Borch Department of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, IN, United States.
Borch Department of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, IN, United States.
Enzymes. 2024;55:283-311. doi: 10.1016/bs.enz.2024.05.011. Epub 2024 Jun 8.
Carbonic anhydrase metalloenzymes are encoded in genomes throughout all kingdoms of life with a conserved function catalyzing the reversible conversion of CO to bicarbonate. Carbonic anhydrases have been well-investigated in humans, but are still relatively understudied in bacterial organisms, including Enterococci. Studies over the past decade have presented bacterial carbonic anhydrases as potential drug targets, with some chemical scaffolds potently inhibiting the Enterococcus carbonic anhydrases in vitro and displaying antimicrobial efficacy against Enterococcus organisms. While carbonic anhydrases in Enterococci still have much to be explored, hypotheses may be drawn from similar Gram-positive organisms for which known information exists about carbonic anhydrase function and relevance. Within this chapter is reported information and rational hypotheses regarding the subcellar locations, potential physiological roles, essentiality, structures, and kinetics of carbonic anhydrases in Enterococci.
碳酸酐酶金属酶在所有生命王国的基因组中都有编码，其保守功能是催化 CO 可逆转化为碳酸氢盐。碳酸酐酶在人类中得到了很好的研究，但在包括肠球菌在内的细菌生物中仍然相对研究不足。过去十年的研究表明，细菌碳酸酐酶是潜在的药物靶点，一些化学支架在体外有力地抑制肠球菌碳酸酐酶，并对肠球菌有抗菌效果。虽然肠球菌中的碳酸酐酶还有很多有待探索，但可以从具有已知碳酸酐酶功能和相关性信息的类似革兰氏阳性菌中得出假设。本章报告了关于肠球菌中碳酸酐酶的亚细胞位置、潜在生理作用、必需性、结构和动力学的信息和合理假设。
