PHO15 genes of Candida albicans and Candida parapsilosis encode HAD-type phosphatases dephosphorylating 2-phosphoglycolate
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F19%3A00541699" target="_blank" >RIV/60162694:G44__/19:00541699 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/19:00503946 RIV/00216275:25310/19:39915052
Result on the web
<a href="https://academic.oup.com/femsyr/article/19/1/foy112/5126360" target="_blank" >https://academic.oup.com/femsyr/article/19/1/foy112/5126360</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/femsyr/foy112" target="_blank" >10.1093/femsyr/foy112</a>
Alternative languages
Result language
angličtina
Original language name
PHO15 genes of Candida albicans and Candida parapsilosis encode HAD-type phosphatases dephosphorylating 2-phosphoglycolate
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEMS Yeast Research
ISSN
1567-1356
e-ISSN
1567-1364
Volume of the periodical
19
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
foy112
UT code for WoS article
000462551200007
EID of the result in the Scopus database
2-s2.0-85055830852