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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
|
pubmed:dateCreated |
1983-10-21
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pubmed:abstractText |
Rabbit mammary fatty acid synthase was labelled in the acyl transferase domain(s) by the formation of the O-ester intermediates after incubation with [14C]acetyl- or malonyl-CoA. Elastase peptides containing the labelled acyl groups were isolated using high performance liquid chromatography and sequenced by fast atom bombardment mass spectrometry. An identical peptide (acyl-Ser-Leu-Gly-Glu-Val-Ala) was obtained after labelling with acetyl- or malonyl-CoA. This confirms the hypothesis that, unlike Escherichia coli or yeast, a single transferase catalyses the transfer of both acetyl- and malonyl-groups in the mammalian complex. The sequence at this site is compared with that around the active serine in other acyl transferases and hydrolases.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
160
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
296-300
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6554204-Acyltransferases,
pubmed-meshheading:6554204-Amino Acid Sequence,
pubmed-meshheading:6554204-Animals,
pubmed-meshheading:6554204-Binding Sites,
pubmed-meshheading:6554204-Fatty Acid Synthetase Complex,
pubmed-meshheading:6554204-Female,
pubmed-meshheading:6554204-Lactation,
pubmed-meshheading:6554204-Mammary Glands, Animal,
pubmed-meshheading:6554204-Pancreatic Elastase,
pubmed-meshheading:6554204-Peptide Fragments,
pubmed-meshheading:6554204-Pregnancy,
pubmed-meshheading:6554204-Rabbits,
pubmed-meshheading:6554204-Species Specificity
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pubmed:year |
1983
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pubmed:articleTitle |
Amino acid sequence around the active serine in the acyl transferase domain of rabbit mammary fatty acid synthase.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|