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Articles 691 - 692 of 692
Full-Text Articles in Medical Microbiology
Inactivation Of Brain Hexokinase By An Adenosine 5'-Triphosphate Analog, Subbarao Bondada, Umakant W. Kenkare
Inactivation Of Brain Hexokinase By An Adenosine 5'-Triphosphate Analog, Subbarao Bondada, Umakant W. Kenkare
Microbiology, Immunology, and Molecular Genetics Faculty Publications
An analog of ATP, 6-mercapto-9+nribofuranosylpurine 5’-triphosphate (SH-TP), functions as a phosphoryl donor for the reaction catalyzed by hexokinase. Incubation of the enzyme with millimolar concentrations of this reagent led to its rapid inactivation. However, the corresponding monophosphate derivative of this reagent was much less effective. A plot of the initial rate of inactivation versus the concentration of SH-TP exhibited saturation, suggesting the formation of a reversible complex between the enzyme and SH-TP prior to the inactivation reaction. The dissociation constant of this enzyme-inhibitor complex was the same as the K, of this reagent with respect to hexokinase in the phosphoryl …
Reaction Of Brain Hexokinase With Tetranitromethane: Oxidation Of Essential Thiol Groups, Subbarao Bondada, Umakant W. Kenkare
Reaction Of Brain Hexokinase With Tetranitromethane: Oxidation Of Essential Thiol Groups, Subbarao Bondada, Umakant W. Kenkare
Microbiology, Immunology, and Molecular Genetics Faculty Publications
Treatment of bovine brain mitochondrial hexokinase with a fivefold molar excess of tetranitromethane (TNM) at pH 8.0 results in a complete loss of activity of the enzyme. Spectral measurements and amino acid analysis showed that only cysteinyl residues were modified by TNM under these conditions. The products of the reaction of TNM with the enzyme were cysteic acid and disulfides as found by amino acid analysis of the carboxymethylated hexokinase. Failure of 2-mercaptoethanol to reverse the effect of TNM suggested that the thiol group that is oxidized to cysteic acid is the one essential for enzyme activity. Substrates glucose and …