Exploration of the residues modulating the catalytic features of human carbonic anhydrase XIII by a site-specific mutagenesis approach

Autor:	Giuseppina De Simone, Anna Di Fiore, Emanuela Truppo, Emma Langella, Daniela Vullo, Claudiu T. Supuran, Simona Maria Monti
Jazyk:	angličtina
Rok vydání:	2019
Předmět:	cytosolic human carbonic anhydrases catalytic activity proton transfer histidine cluster site-specific mutagenesis Therapeutics. Pharmacology RM1-950
Zdroj:	Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 34, Iss 1, Pp 1506-1510 (2019)
Druh dokumentu:	article
ISSN:	1475-6366 1475-6374 14756366
DOI:	10.1080/14756366.2019.1653290
Popis:	Carbonic anhydrases (CAs) are ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide to bicarbonate and proton. In humans there are 15 isoforms among which only 12 are catalytically active. Since active human (h) CAs show different efficiency, the understanding of the molecular determinants affecting it is a matter of debate. Here we investigated, by a site-specific mutagenesis approach, residues modulating the catalytic features of one of the least investigated cytosolic isoform, i.e. hCA XIII. Results showed that residues assisting the formation of an ordered solvent network within the catalytic site as well as those forming a histidine cluster on the protein surface are important to guarantee an efficient proton transfer.
Databáze:	Directory of Open Access Journals
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