UNSPECIFIED (2004) Formaldehyde dehydrogenase preparations from Methylococcus capsulatus (Bath) comprise methanol dehydrogenase and methylene tetrahydromethanopterin dehydrogenase. MICROBIOLOGY-SGM, 150 (Part 3). pp. 707-713. ISSN 1350-0872

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Abstract

In methylotrophic bacteria, formaldehyde is an important but potentially toxic metabolic intermediate that can be assimilated into biomass or oxidized to yield energy. Previously reported was the purification of an NAD(P)(+) -dependent formaldehyde dehydrogenase (FDH) from the obligate methane-oxidizing methylotroph Methylococcus capsulatus (Bath), presumably important in formaldehyde oxidation, which required a heat-stable factor (known as the modifin) for FDH activity. Here, the major protein component of this FDH preparation was shown by biophysical techniques to comprise subunits of 64 and 8 kDa in an alpha(2)beta(2) arrangement. N-terminal sequencing of the subunits of FDH, together with enzymological characterization, showed that the (02 tetramer was a quinoprotein methanol dehydrogenase of the type found in other methylotrophs. The FDH preparations were shown to contain a highly active NAD(P)(+)-dependent methylene tetrahydromethanopterin dehydrogenase that was the probable source of the NAD(P)(+) -dependent formaldehyde oxidation activity. These results support previous findings that methylotrophs possess multiple pathways for formaldehyde dissimilation.

Item Type:	Journal Article
Subjects:	Q Science > QR Microbiology
Journal or Publication Title:	MICROBIOLOGY-SGM
Publisher:	SOC GENERAL MICROBIOLOGY
ISSN:	1350-0872
Date:	March 2004
Volume:	150
Number:	Part 3
Number of Pages:	7
Page Range:	pp. 707-713
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/8628

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