanism of the interaction of D-cycloserine with serine hydroxymethyltransferase
- 28 August 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (18) , 4116-4122
- https://doi.org/10.1021/bi00313a016
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 12 references indexed in Scilit:
- Mechanism of serine hydroxymethylase catalyzed cleavage of L-erythro-.beta.-phenylserine: pH dependence of elementary kinetic processes from spectroscopic, pre-steady-state kinetic, and competitive inhibition studiesBiochemistry, 1979
- Activation of aposerine transhydroxymethylase by pyridoxal-5′-phosphate monomethyl EsterBiochemical and Biophysical Research Communications, 1978
- Suicide substrates for the alanine racemase of Escherichia coli BBiochemistry, 1978
- Studies on the reactions of substituted D,L-erythro-β-phenylserines with lamb liver serine hydroxymethylase. Effects of substituents upon the dealdolization stepBiochemistry, 1977
- Studies of the reactions of lamb liver serine hydroxymethylase with L-phenylalanine: kinetic isotope effects upon quinonoid intermediate formationBiochemistry, 1977
- The Interaction of Cycloserine with Glutamate Aspartate Transaminase as Measured by Fluorescence SpectroscopyJournal of Biological Chemistry, 1967
- Cycloserine inhibition of gamma-aminobutyric-alpha-ketoglutaric transaminaseBiochemical Pharmacology, 1964
- The Enzymatic Synthesis of D-Alanyl-D-alanine. III. On the Inhibition of D-Alanyl-D-alanine Synthetase by the Antibiotic D-Cycloserine*Biochemistry, 1964
- SERINE TRANSHYDROXYMETHYLASE - TRANSAMINATION OF D-ALANINE1964
- SERINE TRANSHYDROXYMETHYLASE - PROPERTIES OF ENZYME-SUBSTRATE COMPLEXES OF D-ALANINE + GLYCINE1964