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

Authors
  • Ngo, Ho-Phuong-Thuy
  • Hong, Seung-Hye
  • Hong, Myoung-Ki
  • Pham, Tan-Viet
  • Oh, Deok-Kun
  • Kang, Lin-Woo
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Publisher
International Union of Crystallography
Publication Date
Sep 01, 2013
Volume
69
Issue
Pt 9
Pages
1037–1040
Identifiers
DOI: 10.1107/S1744309113022008
PMID: 23989158
Source
Medline
Keywords
License
Unknown

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%.

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