ATP-dependent Saccharomyces cerevisiae phospho enol pyruvate carboxykinase: isolation and sequence of a peptide containing a highly reactive cysteine
| Autor: | Steven P. Latshaw, M.Victoria Encinas, Emilio Cardemil, Marysol Alvear, Robert G. Kemp |
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| Rok vydání: | 1992 |
| Předmět: |
Macromolecular Substances
Saccharomyces cerevisiae Molecular Sequence Data Trypanosoma brucei brucei Biophysics Peptide Biochemistry Adenosine Triphosphate Naphthalenesulfonates Structural Biology Sequence Homology Nucleic Acid medicine Escherichia coli Animals Amino Acid Sequence Cysteine Molecular Biology Fluorescent Dyes chemistry.chemical_classification Edman degradation biology Protein primary structure biology.organism_classification Trypsin Peptide Fragments Amino acid Rats Kinetics Spectrometry Fluorescence chemistry Phosphoenolpyruvate Carboxykinase (GTP) Phosphoenolpyruvate carboxykinase medicine.drug |
| Zdroj: | Biochimica et biophysica acta. 1119(1) |
| ISSN: | 0006-3002 |
| Popis: | Saccharomyces cerevisiae phospho enol pyruvate carboxykinase (EC 4.1.1.49), inactivated by N-(iodoacetyl)-N'-(5-sulfo-1-naphthyl)ethylenediamine, incorporated 0.95 mol of the fluorescent moiety per mol of enzyme subunit. Reagent incorporation was completely protected by the presence of ADP plus MnCl2. The labeled protein was digested with trypsin after carboxymethylation. Two labeled peptides were isolated by reverse-phase high-performance liquid chromatography and were sequenced by gas-phase automatic Edman degradation. Both peptides contained overlapping amino acid sequences from Asn-358 to Lys-375, thus identifying Cys-364 as the reactive amino acid residue. The position of the target amino acid residue is immediately preceding a putative phosphoryl-binding sequence proposed for some nucleotide-binding proteins. |
| Databáze: | OpenAIRE |
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