Linked Life Data

12646220

Source:http://linkedlifedata.com/resource/pubmed/id/12646220

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-3-20
pubmed:abstractText
Under nitrosative stressed condition intracellular GSNO accumulation is common to all cell types. Conserved NADH-dependent GSNO reductase was reported previously as an important cellular protective measure against this. In spite of the constitutive nature of the enzyme, we observed in vivo inactivation of two important enzymes-glyoxalase-I and glyceraldehyde-3-phosphate dehydrogenase under 5 mM GSNO stress in two budding yeasts, though with difference in their sensitivity. Former was more susceptible to inactivation in in vitro condition, too. In this study, we explored the competitive nature of yeast glyoxalase-I inhibition by GSNO. GSNO actually competes with GSH substrate-binding site of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
302
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
665-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Nitrosative stress on yeast: inhibition of glyoxalase-I and glyceraldehyde-3-phosphate dehydrogenase in the presence of GSNO.
pubmed:affiliation
Department of Biochemistry, University College of Science, Calcutta University, 35, Ballygunge Circular Road, Kolkata 700 019, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't