Amino acid sequence of a peptide containing an essential cysteine residue of pig heart aconitase
| Autor: | Oscar Gawron, Dennis Piszkiewicz, Kyung-Soo Hahm |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Iron-Sulfur Proteins
Chemical Phenomena Swine Peptide Biochemistry Genetics and Molecular Biology (miscellaneous) Aconitase Residue (chemistry) chemistry.chemical_compound Rubredoxin Animals Trypsin Amino Acid Sequence Cysteine Peptide sequence Aconitate Hydratase chemistry.chemical_classification Binding Sites biology Myocardium Rubredoxins Phenacyl bromide Active site Peptide Fragments Chemistry chemistry Biochemistry biology.protein Protein Binding |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure. 667:457-461 |
| ISSN: | 0005-2795 |
| DOI: | 10.1016/0005-2795(81)90211-7 |
| Popis: | Pig heart aconitase reacts with one mole of phenacyl bromide per molecule to give complete inactivation due to the alkylation of a cysteine residue at the active site. A tryptic peptide containing this essential residue has been isolated and its amino acid sequence determined as Ile-Gln-Leu-Leu-Cys ∗-Pro-Leu-Leu-Asn-Gln-Phe-Asp-Lys by manual methods and by the use of an automated solid phase sequencer. There is a limited similarity in amino acid sequence between this peptide and other peptides containing the cysteine residues involved in the binding of the iron-sulfur clusters of high-potential iron-sulfur protein of Rhodopseudomonas gelatinosa and rubredoxins from various bacteria. |
| Databáze: | OpenAIRE |
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