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Literature summary extracted from

  • Choi, J.M.; Kim, H.G.; Kim, J.S.; Youn, H.S.; Eom, S.H.; Yu, S.L.; Kim, S.W.; Lee, S.H.
    Purification, crystallization and preliminary X-ray crystallographic analysis of a methanol dehydrogenase from the marine bacterium Methylophaga aminisulfidivorans MP(T) (2011), Acta Crystallogr. Sect. F, 67, 513-516.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.2.7 purified native enzyme, hanging drop vapour diffusion method, 8 mg/ml protein in 25 mM Tris-HCl, pH 8.0, mixed with 0.1 M sodium cacodylate pH 6.5, 0.2 M magnesium acetate tetrahydrate and 10% v/v PEG 8000, 20°C, macrocrystals are soaked for 30 s in cryosolution consisting of crystallization solution with 20% v/v glycerol, X-ray diffraction structure determination and analysis at 1.7 A reolution, molecular replacement Methylophaga aminisulfidivorans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.7 periplasm
-
Methylophaga aminisulfidivorans
-
-
1.1.2.7 soluble periplasmic region of the bacterial membrane Methylophaga aminisulfidivorans
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.2.7 Ca2+ catalytic, active site-bound Methylophaga aminisulfidivorans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.2.7 methanol + 2 cytochrome cL Methylophaga aminisulfidivorans
-
formaldehyde + 2 reduced cytochrome cL
-
?
1.1.2.7 methanol + 2 cytochrome cL Methylophaga aminisulfidivorans MPT
-
formaldehyde + 2 reduced cytochrome cL
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.7 Methylophaga aminisulfidivorans A3FJ51 small subunit; genes mxaF and mxaI, encoding the large and small subunit
-
1.1.2.7 Methylophaga aminisulfidivorans MPT A3FJ51 small subunit; genes mxaF and mxaI, encoding the large and small subunit
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.2.7 native active alpha2beta2 MDH complex by ultracentrifugation, anion echange chromatgraphy, and gel filtration Methylophaga aminisulfidivorans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.7 methanol + 2 cytochrome cL
-
Methylophaga aminisulfidivorans formaldehyde + 2 reduced cytochrome cL
-
?
1.1.2.7 methanol + 2 cytochrome cL
-
Methylophaga aminisulfidivorans MPT formaldehyde + 2 reduced cytochrome cL
-
?

Subunits

EC Number Subunits Comment Organism
1.1.2.7 heterotetramer alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits Methylophaga aminisulfidivorans
1.1.2.7 More the alpha-subunit is known to function as the active site for the oxidoreduction reaction, which includes the PQQ group as a redox cofactor and a calcium ion coordinated to vicinal charged and hydrophobic amino-acid residues Methylophaga aminisulfidivorans

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.7 pyrroloquinoline quinone
-
Methylophaga aminisulfidivorans

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.2.7 Methylophaga aminisulfidivorans
-
-
5.4

General Information

EC Number General Information Comment Organism
1.1.2.7 metabolism the electrons released from pyrroloquinoline quinone during the oxidation successively reduce cytochrome cL, cytochrome cH and finally the membrane oxidase cytochrome aa3. As a result of the oxidoreduction pathway, a proton electrochemical gradient is produced around the membrane, which in turn drives the generation of one ATP molecule per molecule of methanol Methylophaga aminisulfidivorans