Linked Life Data

16644029

Source:http://linkedlifedata.com/resource/pubmed/id/16644029

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-7-3
pubmed:databankReference
pubmed:abstractText
LmACR2 is the first identified antimonate reductase responsible for the reduction of pentavalent antimony in pentostam to the active trivalent form of the drug in Leishmania. LmACR2 is a homologue of the yeast arsenate reductase Acr2p and Cdc25 phosphatases and has the HC[X]5R phosphatase motif. Purified LmACR2 exhibited phosphatase activity in vitro and was able to dephosphorylate a phosphotyrosine residue from a synthetic peptide. This phosphatase activity was inhibited by classical inhibitors such as orthovanadate. LmACR2-catalyzed phosphatase activity was inhibited by either antimonate or arsenate. Site-directed mutagenesis experiments showed that the H74C[X]5R81 motif was involved in catalysis. This is the first report of a metalloid reductase with a bifunctional role in protein tyrosine phosphatase activity. Leishmania is never exposed to metalloids during its life cycle. It is therefore unlikely that it would evolve an enzyme exclusively for drug activation. We propose that the physiological function of LmACR2 is to dephosphorylate phosphotyrosine residues in leishmanial proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0166-6851
pubmed:author
pubmed:issnType
Print
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
161-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Bifunctional role of the leishmanial antimonate reductase LmACR2 as a protein tyrosine phosphatase.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, 540 East Canfield Avenue, Detroit, MI 48201, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural