Document Detail


Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase.
MedLine Citation:
PMID:  3922356     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Goat mammary fatty acid synthetase was labelled in the acyltransferase domain by formation of O-ester intermediates by incubation with [1-14C]acetyl-CoA and [2-14C]malonyl-CoA. Tryptic-digest and CNBr-cleavage peptides were isolated and purified by high-performance reverse-phase and ion-exchange liquid chromatography. The sequences of the malonyl- and acetyl-labelled peptides were shown to be identical. The results confirm the hypothesis that both acetyl and malonyl groups are transferred to the mammalian fatty acid synthetase complex by the same transferase. The sequence is compared with those of other fatty acid synthetase transferases.
Authors:
J Mikkelsen; P Højrup; M M Rasmussen; P Roepstorff; J Knudsen
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  227     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1985 Apr 
Date Detail:
Created Date:  1985-06-12     Completed Date:  1985-06-12     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  21-7     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acetyl Coenzyme A / pharmacology
Acyltransferases / metabolism*
Amino Acid Sequence
Animals
Binding Sites
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Fatty Acid Synthetase Complex / metabolism*
Female
Goats
Malonyl Coenzyme A / pharmacology
Mammary Glands, Animal / enzymology*
Peptide Fragments / analysis
Serine / analysis
Chemical
Reg. No./Substance:
0/Peptide Fragments; 524-14-1/Malonyl Coenzyme A; 56-45-1/Serine; 72-89-9/Acetyl Coenzyme A; EC 2.3.-/Acyltransferases; EC 6.-/Fatty Acid Synthetase Complex
Comments/Corrections

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