Role of arginine in the binding of thiamin pyrophosphate to Escherichia coli pyruvate oxidase. 1982

J G Koland, and T A O'Brien, and R B Gennis

The mode of interaction between Escherichia coli pyruvate oxidase and its cofactor, thiamin pyrophosphate (TPP), was studied with the aid of arginine-directed reagents. The enzyme is rapidly inactivated by either phenylglyoxal or 2,3-butanedione, with the cofactor, TPP, offering partial protection against these reagents. The inactivation by phenylglyoxal was found to be reversible. Experiments with [7-14C]phenylglyoxal showed that while several arginine residues react with this reagent, TPP can prevent the labeling of one such residue. Furthermore, inactivation by 2,3-butanedione is attended by at least a 100-fold decrease in affinity of the enzyme for TPP. These results suggest a direct role for arginine in the binding of the cofactor.

UI MeSH Term Description Entries
D010658 Phenylglyoxal A reagent that is highly selective for the modification of arginyl residues. It is used to selectively inhibit various enzymes and acts as an energy transfer inhibitor in photophosphorylation.
D011771 Pyruvate Oxidase Oxidase, Pyruvate
D004852 Epoxy Compounds Organic compounds that include a cyclic ether with three ring atoms in their structure. They are commonly used as precursors for POLYMERS such as EPOXY RESINS. Epoxide,Epoxides,Epoxy Compound,Oxiranes,Compound, Epoxy,Compounds, Epoxy
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D001120 Arginine An essential amino acid that is physiologically active in the L-form. Arginine Hydrochloride,Arginine, L-Isomer,DL-Arginine Acetate, Monohydrate,L-Arginine,Arginine, L Isomer,DL Arginine Acetate, Monohydrate,Hydrochloride, Arginine,L Arginine,L-Isomer Arginine,Monohydrate DL-Arginine Acetate
D013835 Thiamine Pyrophosphate The coenzyme form of Vitamin B1 present in many animal tissues. It is a required intermediate in the PYRUVATE DEHYDROGENASE COMPLEX and the KETOGLUTARATE DEHYDROGENASE COMPLEX. Cocarboxylase,Thiamine Diphosphate,Berolase,Pyrophosphate, Thiamine

Related Publications

J G Koland, and T A O'Brien, and R B Gennis
April 1980, The Journal of biological chemistry,
J G Koland, and T A O'Brien, and R B Gennis
March 1984, The Journal of biological chemistry,
J G Koland, and T A O'Brien, and R B Gennis
June 1991, The Journal of biological chemistry,
J G Koland, and T A O'Brien, and R B Gennis
November 1985, The Journal of biological chemistry,
J G Koland, and T A O'Brien, and R B Gennis
November 1976, Biochimica et biophysica acta,
J G Koland, and T A O'Brien, and R B Gennis
June 1991, The Journal of biological chemistry,
J G Koland, and T A O'Brien, and R B Gennis
November 1982, The Journal of biological chemistry,
Copied contents to your clipboard!