An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral form of ceruloplasmin and ascorbate oxidase. A possible evolutionary relationship of these proteins is proposed. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
机构:
Loma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USALoma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USA
Alexandre, G
;
Zhulin, IB
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机构:
Loma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USALoma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USA
机构:
Loma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USALoma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USA
Alexandre, G
;
Zhulin, IB
论文数: 0引用数: 0
h-index: 0
机构:
Loma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USALoma Linda Univ, Sch Med, Dept Microbiol & Mol Genet, Loma Linda, CA 92350 USA