Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00446845" target="_blank" >RIV/61388963:_____/15:00446845 - isvavai.cz</a>
Result on the web
<a href="http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0134506" target="_blank" >http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0134506</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0134506" target="_blank" >10.1371/journal.pone.0134506</a>
Alternative languages
Result language
angličtina
Original language name
Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase
Original language description
Human aldo-keto reductase 1B15 (AKR1B15) is a newly discovered enzyme which shares 92% amino acid sequence identity with AKR1B10. While AKR1B10 is a well characterized enzyme with high retinaldehyde reductase activity, involved in the development of several cancer types, the enzymatic activity and physiological role of AKR1B15 are still poorly known. Here, the purified recombinant enzyme has been subjected to substrate specificity characterization, kinetic analysis and inhibitor screening, combined withstructural modeling. AKR1B15 is active towards a variety of carbonyl substrates, including retinoids, with lower k(cat) and K-m values than AKR1B10. In contrast to AKR1B10, which strongly prefers all-trans-retinaldehyde, AKR1B15 exhibits superior catalytic efficiency with 9-cis-retinaldehyde, the best substrate found for this enzyme. With ketone and dicarbonyl substrates, AKR1B15 also shows higher catalytic activity than AKR1B10. Several typical AKR inhibitors do not significantly affec
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
PLoS ONE
ISSN
1932-6203
e-ISSN
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Volume of the periodical
10
Issue of the periodical within the volume
7
Country of publishing house
US - UNITED STATES
Number of pages
19
Pages from-to
"e0134506/1"-"e0134506/19"
UT code for WoS article
000358836800146
EID of the result in the Scopus database
2-s2.0-84941671000