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J. Biochem, 1986, Vol. 99, No. 5 1289-1298
© 1986 Japanese Biochemical Society


research-article

Amino Acid Sequence of Copper, Zinc-Superoxide Dimutase from Spinach Leaves

Yasuyuki KITAGAWA*, Susumu TSUNASAWA*, Nobuo TANAKA*, Yukiteru KATSUBE*, Fumio SAKIYAMA* and Kozi ASADA**

*Institute for Protein Research, Osaka Universtiy Suita, Osaka 565
**Research Institute for Food Science, Kyoto University Uji, Kyoto 611

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.


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