CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.140 | 8 Propeller |
|
2.140.10 | Methanol Dehydrogenase; Chain A |
|
2.140.10.10 | Quinoprotein alcohol dehydrogenase-like superfamily |
Domain Context
CATH Clusters
| Superfamily | Quinoprotein alcohol dehydrogenase-like superfamily |
| Functional Family |
Enzyme Information
| 1.1.2.7 |
Methanol dehydrogenase (cytochrome c).
based on mapping to UniProt P38539
A primary alcohol + 2 cytochrome c(L) = an aldehyde + 2 reduced cytochrome c(L) + 2 H(+).
-!- A periplasmic quinoprotein alcohol dehydrogenase that only occurs in methylotrophic bacteria. -!- It uses the novel specific cytochrome c(L) as acceptor. -!- Acts on a wide range of primary alcohols, including ethanol, duodecanol, chloroethanol, cinnamyl alcohol, and also formaldehyde. -!- Activity is stimulated by ammonia or methylamine. -!- It is usually assayed with phenazine methosulfate. -!- Like all other quinoprotein alcohol dehydrogenases it has an 8-bladed 'propeller' structure, a calcium ion bound to the PQQ in the active site and an unusual disulfide ring structure in close proximity to the PQQ. -!- It differs from EC 1.1.2.8, alcohol dehydrogenase (cytochrome c), in having a high affinity for methanol and in having a second essential small subunit (no known function). -!- Formerly EC 1.1.99.8.
|
UniProtKB Entries (1)
| P38540 |
DHM2_METME
Methylophilus methylotrophus
Methanol dehydrogenase [cytochrome c] subunit 2
|
PDB Structure
| PDB | 1G72 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation.
Proc.Natl.Acad.Sci.USA
|
