A novel bifunctional molybdo‐enzyme catalyzing both decarboxylation of indolepyruvate and oxidation of indoleacetaldehyde from a thermoacidophilic archaeon, Sulfolobus sp. strain 7

FEBS Letters

Wakagi, Takayoshi¹  Matsuzawa, Hiroshi²  Kino, Hiroyasu¹  Ogawa, Yoko¹  Fukuda, Eriko¹ 

[1] Department of Biotechnology, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan;Department of Bioscience and Biotechnology, Aomori University, 2-3-1 Kohbata, Aomori 030-0943, Japan

关键词: Indolepyruvate;    Indolealdehyde;    Decarboxylase;    Oxidoreductase;    Archaeon;    OOR;    2-oxoacid:ferredoxin oxidoreductase;    POR;    pyruvate:ferredoxin oxidoreductase;    KOR;    2-oxoglutarate(α-ketoglutarate):ferredoxin oxidoreductase;    VOR;    isovalerate:ferredoxin oxidoreductase;    IOR;    indolepyruvate:ferredoxin oxidoreductase;    IMOR;    indolepyruvate:methylviologen oxidoreductase;    IAA;    indole-3-acetic acid;    IPyA;    indolepyruvic acid;    indole-3-pyruvic acid;    IAAld;    indole-3-acetaldehyde;    DCPIP;    dichlorophenolindophenol;    MV;    methylviologen;    TPP;    thiamine pyrophosphate;   

DOI  :  10.1016/S0014-5793(01)03259-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown