| Literature DB >> 3383846 |
D Cocco1, A Rinaldi, I Savini, J M Cooper, J 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.Entities:
Mesh：
Substances：
Year: 1988 PMID： 3383846 DOI： 10.1111/j.1432-1033.1988.tb14093.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956