Linked Life Data

7236607

Source:http://linkedlifedata.com/resource/pubmed/id/7236607

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1981-8-27
pubmed:abstractText
We have previously reported the physicochemical and kinetic properties of glycogen phosphorylase modified by arginine-specific reagent under different conditions [Dreyfus, M., Vandenbunder, B., & Buc, H. (1980) Biochemistry 19, 3634-3642]. The properties of the modified enzyme depend upon the conformation adopted by the enzyme during the modification reaction. In this paper, we report the localization of the crucial modified arginine residues on the primary structure. The chymotryptic peptide extending from residue Asp-563 to residue Tyr-572 was shown to contain one arginine residue (Arg-568) which is chemically modified by phenylglyoxal in phosphorylase a and in activated phosphorlase b. Inclusion of glucose 1-phosphate in the modification medium protects this residue from modification, with a concomitant protection of the enzyme activity. Furthermore, this residue is not reactive toward phenylglyoxal in phosphorylase b in the absence of any effector. Addition of the AMP analogue 2'dAMP, which is not an activator of the enzyme, does not increase Arg-568 reactivity but protects from modification several arginine residues located between Arg-242 and Leu-348. The location and the role of Arg-568 in phosphorylase are discussed with reference to recent data from X-ray crystallography.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2354-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Mechanism of allosteric activation of glycogen phosphorylase probed by the reactivity of essential arginine residues. Identification of an arginine residue involved in the binding of glucose 1-phosphate.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't