title: Amino acid sequence of copper,zinc-superoxide dismutase from spinach leaves.
abstract: The complete amino acid sequence of Cu,Zn-superoxide dismutase (SOD) from spinach leaves has been determined on the basis of peptides obtained by cyanogen bromide (BrCN) cleavage and by enzymic hydrolyses with Achromobacter lyticus lysylendopeptidase, Staphylococcus aureus V8 protease, trypsin, and thermolysin. The spinach SOD consists of a total of 154 amino acid residues with alanine as the amino(N)-terminus and valine as the carboxy(C-)terminus. The present sequence, which has been established for the enzyme from a plant, is also highly homologous to those of the enzymes from other species. Especially, the residues essential for metal binding and enzyme activity have been extensively conserved among all of the Cu,Zn-SODs hitherto analyzed.
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D004175:Diptera; D005399:Fishes; D006736:Horses; D006801:Humans; D006868:Hydrolysis; D010447:Peptide Hydrolases; D010944:Plants / Q000201:enzymology*; D012441:Saccharomyces cerevisiae; D013045:Species Specificity; D013482:Superoxide Dismutase / Q000302:isolation & purification
chemical_list: D013482:Superoxide Dismutase; D010447:Peptide Hydrolases; D003488:Cyanogen Bromide