Linked Life Data

12595715

Source:http://linkedlifedata.com/resource/pubmed/id/12595715

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2003-2-21
pubmed:abstractText
Crystals of the glycogen synthase (GS) from Agrobacterium tumefaciens have been grown that diffract to 2.6 A resolution. The enzyme, which is homologous to the starch synthases of plants, catalyzes the last reaction step in the biosynthesis of glycogen. It is a alpha-retaining glucosyltransferase that uses ADP-glucose to incorporate additional glucose monomers onto the growing glycogen polymer. Its homology with mammalian GSs is marginal, but several regions shown to be important in catalysis are strictly conserved. Knowledge of the crystal structure of GS will be a major advance in the understanding of glycogen/starch metabolism and its regulation. A rational approach in enzyme engineering can subsequently be envisaged. The multiwavelength anomalous diffraction approach will be used to solve the phase problem.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
526-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Preliminary crystallographic studies of glycogen synthase from Agrobacterium tumefaciens.
pubmed:affiliation
Insituto de Investigaciones Biotecnologicas UNSAM, San Martin, Argentina.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't