Linked Life Data

3098284

Source:http://linkedlifedata.com/resource/pubmed/id/3098284

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1987-2-10
pubmed:abstractText
The glycogen phosphorylase molecule absorbs the ultraviolet energy of a nitrogen laser to form an excited state of the cofactor. The decay rate of this state has a lifetime of 6.7 microseconds, and its sensitivity to bound substrates presents a new perspective of the mechanism. A careful analysis of the decay curve for native enzyme and cofactor analogues showed that the lifetime depends on the conformation of protein groups at the active site and how the residues change with bound substrate. The reactive ternary complexes obtained from either direction of the reaction yielded the same lifetime, indicating a change in the active-site conformation to a common configuration for the cofactor and substrate phosphate. This configuration indicates an increase in the cofactor 5'-PO4 pKa and a possible proton shuttle. The pyridoxal 5'-pyrophosphate reconstituted enzyme showed no conformational change alone or in the presence of oligosaccharide. This result does not support an electrophilic attack by the 5'-PO4 phosphorus.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6070-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Protein dynamics of glycogen phosphorylase.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.