منابع مشابه
Catalytic Site Cysteines of Thiol Enzyme: Sulfurtransferases
Thiol enzymes have single- or double-catalytic site cysteine residues and are redox active. Oxidoreductases and isomerases contain double-catalytic site cysteine residues, which are oxidized to a disulfide via a sulfenyl intermediate and reduced to a thiol or a thiolate. The redox changes of these enzymes are involved in their catalytic processes. On the other hand, transferases, and also some ...
متن کاملMutational analysis of the three cysteines and active-site aspartic acid 103 of ketosteroid isomerase from Pseudomonas putida biotype B.
In order to clarify the roles of three cysteines in ketosteroid isomerase (KSI) from Pseudomonas putida biotype B, each of the cysteine residues has been changed to a serine residue (C69S, C81S, and C97S) by site-directed mutagenesis. All cysteine mutations caused only a slight decrease in the k(cat) value, with no significant change of Km for the substrate. Even modification of the sulfhydryl ...
متن کاملMechanism-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...
متن کاملInvestigation of solvent effect on the active site energy of Carbonic Anhydrase and Ribonucleotide Reductase
Enzymes catalyze many biological reactions. The rates of chemical reaction in the presence ofenzymes are, in some cases, accelerated more than 10 orders of magnitude relative to thecorresponding rates in solution.In this paper a comparison between optimized structures of two enzyme molecules in aspect ofenergy and dipole moment in different conditions including presence of metallic ion, without...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1970
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1970.tb01108.x