spacer

Overview for MACiE Entry M0099

Version history

General Information

EC Number: 1.1.99.8 (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

Overall Reaction:

Image of acceptor

Image of primary alcohol

right arrow

Image of proton

Image of aldehyde

Image of reduced acceptor

acceptor
C00028
CHEBI:15339
primary alcohol
C00226
CHEBI:15734
2 proton
C00080
CHEBI:24636
aldehyde
C00071
CHEBI:17478
reduced acceptor
C00030
CHEBI:17499

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.


View similar reactions


Stepwise Description of the Reaction

Step 1Asp297 deprotonates the alcohol group of the primary alcohol, which initiates a nucleophilic attack on the C5 of PQQ.
Step 2The oxyanion of PQQ deprotonates Asp297.
Step 3The 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 4In the first step of the reduction of PQQ, a single electron and single proton are lost from the cofactor.
Step 5In the final step of the reduction of PQQ, a single electron and single proton are lost from the cofactor.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Asp 297 A Side Chain

Organic Cofactors for M0099

Type Identity Chain
PQQ PQQ 701 Overview

Metal Cofactors for M0099

Type Het group Number Chain
calcium CA 702 x Overview

References

  1. 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.
    Medline: 9930981
  2. C. Anthony et al. (2003), Biochim. Biophys. Acta, 1647, 18-23. The structure and mechanism of methanol dehydrogenase.
    Medline: 12686102
  3. 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.
    Medline: 15273299

Homologue information for M0099 (1g72)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ
Link to EzCatDB

GOA logo
alcohol dehydrogenase (NAD) activity (molecular function)
calcium ion binding (molecular function)
plasma membrane (cellular component)
methanol metabolic process (biological process)
methanol oxidation (biological process)
membrane (cellular component)
oxidoreductase activity (molecular function)
oxidoreductase activity, acting on CH-OH group of donors (molecular function)
outer membrane-bounded periplasmic space (cellular component)
metal ion binding (molecular function)
oxidation-reduction process (biological process)
spacer
spacer