Paraoxon, 4-nitrophenyl phosphate and acetate are substrates of α- but not of β-, γ- and ζ-carbonic anhydrases

被引：46

作者：

Innocenti, Alessio

Supuran, Claudiu T. ^{[1
]}

机构：

[1] Univ Florence, Lab Chim Bioinorgan, Rm 188,Via Lastruccia 3, I-50019 Florence, Italy

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2010年 / 20卷 / 21期

关键词：

Carbonic anhydrase; Esterase; CO2; hydrase; Phosphatase; Paraoxon; Metalloenzyme; THALASSIOSIRA-WEISSFLOGII; THERAPEUTIC APPLICATIONS; HELICOBACTER-PYLORI; MARINE DIATOMS; CLASS ENZYME; ACTIVE-SITE; INHIBITORS; TARGET; IX; SULFONAMIDES;

D O I：

10.1016/j.bmcl.2010.08.110

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to alpha-, beta-, gamma- and zeta-classes and from various organisms, ranging from the bacteria, archaea to eukarya domains, were investigated for their esterase/phosphatase activity with 4-nitrophenyl acetate, 4-nitrophenyl phosphate and paraoxon as substrates. Only alpha-CAs showed esterase/phosphatase activity, whereas enzymes belonging to the beta-, gamma- and zeta-classes were completely devoid of such activity. Paraoxon, the metabolite of the organophosphorus insecticide parathione, was a much better substrate for several human/murine alpha-CA isoforms (CA I, II and XIII), with k(cat)/K-M in the range of 2681.6-4474.9 M (1) s (1), compared to 4-nitrophenyl phosphate (k(cat)/K-M of 14.9-1374.4 M (1) s (1)). (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：6208 / 6212

页数：5