Linked Life Data

6712729

Source:http://linkedlifedata.com/resource/pubmed/id/6712729

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1984-5-23
pubmed:abstractText
The mechanism of inactivation by (S)-alpha-fluoromethylhistidine (FMH) of L-histidine decarboxylase (HDC, L-histidine carboxy-lyase, EC 4.1.1.22) purified from whole bodies of fetal rats was studied. FMH inhibited the activities of HDC purified from fetal HDC as well as HDCs from the brain and stomach of adult rats. The activity was not restored by extensive dialysis, indicating that the inhibition was irreversible. The inactivation of HDC was time and concentration dependent and followed pseudo first-order kinetics. L-Histidine, a substrate, protected HDC against inactivation, but D-histidine did not. Apo-HDC was not inactivated by FMH. On labeling of HDC with [3H]FMH, a correlation was found between the extent of incorporation of radioactivity into the enzyme and the degree of inactivation. Two moles of the inhibitor were incorporated into one mole of HDC (108,000 daltons). Experiments with [carboxyl-14C]FMH and [ring 2-14C]FMH showed that decarboxylation was necessary for the inactivation and that one molecule of FMH moiety was incorporated into an HDC monomer during every three decarboxylations of FMH.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
983-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Mechanism of inactivation of mammalian L-histidine decarboxylase by (S)-alpha-fluoromethylhistidine.
pubmed:publicationType
Journal Article