Structural and biochemical characterization of the folyl-poly-gamma-L-glutamate hydrolyzing activity of human glutamate carboxypeptidase II
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10285953" target="_blank" >RIV/00216208:11310/14:10285953 - isvavai.cz</a>
Alternative codes found
RIV/86652036:_____/14:00431487 RIV/61388963:_____/14:00431487
Result on the web
<a href="http://dx.doi.org/10.1111/febs.12857" target="_blank" >http://dx.doi.org/10.1111/febs.12857</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/febs.12857" target="_blank" >10.1111/febs.12857</a>
Alternative languages
Result language
angličtina
Original language name
Structural and biochemical characterization of the folyl-poly-gamma-L-glutamate hydrolyzing activity of human glutamate carboxypeptidase II
Original language description
In addition to its well-characterized role in the central nervous system, human glutamate carboxypeptidase II (GCPII; Uniprot ID Q04609) acts as a folate hydrolase in the small intestine, participating in the absorption of dietary polyglutamylated folates (folyl-n-gamma-L-glutamic acid), which are the provitamin form of folic acid (also known as vitamin B-9). Despite the role of GCPII as a folate hydrolase, nothing is known about the processing of polyglutamylated folates by GCPII at the structural or enzymological level. Moreover, many epidemiologic studies on the relationship of the naturally occurring His475Tyr polymorphism to folic acid status suggest that this polymorphism may be associated with several pathologies linked to impaired folate metabolism. In the present study, we report: (a) a series X-ray structures of complexes between a catalytically inactive GCPII mutant (Glu424Ala) and a panel of naturally occurring polyglutamylated folates; (b) the X-ray structure of the His475
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEBS Journal
ISSN
1742-464X
e-ISSN
—
Volume of the periodical
281
Issue of the periodical within the volume
14
Country of publishing house
GB - UNITED KINGDOM
Number of pages
15
Pages from-to
3228-3242
UT code for WoS article
000339800800011
EID of the result in the Scopus database
—