Substrate specificity and reaction mechanism of human prolidase
نویسندگان
چکیده
منابع مشابه
Reaction Mechanism and Specificity of Human GMP Reductase
GMP reductase was purified 150,000-fold from human erythrocytes by affinity chromatography on Cibacron blue/agarose. The enzyme was stable to storage and could be assayed spectrophotometrically. Plots of the velocity-* uersus [GMP]-’ demonstrated downward curvature above 250 pM GMP. GTP was found to be a nonessential activator. It caused the K’, for GMP to decrease from 7.5 to 4.4 pM and the V&...
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Haloalkane dehalogenases catalyse environmentally important dehalogenation reactions. These microbial enzymes represent objects of interest for protein engineering studies, attempting to improve their catalytic efficiency or broaden their substrate specificity towards environmental pollutants. This paper presents the results of a comparative study of haloalkane dehalogenases originating from di...
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متن کاملSpecificity and pH dependence for acylproline cleavage by prolidase.
Catalytic pH dependence for the hydrolytic activity of the enzyme prolidase with a series of dipeptide substrates is found to be generally bell-shaped (kcat/Km) or simple sigmoidal (kcat). An enzymic residue with a pKa value of 6.6 is found to be critically involved in the catalytic mechanism, as is the substrate amino group. Significant catalysis at a pH of 6.6 is also observed for prolidase w...
متن کاملReaction mechanism and specificity of human GMP reductase. Substrates, inhibitors, activators, and inactivators.
GMP reductase was purified 150,000-fold from human erythrocytes by affinity chromatography on Cibacron blue/agarose. The enzyme was stable to storage and could be assayed spectrophotometrically. Plots of the velocity-* uersus [GMP]-’ demonstrated downward curvature above 250 pM GMP. GTP was found to be a nonessential activator. It caused the K’, for GMP to decrease from 7.5 to 4.4 pM and the V&...
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ژورنال
عنوان ژورنال: The FEBS Journal
سال: 2017
ISSN: 1742-464X
DOI: 10.1111/febs.14158