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A novel bifunctional molybdo‐enzyme catalyzing both decarboxylation of indolepyruvate and oxidation of indoleacetaldehyde from a thermoacidophilic archaeon, Sulfolobus sp. strain 7
Author(s) -
Wakagi Takayoshi,
Fukuda Eriko,
Ogawa Yoko,
Kino Hiroyasu,
Matsuzawa Hiroshi
Publication year - 2002
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(01)03259-8
Subject(s) - decarboxylation , enzyme , thiamine pyrophosphate , phosphofructokinase 2 , biochemistry , cofactor , chemistry , strain (injury) , oxidative decarboxylation , protein subunit , stereochemistry , biology , catalysis , gene , anatomy
An enzyme, which catalyzes both decarboxylation of indolepyruvate and subsequent oxidation of indoleacetaldehyde into indoleacetate, was purified from a thermoacidophilic archaeon, Sulfolobus sp. strain 7. The enzyme showed a M r of 280 kDa on gel filtration and was composed of three subunits (a, 89; b, 30; and c, 19 kDa), possibly in a stoichiometry of 2:2:2. Mo and Fe were detected. Thiamine pyrophosphate was absent. Biotin was suggested to bind to the b‐subunit. The first step, the decarboxylation reaction, was specific for 2‐oxoacids with an aromatic group, while in the second reaction, various aldehydes including glyceraldehyde, which is a glycolytic intermediate in the organism, were oxidized.