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Expression, crystallization and preliminary X-ray crystallographic analysis of alcohol dehydrogenase (ADH) from Kangiella koreensis.

ABSTRACT: Alcohol dehydrogenases (ADHs) are a group of dehydrogenase enzymes that facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of NAD(+) to NADH. In bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD(+). The adh gene from Kangiella koreensis was cloned and the protein (KkADH) was expressed, purified and crystallized. A KkADH crystal diffracted to 2.5?Å resolution and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 94.1, b = 80.9, c = 115.6?Å, ? = 111.9°. Four monomers were present in the asymmetric unit, with a corresponding VM of 2.55?Å(3)?Da(-1) and a solvent content of 51.8%.

SUBMITTER: Ngo HP

PROVIDER: S-EPMC3758158 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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Expression, crystallization and preliminary X-ray crystallographic analysis of alcohol dehydrogenase (ADH) from Kangiella koreensis.

Ngo Ho-Phuong-Thuy HP Hong Seung-Hye SH Hong Myoung-Ki MK Pham Tan-Viet TV Oh Deok-Kun DK Kang Lin-Woo LW

Acta crystallographica. Section F, Structural biology and crystallization communications 20130821 Pt 9

Alcohol dehydrogenases (ADHs) are a group of dehydrogenase enzymes that facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of NAD(+) to NADH. In bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD(+). The adh gene from Kangiella koreensis was cloned and the protein (KkADH) was expressed, purified and crystallized. A KkADH crystal diffracted to 2.5 Å resolution and belonged to the ...[more]

PMID: 23989158

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