Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis. - Wikidata - wikimedia - TriplyDB

Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

http://www.wikidata.org/entity/Q42726645

about

An intact eight-membered water chain in drosophilid alcohol dehydrogenases is essential for optimal enzyme activity The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc.Sequences upstream of the homologous cis-elements of the Adh adult enhancer of Drosophila are required for maximal levels of Adh gene transcription in adults of Scaptodrosophila lebanonensis.Functional analysis of a mosquito short-chain dehydrogenase cluster.Structural Insights into the Drosophila melanogaster Retinol Dehydrogenase, a Member of the Short-Chain Dehydrogenase/Reductase Family.Drosophila lebanonensis ADH: analysis of recombinant wild-type enzyme and site-directed mutants. The effect of restoring the consensus sequence in two positions.Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation.The AdhS alleloenzyme of alcohol dehydrogenase from Drosophila melanogaster. Variation of kinetic parameters with pH Drosophila melanogaster alcohol dehydrogenase: product-inhibition studies.Drosophila melanogaster alcohol dehydrogenase. Biochemical properties of the NAD+-plus-acetone-induced isoenzyme conversion Evolution of enzymatic activities of testis-specific short-chain dehydrogenase/reductase in Drosophila.Theoretical calculations of the catalytic triad in short-chain alcohol dehydrogenases/reductases.The catalytic mechanism of Drosophila alcohol dehydrogenase: evidence for a proton relay modulated by the coupled ionization of the active site Lysine/Tyrosine pair and a NAD+ ribose OH switch.Comparative molecular dynamic simulations of wild type and Thr114Val mutated Scaptodrosophila lebanonensis alcohol dehydrogenase.Substrate and inhibitor specificities of the thermostable alcohol dehydrogenase allozymes ADH-71k and ADH-FCh.D. of Drosophila melanogaster.ADH and phylogenetic relationships of Drosophila lebanonesis (Scaptodrosophila).Involvement of the C-terminal tail in the activity of Drosophila alcohol dehydrogenase. Evaluation of truncated proteins constructed by site-directed mutagenesis.Evidence of serine-protease activity closely associated with Drosophila alcohol dehydrogenase.

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P2860

Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

http://www.wikidata.org/entity/Q42726645

description

1986 nî lūn-bûn

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1986年の論文

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1986年論文

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1986年論文

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1986年论文

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1986年论文

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name

Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

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Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

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type

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Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

@en

Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

@nl

prefLabel

Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

@en

Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

@nl

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Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis.

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Gonzalez-Duarte R

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Hovik R

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Juan E

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McKinley-McKee JS

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Winberg JO

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P2860

Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein

Purification and enzyme stability of alcohol dehydrogenase from Drosophila simulans, Drosophila virilis and Drosophila melanogaster adhS.

Secondary-structure prediction from the sequence of Drosophila melanogaster (fruitfly) alcohol dehydrogenase.

Determination of some biochemical and structural features of alcohol dehydrogenases from Drosophila simulans and Drosophila virilis. Comparison of their properties with the Drosophila melanogaster Adhs enzyme.

Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Substrate specificity of the alleloenzymes AdhS and AdhUF.

The contribution of ecological genetics to evolutionary theory: detecting the direct effects of natural selection on particular polymorphic loci.

Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Inhibition studies of the alleloenzymes AdhS and AdhUF.

Alcohol dehydrogenase from Drosophila funebris and Drosophila immigrans: molecular and evolutionary aspects.

Presumptive control mutation for alcohol dehydrogenase in Drosophila melanogaster.

The alcohol dehydrogenase alleloenzymes AdhS and AdhF from the fruitfly Drosophila melanogaster: an enzymatic rate assay to determine the active-site concentration.

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2

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235

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2943270

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