dehydrogenase from Methylobacterium extorquens
نویسندگان
چکیده
The structure of methanol dehydrogenase (MDH) at 0.194 nm (1.94 A) has been used to provide a model structure for part of a membrane quinoprotein glucose dehydrogenase (GDH). The basic superbarrel structure is retained, along with the tryptophandocking motifs. The active-site regions are similar, but there are important differences, the most important being that GDH lacks the novel disulphide ring structure formed from adjacent cysteines in MDH; in GDH the equivalent region is occupied by His-262. Because of the overall similarities in the active-site region, the mechanism of action of GDH is likely to be similar to that of
منابع مشابه
The 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.
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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.
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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...
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Ten novel methylotrophy genes of the facultative methylotroph Methylobacterium extorquens AM1 were identified from a transposon mutagenesis screen. One of these genes encodes a product having identity with dihydrofolate reductase (DHFR). This mutant has a C(1)-defective and methanol-sensitive phenotype that has previously only been observed for strains defective in tetrahydromethanopterin (H(4)...
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