title: Amino acid sequence of a peptide containing an essential cysteine residue of pig heart aconitase.
abstract: Pig heart aconitase reacts with one mole of phenacyl bromide per molecule to give complete inactivation due to the alkylation of a cysteine reside at the active site. A tryptic peptide containing this essential residue has been isolated and its amino acid sequence determined at 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.
mesh_terms: D000154:Aconitate Hydratase; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D003545:Cysteine; D007506:Iron-Sulfur Proteins; D009206:Myocardium / Q000201:enzymology*; D010446:Peptide Fragments; D011485:Protein Binding; D012416:Rubredoxins; D013552:Swine; D014357:Trypsin
chemical_list: D007506:Iron-Sulfur Proteins; D010446:Peptide Fragments; D012416:Rubredoxins; D014357:Trypsin; D000154:Aconitate Hydratase; D003545:Cysteine