Literature summary for 1.1.2.B2 extracted from

Xia, Z.X.; Dai, W.W.; He, Y.N.; White, S.A.; Mathews, F.S.; Davidson, V.L.
X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i (2003), J. Biol. Inorg. Chem., 8, 843-854.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified enzyme, hanging drop vapor diffusion and macro-seeding, mixing of protein solution containing 5 mg/ml protein, 0.1 M Tris-HCl, pH 8.3, 0.2 M Li2SO4, 30% PEG 3350, with precipitant solution containing 0.1 M Tris-HCl, pH 8.5, 30% PEG 4000, 0.2 M Li2SO4, several days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modelling	Paracoccus denitrificans

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	-	Paracoccus denitrificans

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
methanol + ferricytochrome c551i	Paracoccus denitrificans	the primary electron acceptor of MEDH-PD is cytochrome c-551i	formaldehyde + ferrocytochrome c551i	-	?

Organism

Organism	UniProt	Comment	Textmining
Paracoccus denitrificans	P12293	P12293 (large subunit, alpha) and P12293 (small subunit, beta)	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
methanol + ferricytochrome c551i	the primary electron acceptor of MEDH-PD is cytochrome c-551i	Paracoccus denitrificans	formaldehyde + ferrocytochrome c551i	-	?
additional information	interaction of the enzyme with cytochrome c551i, and electron transfer from reduced pyrroloquinoline quinone to the cytochrome, interface structure, modelling, overview	Paracoccus denitrificans	?	-	?

Synonyms

Synonyms	Comment	Organism
MEDH	-	Paracoccus denitrificans
MEDH-PD	-	Paracoccus denitrificans
methanol dehydrogenase	-	Paracoccus denitrificans

Cofactor

Cofactor	Comment	Organism	Structure
pyrroloquinoline quinone	-	Paracoccus denitrificans

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Release 2023.1 (January 2023)