The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1.
نویسندگان
چکیده
The nucleotide and deduced amino acid sequence of a novel small (beta) subunit of methanol dehydrogenase of Methylobacterium extorquens AM1 (previously Pseudomonas AM1) has been determined. Work with the whole protein has shown that is has an alpha 2 beta 2 configuration.
منابع مشابه
Functional investigation of methanol dehydrogenase-like protein XoxF in Methylobacterium extorquens AM1.
Methanol dehydrogenase-like protein XoxF of Methylobacterium extorquens AM1 exhibits a sequence identity of 50 % to the catalytic subunit MxaF of periplasmic methanol dehydrogenase in the same organism. The latter has been characterized in detail, identified as a pyrroloquinoline quinone (PQQ)-dependent protein, and shown to be essential for growth in the presence of methanol in this methylotro...
متن کاملThe small-subunit polypeptide of methylamine dehydrogenase from Methylobacterium extorquens AM1 has an unusual leader sequence.
The nucleotide sequence for the N-terminal region of the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1 has revealed a leader sequence that is unusual in both its length and composition. Gene fusions to lacZ and phoA show that this leader sequence does not function in Escherichia coli but does function in M. extorquens AM1.
متن کاملA Catalytic Role of XoxF1 as La3+-Dependent Methanol Dehydrogenase in Methylobacterium extorquens Strain AM1
In the methylotrophic bacterium Methylobacterium extorquens strain AM1, MxaF, a Ca(2+)-dependent methanol dehydrogenase (MDH), is the main enzyme catalyzing methanol oxidation during growth on methanol. The genome of strain AM1 contains another MDH gene homologue, xoxF1, whose function in methanol metabolism has remained unclear. In this work, we show that XoxF1 also functions as an MDH and is ...
متن کاملXoxF is required for expression of methanol dehydrogenase in 1 Methylobacterium extorquens AM 1 2 3
XoxF is required for expression of methanol dehydrogenase in 1 Methylobacterium extorquens AM1 2 3 Elizabeth Skovran, Alexander D. Palmer, Austin M. Rountree, Nathan M. Good and 4 Mary E. Lidstrom 5 Department of Chemical Engineering and Department of Microbiology 6 University of Washington 7 Seattle, WA 98195-2180 8 9 Submission Date: 5-20-11 10 11 12 * Corresponding author: Mailing address: 6...
متن کاملMultiple formate dehydrogenase enzymes in the facultative methylotroph Methylobacterium extorquens AM1 are dispensable for growth on methanol.
Formate dehydrogenase has traditionally been assumed to play an essential role in energy generation during growth on C(1) compounds. However, this assumption has not yet been experimentally tested in methylotrophic bacteria. In this study, a whole-genome analysis approach was used to identify three different formate dehydrogenase systems in the facultative methylotroph Methylobacterium extorque...
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ورودعنوان ژورنال:
- The Biochemical journal
دوره 260 3 شماره
صفحات -
تاریخ انتشار 1989