Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase
| Autor: | Peter Højrup, J Mikkelsen, M M Rasmussen, Jens Knudsen, Peter Roepstorff |
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| Jazyk: | angličtina |
| Rok vydání: | 1985 |
| Předmět: |
Serine/analysis
Biology Biochemistry Peptide Fragments/analysis Fatty Acid Synthases/metabolism Serine Residue (chemistry) Mammary Glands Animal Acetyl Coenzyme A Transferase Animals Amino Acid Sequence Molecular Biology Peptide sequence Chromatography High Pressure Liquid chemistry.chemical_classification Binding Sites Goats Protein primary structure Fatty acid Cell Biology Chromatography Ion Exchange Peptide Fragments Malonyl Coenzyme A/pharmacology Malonyl Coenzyme A Mammary Glands Animal/enzymology Enzyme chemistry Acyltransferase Acyltransferases/metabolism Female Fatty Acid Synthases Acyltransferases Acetyl Coenzyme A/pharmacology Research Article |
| Zdroj: | Mikkelsen, J, Højrup, P, Rasmussen, M M, Roepstorff, P & Knudsen, J 1985, ' Amino acid sequence around the active-site serine residue in the acyltransferase domain of goat mammary fatty acid synthetase ', The Biochemical journal, vol. 227, no. 1, pp. 21-27 . https://doi.org/10.1042/bj2270021 |
| DOI: | 10.1042/bj2270021 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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