Linked Life Data

9587003

Source:http://linkedlifedata.com/resource/pubmed/id/9587003

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-6-1
pubmed:databankReference
pubmed:abstractText
Hydrogen peroxide (H2O2) has been implicated recently as an intracellular messenger that affects cellular processes including protein phosphorylation, transcription and apoptosis. A set of novel peroxidases, named peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor. The crystal structure of a human Prx enzyme, hORF6, reveals that the protein contains two discrete domains and forms a dimer. The N-terminal domain has a thioredoxin fold and the C-terminal domain is used for dimerization. The active site cysteine (Cys 47), which exists as cysteine-sulfenic acid in the crystal, is located at the bottom of a relatively narrow pocket. The positively charged environment surrounding Cys 47 accounts for the peroxidase activity of the enzyme, which contains no redox cofactors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1072-8368
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
400-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution.
pubmed:affiliation
Division of Protein Engineering, Korea Research Institute of Bioscience and Biotechnology, KIST, Yusong, Taejon, South Korea.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't