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Literature summary for 1.1.1.80 extracted from

  • Peretz, M.; Bogin, O.; Keinan, E.; Burstein, Y.
    Stereospecificity of hydrogen transfer by the NADP-linked alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii (1993), Int. J. Pept. Protein Res., 42, 490-495.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Thermoanaerobacter brockii P14941
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme transfers the pro-R hydrogen from the pyridine 4 position of the reduced coenzyme. This stereospecificity is stable over a broad range of temperatures up to 70°C and different concentrations of the coenzyme (catalytic or stoichiometric). NADP+ and its synthetic analogs, 3-acetylpyridine-ADP+ and thio-NADP+, can be used successfully Thermoanaerobacter brockii ?
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Cofactor

Cofactor Comment Organism Structure
additional information no cofactor: NADH Thermoanaerobacter brockii
NADPH enzyme transfers the pro-R hydrogen from the pyridine 4 position of the reduced coenzyme. This stereospecificity is stable over a broad range of temperatures up to 70°C and different concentrations of the coenzyme (catalytic or stoichiometric) Thermoanaerobacter brockii