Linked Life Data

1599467

Source:http://linkedlifedata.com/resource/pubmed/id/1599467

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-7-9
pubmed:abstractText
Incubation of Escherichia coli 5-enolpyruvylshikimate 3-phosphate synthase with its substrate analogue pyruvate in the presence of sodium cyanoborohydride resulted in a significant decrease in its enzyme activity. The inactivation followed pseudo-first order and saturation kinetics with a Kinact of 16.12 mM and a maximum rate of constant of 0.046 min-1. The inactivation was specifically prevented by preincubation of the enzyme with a combination of the substrate shikimate 3-phosphate plus competitive inhibitor glyphosate. Upon 90% inactivation, approximately 1 mole of [14C]-label from [14C]-pyruvate was incorporated per mole of enzyme. Tryptic mapping of the modified enzyme as well as analysis of an isolated radioactive peptide indicated that Lys22 was the modified site. The results suggested that pyruvate inactivated the enzyme by forming a Schiff-base with Lys22 at the enzyme's active site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
185
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
317-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Inactivation of 5-enolpyruvylshikimate 3-phosphate synthase by its substrate analogue pyruvate in the presence of sodium cyanoborohydride.
pubmed:affiliation
Department of Protein Biochemistry, Monsanto Company, St. Louis, MO 63198.
pubmed:publicationType
Journal Article