Linked Life Data

21129966

Source:http://linkedlifedata.com/resource/pubmed/id/21129966

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-12-24
pubmed:abstractText
Oxidative modification of protein tyrosine phosphatases (PTPs) has recently been recognized as an important regulatory mechanism in biological systems. Reported herein is the oxidative inactivation of the lymphoid tyrosine phosphatase (LYP) with both the general nitrosating reagent sodium nitroprusside (SNP) and also a novel peptide-based nitrosating reagent, Ac-ARLIEDNE(HcyNO)TAREG-NH(2), where HcyNO = S-nitrosohomocysteine. The SNP oxidatively inactivated LYP with a k(inact) of 0.383 per min and a K(I) of 27.4 ?M and mixed-type inactivation kinetics. The peptide was a competitive LYP inactivator with a k(inact) of 0.0472 per min and a K(I) of 7.00 ?M. LYP nitrosation by SNP was characterized by the addition of several NO moieties to the enzyme, while oxidation of LYP by the peptide did not result in the formation of a LYP-NO adduct. We propose that general NO donors promiscuously nitrosate any free cysteine residue while the active-site directed peptide selectively oxidizes the catalytic cysteine residue, resulting in the formation of a disulfide bond between the catalytic cysteine residue and a second cysteine in the active site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1464-3405
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
285-7
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Oxidative inactivation of the lymphoid tyrosine phosphatase mediated by both general and active site directed NO donors.
pubmed:affiliation
Department of Medicinal Chemistry, University of Utah, Salt Lake City, UT 84112, United States.
pubmed:publicationType
Journal Article