Activation studies with amino acids and amines of a β-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri previously annotated as Staphylococcus aureus (SauBCA) carbonic anhydrase

被引：10
|
作者：
Angeli, Andrea [1 ]
Urbanski, Linda J. [2 ]
Capasso, Clemente [3 ]
Parkkila, Seppo [2 ,4 ]
Supuran, Claudiu T. [1 ]
机构：
[1] Univ Firenze, Sez Sci Farmaceut & Nutraceut, Dipartimento Neurofarba, Sesto Fiorentino, Florence, Italy
[2] Tampere Univ, Fac Med & Hlth Technol, Tampere, Finland
[3] Inst Biosci & Bioresources, Dept Biol Agr & Food Sci, Naples, Italy
[4] Tampere Univ Hosp, Fimlab Ltd, Tampere, Finland
来源：
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY | 2022年 / 37卷 / 01期
基金：
芬兰科学院;
关键词：
Staphylococcaceae; carbonic anhydrase; activator; amine; amino acid; Mammaliicoccus (Staphylococcus) sciuri; HISTAMINE SCHIFF-BASES; ISOZYME-II; ACTIVE-SITE; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; SPECTROSCOPIC INVESTIGATIONS; CRYSTALLOGRAPHIC ANALYSIS; PATHOGENIC BACTERIA; ISOFORM-VII; L-HISTIDINE;
D O I：
10.1080/14756366.2022.2131780
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A beta-carbonic anhydrase (CA, EC 4.2.1.1) previously annotated to be present in the genome of Staphylococcus aureus, SauBCA, has been shown to belong to another pathogenic bacterium, Mammaliicoccus (Staphylococcus) sciuri. This enzyme, MscCA, has been investigated for its activation with a series of natural and synthetic amino acid and amines, comparing the results with those obtained for the ortholog enzyme from Escherichia coli, EcoCA beta. The best MscCA activators were D-His, L- and D-DOPA, 4-(2-aminoethyl)-morpholine and L-Asn, which showed K(A)s of 0.12 - 0.89 mu M. The least efficient activators were D-Tyr and L-Gln (K(A)s of 13.9 - 28.6 mu M). The enzyme was also also inhibited by anions and sulphonamides, as described earlier. Endogenous CA activators may play a role in bacterial virulence and colonisation of the host which makes this research topic of great interest.
引用
收藏
页码：2786 / 2792
页数：7
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