Overview for MACiE Entry M0099
EC Number: 188.8.131.52 (A member of the Oxidoreductases, Acting on the CH-OH group of donors, With other acceptors)
Enzyme Name: quinoprotein alcohol dehydrogenase
Biological Species: Methylophilus methylotrophus (Bacteria)
Catalytic Chain UniprotKB Accession Codes:
- P38539 - Methanol dehydrogenase [cytochrome c] subunit 1
Representative PDB Code: 1g72 - CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: ATHEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION (Resolution = 1.90 Å).
Catalytic CATH Codes:
"Other" CATH Codes:
Display structure information
It is unknown whether this reaction is reversible or not.
Overall Comment: A second mechanism to the addition/elimination, involving a hydride transfer, has been proposed from molecular dynamics calculations.
This mechanism employs Glu171 as a general base at the alcohol substrate, removing the hydroxyl proton and initiating hydride transfer from the alpha carbon to the C5 carbonyl of PQQ.
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Stepwise Description of the Reaction
|Step 1||Asp297 deprotonates the alcohol group of the primary alcohol, which initiates a nucleophilic attack on the C5 of PQQ.|
|Step 2||The oxyanion of PQQ deprotonates Asp297.|
|Step 3||The oxygen of the PQQ C6 carbonyl group abstracts a proton from the bound primary alcohol, eliminating the reduced PQQ and forming the aldehyde product.|
|Step 4||In the first step of the reduction of PQQ, a single electron and single proton are lost from the cofactor.|
|Step 5||In the final step of the reduction of PQQ, a single electron and single proton are lost from the cofactor.|
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Catalytic Residues Involved
||Location of Function
Organic Cofactors for M0099
Metal Cofactors for M0099
- Z. X. Xia et al. (1999), Biochemistry, 38, 1214-1220. Detailed active site configuration of a new crystal form of methanol dehydrogenase from Methylophilus W3A1 at 1.9 A resolution.
- C. Anthony et al. (2003), Biochim. Biophys. Acta, 1647, 18-23. The structure and mechanism of methanol dehydrogenase.
- S.Y. Reddy et al. (2004), Protein Sci., 13, 1965-78. Determination of enzyme mechanisms by molecular dynamics: studies on quinoproteins, methanol dehydrogenase, and soluble glucose dehydrogenase.
Homologue information for M0099 (1g72)
MACiE Homologues (within the PDB)
MACiE Homologues (within UniprotKB/SwissProt)
Links to this entry in other databases