Linked Life Data

7663423

Source:http://linkedlifedata.com/resource/pubmed/id/7663423

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-10-10
pubmed:abstractText
The interaction of glutamate decarboxylase with the aspartate analogues 3-arsonoalanine and 3-phosphonoalanine, with the glutamate analogues 2-amino-4-arsonobutyric acid and 2-amino-4-phosphonobutyric acid, and with 4-(methylthio)-L-glutamic acid, both as a mixture of diastereoisomers and as the (2S,4R)-form, was studied. All these analogues were poor substrates for the enzyme and only weak inhibitors. Their decarboxylation was accompanied by transamination of the enzyme-bound pyridoxal phosphate (PLP) to pyridoxamine phosphate (PMP), thus inactivating the decarboxylase. With arsonoalanine only part of the PLP was converted into PMP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
77-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The interaction of glutamate decarboxylase from Escherichia coli with substrate analogues modified at C-3 and C-4.
pubmed:affiliation
Engelhardt Institute of Molecular Biology, RAN, Moscow, Russia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't