Linked Life Data

14508061

Source:http://linkedlifedata.com/resource/pubmed/id/14508061

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-9-25
pubmed:abstractText
Transglutaminase enzymes (TGases) catalyze the calcium dependent formation of an isopeptide bond between protein-bound glutamine and lysine substrates. Previously we have shown that activated TGase 3 acquires two additional calcium ions at site two and three. The calcium ion at site three results in the opening of a channel. At this site, the channel opening and closing could modulate, depending on which metal is bound. Here we propose that the front of the channel could be used by the two substrates for enzyme reaction. We propose that the glutamine substrate is directed from Trp236 into the enzyme, shown by molecular docking. Then a lysine substrate approaches the opened active site to engage Trp327, leading to formation of the isopeptide bond. Further, direct comparisons of the structures of TGase 3 with other TGases have allowed us to identify several residues that might potentially be involved in generic and specific recognition of the glutamine and lysine substrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1226-3613
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
228-42
pubmed:dateRevised
2007-4-25
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
A model for the reaction mechanism of the transglutaminase 3 enzyme.
pubmed:affiliation
Laboratory of X-ray Crystallography Facility/Office of Science and Technology, National Institutes of Health, Bethesda, MD 20892-8023, USA. ahvazib@mail.nih.gov
pubmed:publicationType
Journal Article, Review