PMID: 3383846Jun 1, 1988Paper

NADH oxidase from the extreme thermophile Thermus aquaticus YT-1. Purification and characterisation

European Journal of Biochemistry
D CoccoJ V Bannister

Abstract

A protein with NADH oxidase activity from the extreme thermophile Thermus aquaticus YT-1 was purified and characterised. The enzyme was found to have a relative molecular mass of 110,000 and be composed of two subunits of identical size. FAD was found to be present at a concentration of 0.7 mol/mol dimer and was required for activity. During the oxidation of NADH, oxygen uptake takes place with the production of hydrogen peroxide. The enzyme had, with the exception of a higher glutamic acid and tryptophan content, a similar amino acid composition as the NADH oxidase isolated from the mesophile Bacillus megaterium. Purified NADH oxidase was found to have a Km of 39 microM for beta-NADH and a Vmax of 4.68 mumol NADH mg-1 min-1 and was still active at 95 degrees C. Enzymatic activity was found to be independent of pH between 5.0 and 10.5.

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Citations

Dec 2, 1994·Journal of Immunological Methods·D Athey, C J McNeil
Dec 1, 1995·Nature Structural Biology·H J HechtR D Schmid
Sep 30, 2000·European Journal of Biochemistry·L B PooleM Li Calzi
Jan 9, 2007·Biochemical and Biophysical Research Communications·Kazuteru Aoki, Tateo Itoh
Nov 29, 1996·The Journal of Biological Chemistry·Y Niimura, V Massey
Oct 1, 1996·European Journal of Biochemistry·D M BrownP Upcroft
Apr 19, 1996·The Journal of Biological Chemistry·R KatoS Kuramitsu
Mar 3, 1998·Biochemical and Biophysical Research Communications·C M Gomes, M Teixeira
May 1, 1993·Journal of Bacteriology·T B Stanton, N S Jensen

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