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Literature summary for 1.1.2.7 extracted from
- The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens (1995), Biochem. J., 308, 375-379.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structure analysis | Methylorubrum extorquens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| periplasm | - |
Methylorubrum extorquens | - |
- |
| soluble | - |
Methylorubrum extorquens | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | one molecule per enzyme alpha-subunit, binding involves Glu177 and Asn261, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism | Methylorubrum extorquens |  |
| Fe2+ | a cytochrome protein | Methylorubrum extorquens | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 66000 | - |
4 * 66000, alpha2beta2, crystal structure | Methylorubrum extorquens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Methylorubrum extorquens | MDH is a soluble periplasmic enzyme, having cytochrome CL as electron acceptor, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methylorubrum extorquens | P16027 and P14775 | P16027 (large subunit, alpha) and P14775 (small subunit, beta) | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | MDH is a soluble periplasmic enzyme, having cytochrome CL as electron acceptor, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism, overview | Methylorubrum extorquens | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | 4 * 66000, alpha2beta2, crystal structure | Methylorubrum extorquens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MDH | - |
Methylorubrum extorquens |
| methanol dehydrogenase | - |
Methylorubrum extorquens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome cL | - |
Methylorubrum extorquens | |
| additional information | an NAD(P)-independent enzyme | Methylorubrum extorquens | |
| pyrroloquinoline quinone | PQQ, one molecule per enzyme alpha-subunit. The PQQ ring is sandwiched between the indole ring of Trp243 and the two sulphur atoms of the disulfide ring structure | Methylorubrum extorquens | |
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Release 2023.1 (January 2023)
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