Amino acid sequence of a peptide containing an essential cysteine residue of pig heart aconitase.
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.
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
D007506:Iron-Sulfur Proteins; D010446:Peptide Fragments; D012416:Rubredoxins; D014357:Trypsin; D000154:Aconitate Hydratase; D003545:Cysteine