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PHO15 genes of Candida albicans and Candida parapsilosis encode HAD-type phosphatases dephosphorylating 2-phosphoglycolate
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SYSNO ASEP 0503946 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název PHO15 genes of Candida albicans and Candida parapsilosis encode HAD-type phosphatases dephosphorylating 2-phosphoglycolate Tvůrce(i) Kročová, E. (CZ)
Neradová, S. (CZ)
Kupčík, R. (CZ)
Janovská, S. (CZ)
Bílková, Z. (CZ)
Heidingsfeld, Olga (UOCHB-X) RID, ORCIDČíslo článku foy112 Zdroj.dok. FEMS Yeast Research. - : Oxford University Press - ISSN 1567-1356
Roč. 19, č. 1 (2019)Poč.str. 10 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova Candida albicans ; Candida parapsilosis ; phosphatase ; HAD-family ; 2-phosphoglycolate ; PHO15 Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology Způsob publikování Open access Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000462551200007 EID SCOPUS 85055830852 DOI 10.1093/femsyr/foy112 Anotace Most of the phosphatases of human fungal pathogens Candida albicans and C. parapsilosis have never been experimentally characterised, although dephosphorylation reactions are central to many biological processes. PHO15 genes of these yeasts have been annotated as the sequences encoding 4-nitrophenyl phosphatase, on the basis of homology to PHO13 gene from the bakers' yeast Saccharomyces cerevisiae. To examine the real function of these potential phosphatases from Candida spp., CaPho15p and CpPho15p were prepared using expression in Escherichia coli and characterised. They share the hallmark motifs of the haloacid dehalogenase superfamily, readily hydrolyse 4-nitrophenyl phosphate at pH 8-8.3 and require divalent cations (Mg2+, Mn2+ or Co2+) as cofactors. CaPho15p and CpPho15p did not dephosphorylate phosphopeptides, but rather hydrolysed molecules related to carbohydrate metabolism. The preferred substrate for the both phosphatases was 2-phosphoglycolate. Among the other molecules tested, CaPho15 showed preference for glyceraldehyde phosphate and ss-glycerol phosphate, while CpPho15 dephosphorylated mainly 1,3-dihydroxyacetone phosphate. This type of substrate specificity indicates that CaPho15 and CpPho15 may be a part of metabolic repair system of C. albicans and C. parapsilosis. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2020 Elektronická adresa https://academic.oup.com/femsyr/article/19/1/foy112/5126360
Počet záznamů: 1