The extremo-α-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense, the fastest CA known, is highly activated by amino acids and amines

被引：43

作者：

Akdemir, Atilla ^{[1
]}

Vullo, Daniela ^{[2
]}

De Luca, Viviana ^{[3
]}

Scozzafava, Andrea ^{[2
]}

Carginale, Vincenzo ^{[3
]}

Rossi, Mose ^{[3
,4
]}

Supuran, Claudiu T. ^{[2
,5
]}

Capasso, Clemente ^{[3
]}

机构：

[1] Bezmialem Vakif Univ, Fac Pharm, Dept Pharmacol, TR-34093 Istanbul, Turkey

[2] Univ Firenze, Lab Chim Bioinorgan, I-50019 Florence, Italy

[3] Ist Biochim Prot VNR, I-80131 Naples, Italy

[4] Univ Naples Federico II, Ctr Ric Interdipartimentale Biomat, I-80125 Naples, Italy

[5] Univ Firenze, Dipartimento Sci Farmaceut, I-50019 Florence, Italy

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2013年 / 23卷 / 04期

关键词：

Carbonic anhydrase; Extremophile; Sulfurihydrogenibium azorense; Enzyme activator; Amine; Amino acid; HUMAN ISOZYME-II; THERAPEUTIC APPLICATIONS; HELICOBACTER-PYLORI; ISOFORM-I; MYCOBACTERIUM-TUBERCULOSIS; CRYSTALLOGRAPHIC ANALYSIS; YELLOWSTONENSE YO3AOP1; NEISSERIA-GONORRHOEAE; CRYSTAL-STRUCTURE; ANION INHIBITION;

D O I：

10.1016/j.bmcl.2012.12.009

中图分类号：

R914 [药物化学];

学科分类号：

100705 [微生物与生化药学];

摘要：

The alpha-carbonic anhydrase (CA, EC 4.2.1.1) from the extremophilic bacterium Sulfurihydrogenibium azo-rense (SazCA) was recently shown to be the fastest CA known. Here we investigated this enzyme for its activation with a series of amino acids and amines. The best SazCA activators were D-Phe, L-DOPA, L- and D-Trp, dopamine and serotonin, which showed activation constants in the range of 3-23 nM. L- and D-His, L-Phe, L-Tyr, 2-pyridyl-methylamine and L-adrenaline were also effective activators (K(A)s in the range of 62-90 nM), whereas D-Dopa, D-Tyr and several heterocyclic amines showed activity in the micromolar range. The good thermal stability, robustness, very high catalytic activity and propensity to be activated by simple amino acids and amines, make SazCA a very interesting candidate for biomimetic CO2 capture processes. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：1087 / 1090

页数：4

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