Biochemical characterization of ethanol-dependent reduction of furfural by alcohol dehydrogenases.

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2011 nî lūn-bûn

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年學術文章

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2011年學術文章

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2011年學術文章

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name

Biochemical characterization o ...... ral by alcohol dehydrogenases.

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Biochemical characterization o ...... ral by alcohol dehydrogenases.

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Biochemical characterization o ...... ral by alcohol dehydrogenases.

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Biochemical characterization o ...... ral by alcohol dehydrogenases.

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Biochemical characterization o ...... ral by alcohol dehydrogenases.

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Biochemical characterization o ...... ral by alcohol dehydrogenases.

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P1476

Biochemical characterization o ...... ral by alcohol dehydrogenases.

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P2093

L K Metthew Lam

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Luying Xun

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Qunrui Li

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Clustal W and Clustal X version 2.0

Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family.

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Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction

Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes.

Aldehyde sources, metabolism, molecular toxicity mechanisms, and possible effects on human health.

The alcohol dehydrogenases of Saccharomyces cerevisiae: a comprehensive review.

Multiple gene-mediated NAD(P)H-dependent aldehyde reduction is a mechanism of in situ detoxification of furfural and 5-hydroxymethylfurfural by Saccharomyces cerevisiae.

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10.1007/S10532-011-9477-X

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2011-04-28T00:00:00Z

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