Dipartimento Neurofarba, Sezione di Scienze Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze, Sesto Fiorentino (Florence), Italy.
Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
J Enzyme Inhib Med Chem. 2022 Dec;37(1):2786-2792. doi: 10.1080/14756366.2022.2131780.
A β-carbonic anhydrase (CA, EC 4.2.1.1) previously annotated to be present in the genome of , SauBCA, has been shown to belong to another pathogenic bacterium, . 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 , EcoCAβ. The best MscCA activators were D-His, L- and D-DOPA, 4-(2-aminoethyl)-morpholine and L-Asn, which showed Ks of 0.12 - 0.89 µM. The least efficient activators were D-Tyr and L-Gln (Ks of 13.9 - 28.6 µM). 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.
先前在 基因组中注释存在的一种β-碳酸酐酶（CA，EC 4.2.1.1），已被证明属于另一种致病细菌 。已经研究了这种酶 MscCA 与一系列天然和合成氨基酸和胺的激活作用，并将结果与来自 的同源酶 EcoCAβ 的结果进行了比较。最佳的 MscCA 激活剂是 D-His、L-和 D-DOPA、4-（2-氨基乙基）吗啉和 L-Asn，其 Ks 值为 0.12-0.89μM。最不有效的激活剂是 D-Tyr 和 L-Gln（Ks 值为 13.9-28.6μM）。正如之前所描述的，该酶还受到阴离子和磺胺类药物的抑制。内源性 CA 激活剂可能在细菌的毒力和宿主的定植中发挥作用，这使得这一研究课题非常有趣。
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