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 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aldehyde Oxidase
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Aldehyde Oxidoreductases / chemistry
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Aldehyde Oxidoreductases / isolation & purification
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Amino Acid Sequence
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Archaeal Proteins / chemistry
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Archaeal Proteins / isolation & purification
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Biotin / chemistry
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Carboxy-Lyases / chemistry*
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Carboxy-Lyases / isolation & purification
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Chromatography, Gel
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Chromatography, High Pressure Liquid
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Enzyme Stability
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Hydrogen-Ion Concentration
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Indoles / chemistry
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Molecular Sequence Data
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Molecular Weight
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Molybdenum / chemistry*
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Multienzyme Complexes / chemistry*
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Multienzyme Complexes / isolation & purification
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Oxidation-Reduction
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Oxidoreductases / chemistry*
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Oxidoreductases / isolation & purification
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Protein Subunits
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Sequence Analysis, Protein
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Sequence Homology, Amino Acid
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Substrate Specificity
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Sulfolobus / enzymology*
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Temperature
Substances
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Archaeal Proteins
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Indoles
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Multienzyme Complexes
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Protein Subunits
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indolepyruvate - methylviologen oxidoreductase
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indole-3-acetaldehyde
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Biotin
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Molybdenum
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Oxidoreductases
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Aldehyde Oxidoreductases
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Aldehyde Oxidase
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indolepyruvate decarboxylase
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Carboxy-Lyases