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Title: H NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine gamma-lyase

Abstract

Hydrogen exchange reactions of various L-amino acids catalyzed by L-methionine gamma-lyase (EC 4.4.1.11) have been studied. The enzyme catalyzes the rapid exchange of the alpha- and beta-hydrogens of L-methionine and S-methyl-L-cysteine with deuterium from the solvent. The rate of alpha-hydrogen exchange was about 40 times faster than that of the enzymatic elimination reaction of the sulfur-containing amino acids. The enzyme also catalyzes the exchange reaction of alpha- and beta-hydrogens of the straight-chain L-amino acids which are not susceptible to elimination. The exchange rates of the alpha-hydrogen and the total beta-hydrogens of L-alanine and L-alpha-aminobutyrate with deuterium followed first-order kinetics. For L-norvaline, L-norleucine, S-methyl-L-cysteine, and L-methionine, the rate of alpha-hydrogen exchange followed first-order kinetics, but the rate of total beta-hydrogen exchange decreased due to a primary isotope effect at the alpha-position. L-Phenylalanine and L-tryptophan slowly underwent alpha-hydrogen exchange. The pro-R hydrogen of glycine was deuterated stereospecifically.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Kyoto Univ., Kyoto-Fu, Japan
OSTI Identifier:
6235430
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemistry; (United States); Journal Volume: 15
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 62 RADIOLOGY AND NUCLEAR MEDICINE; HYDRO-LYASES; BIOCHEMICAL REACTION KINETICS; NUCLEAR MAGNETIC RESONANCE; AMINO ACIDS; CYSTEINE; DEUTERIUM; HYDROGEN; METHIONINE; PSEUDOMONAS; BACTERIA; CARBON-OXYGEN LYASES; CARBOXYLIC ACIDS; DRUGS; ELEMENTS; ENZYMES; HYDROGEN ISOTOPES; ISOTOPES; KINETICS; LIGHT NUCLEI; LIPOTROPIC FACTORS; LYASES; MAGNETIC RESONANCE; MICROORGANISMS; NONMETALS; NUCLEI; ODD-ODD NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; REACTION KINETICS; RESONANCE; STABLE ISOTOPES; THIOLS; 550201* - Biochemistry- Tracer Techniques; 550601 - Medicine- Unsealed Radionuclides in Diagnostics

Citation Formats

Esaki, N., Nakayama, T., Sawada, S., Tanaka, H., and Soda, K.. H NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine gamma-lyase. United States: N. p., 1985. Web. doi:10.1021/bi00336a007.
Esaki, N., Nakayama, T., Sawada, S., Tanaka, H., & Soda, K.. H NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine gamma-lyase. United States. doi:10.1021/bi00336a007.
Esaki, N., Nakayama, T., Sawada, S., Tanaka, H., and Soda, K.. Tue . "H NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine gamma-lyase". United States. doi:10.1021/bi00336a007.
@article{osti_6235430,
title = {H NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine gamma-lyase},
author = {Esaki, N. and Nakayama, T. and Sawada, S. and Tanaka, H. and Soda, K.},
abstractNote = {Hydrogen exchange reactions of various L-amino acids catalyzed by L-methionine gamma-lyase (EC 4.4.1.11) have been studied. The enzyme catalyzes the rapid exchange of the alpha- and beta-hydrogens of L-methionine and S-methyl-L-cysteine with deuterium from the solvent. The rate of alpha-hydrogen exchange was about 40 times faster than that of the enzymatic elimination reaction of the sulfur-containing amino acids. The enzyme also catalyzes the exchange reaction of alpha- and beta-hydrogens of the straight-chain L-amino acids which are not susceptible to elimination. The exchange rates of the alpha-hydrogen and the total beta-hydrogens of L-alanine and L-alpha-aminobutyrate with deuterium followed first-order kinetics. For L-norvaline, L-norleucine, S-methyl-L-cysteine, and L-methionine, the rate of alpha-hydrogen exchange followed first-order kinetics, but the rate of total beta-hydrogen exchange decreased due to a primary isotope effect at the alpha-position. L-Phenylalanine and L-tryptophan slowly underwent alpha-hydrogen exchange. The pro-R hydrogen of glycine was deuterated stereospecifically.},
doi = {10.1021/bi00336a007},
journal = {Biochemistry; (United States)},
number = ,
volume = 15,
place = {United States},
year = {Tue Jul 16 00:00:00 EDT 1985},
month = {Tue Jul 16 00:00:00 EDT 1985}
}