Linked Life Data

391557

Source:http://linkedlifedata.com/resource/pubmed/id/391557

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-3-17
pubmed:abstractText
Active-site peptides of malonyl and palmitoyl transferase from yeast fatty acid synthetase were isolated and sequenced to try to prove the hypothesis [J. Ayling, R. Pirson & F. Lynen (1979) Biochemistry 11, 526--533] that both enzymes are identical. For this purpose synthetase modified with 5,5'-dithiobis(2-nitrobenzoic acid) was labelled with either [14C]malonyl or [14C]palmitoyl residues followed by proteolytic digestion of the labelled protein. [14C]Malonyl-peptides were isolated by conventional purification procedures; their structures were determined by a combination of methods. [14C]Palmitoyl-peptide material was purified by high-performance liquid chromatography and the structure determined by solid-phase Edman degradation and other analytical methods. Serine was identified as the acyl acceptor group in both transferases. Comparison of the sequence data available shows that the sequence around the acyl acceptor group in both cases is identical. This proves the identity of malonyl and palmitoyl transferase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
101
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
413-22
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Identity of malonyl and palmitoyl transferase of fatty acid synthetase from yeast. 2. A comparison of active-site peptides.
pubmed:publicationType
Journal Article