| Literature DB >> 23989158 |
Ho-Phuong-Thuy Ngo1, Seung-Hye Hong, Myoung-Ki Hong, Tan-Viet Pham, Deok-Kun Oh, Lin-Woo Kang.
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, β = 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%.Entities:
Keywords: ADH; Kangiella koreensis; alcohol dehydrogenase
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Year: 2013 PMID: 23989158 PMCID: PMC3758158 DOI: 10.1107/S1744309113022008
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091