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Article

Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion.

The Biochemical journal - 1 Nov 1992

Richardson I W, Anthony C

Abstract excerpt

Methanol dehydrogenase (MDH) from Methylobacterium extorquens, Methylophilus methylotrophus, Paracoccus denitrificans and Hyphomicrobium X all contained a single atom of Ca2+ per alpha 2 beta 2 tetramer. The role of Ca2+ was investigated using the MDH from Methylobacterium extorquens. This was shown to be similar to the MDH from Hyphomicrobium X in having 2 mol of prosthetic group (pyrroloquinoline quinine; PQQ)...

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Identifiers

PMID: 1332681
DOI: 10.1042/bj2870709
PMCID: PMC1133066

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Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion.PMID 1332681Read ↗

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Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L).Semantic proximity Read ↗

Identification of a magnesium-dependent NAD(P)(H)-binding domain in the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus.Semantic proximity Read ↗

Mutants of Methylobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesise the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan-tryptophylquinone group.Semantic proximity Read ↗

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