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 |
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 | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.7 | Ca2+ | catalytic, active site-bound | Methylophaga aminisulfidivorans |
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 | - |
? |
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 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.2.7 | native active alpha2beta2 MDH complex by ultracentrifugation, anion echange chromatgraphy, and gel filtration | Methylophaga aminisulfidivorans |
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 | - |
? |
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 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.7 | pyrroloquinoline quinone | - |
Methylophaga aminisulfidivorans |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.1.2.7 | Methylophaga aminisulfidivorans | - |
- |
5.4 |
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 |