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.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Arfman N,de Vries KJ,Moezelaar HR,Attwood MM,Robinson GK,van Geel M,Dijkhuizen Ldoi
10.1007/BF00245161keywords:
subject
Has Abstractpub_date
1992-01-01 00:00:00pages
272-8issue
3eissn
0302-8933issn
1432-072Xjournal_volume
157pub_type
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pub_type： 杂志文章,评审
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