ON THE MECHANISM OF ENZYME INHIBITION BY SULFHYDRYL REAGENTS
نویسندگان
چکیده
منابع مشابه
On the mechanism of enzyme inhibition by sulfhydryl reagents.
In recent years a great deal of evidence has accumulated to show that intact -SH groups are necessary for the full activity of a variety of enzymes. The exact function of the thiol group in the protein part of these “sulfhydryl enzymes,” however, remains obscure. It has been suggested that the -SH group directly participates in the activity of these enzymes, and that it might be actually locate...
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Mechanism of ATP-sensitive K Channel Inhibition by Sulfhydryl Modification
ATP-sensitive potassium (KATP) channels are reversibly inhibited by intracellular ATP. Agents that interact with sulfhydryl moieties produce an irreversible inhibition of KATP channel activity when applied to the intracellular membrane surface. ATP appears to protect against this effect, suggesting that the cysteine residue with which thiol reagents interact may either lie within the ATP-bindin...
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15 صفحه اولMechanism-Based Studies of the Active Site-Directed Inhibition and Activation of Enzyme Transketolase
Derivatives of phenyl-keto butenoic acids have been reported to be inhibitors of pyruvate decarboxylase, (PDC). The inhibition of transketolase, a thiamine requiring enzyme such as PDF, by meta nitrophenyl derivative of 2-oxo-3-butenoic acid (MNPB) is reported here. These studies indicate that the inhibitor binds to the enzyme at the active site. A two-step inhibition was observed, first th...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1948
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)57369-5