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Novel types of two‐domain multi‐copper oxidases: possible missing links in the evolution
Author(s) -
Nakamura Kensuke,
Kawabata Takeshi,
Yura Kei,
Go Nobuhiro
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01000-7
Subject(s) - ceruloplasmin , copper , nitrite reductase , oxidase test , domain (mathematical analysis) , chemistry , copper protein , biochemistry , metalloprotein , lysyl oxidase , enzyme , nitrate reductase , mathematical analysis , mathematics , organic chemistry
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.