CATH Classification

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 P16027
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)

P16027
DHM1_METEA
Methylorubrum extorquens AM1
Methanol dehydrogenase [cytochrome c] subunit 1

PDB Structure

PDB 1H4J
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Site-Directed Mutagenesis and X-Ray Crystallography of the Pqq-Containing Quinoprotein Methanol Dehydrogenase and its Electron Acceptor, Cytochrome C(L)(,)
Afolabi, P.R., Mohammed, F., Amaratunga, K., Majekodunmi, O., Dales, S.L., Gill, R., Thompson, D., Cooper, J.B., Wood, S.P., Goodwin, P.M., Anthony, C.
Biochemistry