A novel bifunctional molybdo-enzyme catalyzing both decarboxylation of indolepyruvate and oxidation of indoleacetaldehyde from a thermoacidophilic archaeon, Sulfolobus sp. strain 7 |
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Authors: | Takayoshi Wakagi Eriko Fukuda Yoko Ogawa Hiroyasu Kino Hiroshi Matsuzawa |
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Institution: | Department of Biotechnology, The University of Tokyo, Japan. atwakag@mail.ecc.u-tokyo.ac.jp |
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Abstract: | 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 Mr 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. |
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Keywords: | Indolepyruvate Indolealdehyde Decarboxylase Oxidoreductase Archaeon |
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