Linked Life Data

11237702

Source:http://linkedlifedata.com/resource/pubmed/id/11237702

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-3-12
pubmed:abstractText
Nitric oxide (NO) is synthesized from l-Arg via N(G)-hydroxyl-l-Arg (NHA) in the heme active site of nitric oxide synthase (NOS). According to the crystal structure of other NOS isoforms, the carboxylate group of l-Arg hydrogen bonds to the hydroxyl group of the conserved Tyr588 residue in the heme distal site of neuronal NOS (nNOS). Indeed, the nNOS mutations Tyr588His, Tyr588Ser, and Tyr588Phe markedly increased the dissociation constants for l-Arg and NHA by 2.2-8.2-fold and 1.5-3.9-fold, respectively. Similarly, Tyr588His and Tyr588Ser mutations markedly decreased the l-Arg-driven NO formation rates by 50 and 30% than that of the wild type, respectively. However, the catalytic activities of the same mutants using NHA were higher than that of the wild type by up to 136%. As a result, the turnover ratio of NHA to l-Arg was 4.12 for the Tyr588Ser mutant, compared with 1.07 for the wild-type enzyme. Intriguingly, heme reduction rates for the Tyr588 mutants were much lower than for wild type by two orders of magnitude.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
621-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Unusual role of Tyr588 of neuronal nitric oxide synthase in controlling substrate specificity and electron transfer.
pubmed:affiliation
Institute for Chemical Reaction Science, Tohoku University, Sendai, 980-8577, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't