title: Environmental regulation of alcohol metabolism in thermotolerant methylotrophic Bacillus strains.
abstract: The thermotolerant methylotroph Bacillus sp. C1 possesses a novel NAD-dependent methanol dehydrogenase (MDH), with distinct structural and mechanistic properties. During growth on methanol and ethanol, MDH was responsible for the oxidation of both these substrates. MDH activity in cells grown on methanol or glucose was inversely related to the growth rate. Highest activity levels were observed in cells grown on the C1-substrates methanol and formaldehyde. The affinity of MDH for alcohol substrates and NAD, as well as Vmax, are strongly increased in the presence of a Mr 50,000 activator protein plus Mg(2+)-ions [Arfman et al. (1991) J Biol Chem 266: 3955-3960]. Under all growth conditions tested the cells contained an approximately 18-fold molar excess of (decameric) MDH over (dimeric) activator protein. Expression of hexulose-6-phosphate synthase (HPS), the key enzyme of the RuMP cycle, was probably induced by the substrate formaldehyde. Cells with high MDH and low HPS activity levels immediately accumulated (toxic) formaldehyde when exposed to a transient increase in methanol concentration. Similarly, cells with high MDH and low CoA-linked NAD-dependent acetaldehyde dehydrogenase activity levels produced acetaldehyde when subjected to a rise in ethanol concentration. Problems frequently observed in establishing cultures of methylotrophic bacilli on methanol- or ethanol-containing media are (in part) assigned to these phenomena.
authors.affiliation: Department of Microbiology, University of Groningen, Haren, The Netherlands.
authors.forename: N
authors.initials: N
authors.lastname: Arfman
authors.forename: K J
authors.initials: KJ
authors.lastname: de Vries
authors.forename: H R
authors.initials: HR
authors.lastname: Moezelaar
authors.forename: M M
authors.initials: MM
authors.lastname: Attwood
authors.forename: G K
authors.initials: GK
authors.lastname: Robinson
authors.forename: M
authors.initials: M
authors.lastname: van Geel
authors.forename: L
authors.initials: L
authors.lastname: Dijkhuizen
mesh_terms: D000426:Alcohol Dehydrogenase / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000438:Alcohols / Q000378:metabolism*; D000444:Aldehyde Dehydrogenase / Q000378:metabolism; D000446:Aldehyde-Lyases / Q000378:metabolism; D001407:Bacillus / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D002455:Cell Division; D003065:Coenzyme A / Q000378:metabolism; D000431:Ethanol / Q000378:metabolism; D005557:Formaldehyde / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D005947:Glucose / Q000378:metabolism; D006358:Hot Temperature; D000432:Methanol / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D000438:Alcohols; D001426:Bacterial Proteins; D005557:Formaldehyde; D000431:Ethanol; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; C019641:alcohol dehydrogenase (acceptor); D000444:Aldehyde Dehydrogenase; D000446:Aldehyde-Lyases; C021355:hexose phosphate synthetase; D005947:Glucose; D003065:Coenzyme A; D000432:Methanol