Linked Life Data

6749853

Source:http://linkedlifedata.com/resource/pubmed/id/6749853

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1982-12-3
pubmed:abstractText
A covalently linked pyruvoyl group is essential for the enzymatic activity of S-adenosylmethionine decarboxylase from Escherichia coli. A rapid purification method based on affinity chromatography is described for the isolation of this enzyme from an E. coli K12 strain which contains a plasmid containing the structural gene for S-adenosylmethionine decarboxylase, and which overproduces this enzyme. The purified enzyme contains one pyruvate moiety on each of six subunits. The enzyme is inactivated by incubation with carbonyl group reagents such as NaBH4 and phenylhydrazine; after inactivation, 1 mol of lactate or 1 mol of phenylhydrazone is found/mol of enzyme subunit. The enzyme is also inactivated by NaCNBH3 but only in the presence of either substrate or product and the divalent metal ion activator Mg2+; inactivation is accompanied by incorporation of 1 mol of the product, decarboxylated adenosylmethionine, per mol of enzyme subunit, suggesting that the pyruvoyl group participates in catalysis by formation of a Schiff base with the substrate. Equilibrium dialysis studies indicated a single substrate (or product) binding site/enzyme subunit.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12063-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
S-adenosylmethionine decarboxylase of Escherichia coli. Studies on the covalently linked pyruvate required for activity.
pubmed:publicationType
Journal Article