Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-3-27
pubmed:abstractText
The X-ray crystal structures of two glycosyltransferases (GTs)--beta 1,3-glucuronyltransferase 1 (GlcAT1) and alpha 1,4-N-acetylhexosaminyltransferase (EXTL2)--have now been determined in the presence of both donor and acceptor substrates. These enzymes are involved in glucosaminylglycan (GAG) synthesis where they catalyze inverting and retaining transfer reactions, respectively. As members of a large family of enzymes that transfer sugar groups from donor nucleotide-sugars to acceptor substrates, GlcAT1 and EXTL2 retain conserved GT folds. Comparative analysis of these structures reveals signature features for selecting specific donor sugars. Adaptive binding of the disaccharide moiety of the acceptor sugars enables the enzymes to catalyze either an inverting S(N)2-type displacement reaction or a retaining S(N)i-like transfer reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
303
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
393-8
pubmed:dateRevised
2005-11-16
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Glucosaminylglycan biosynthesis: what we can learn from the X-ray crystal structures of glycosyltransferases GlcAT1 and EXTL2.
pubmed:affiliation
Pharmacogenetics Section, Laboratory of Reproductive and Developmental Toxicology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA. negishi@niehs.nih.gov
pubmed:publicationType
Journal Article, Review