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Overview for MACiE Entry M0105

Version history

General Information

EC Number: 1.2.3.1 (A member of the Oxidoreductases, Acting on the aldehyde or oxo group of donors, With oxygen as acceptor)

Enzyme Name: aldehyde oxidase

Biological Species: Desulfovibrio gigas (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

  • Q46509 - Aldehyde oxidoreductase

Representative PDB Code: 1vlb - STRUCTURE REFINEMENT OF THE ALDEHYDE OXIDOREDUCTASE FROMDESULFOVIBRIO GIGAS AT 1.28 A (Resolution = 1.28 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of acceptor

Image of aldehyde

Image of water

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Image of proton

Image of carboxylic acid

Image of reduced acceptor

acceptor
C00028
CHEBI:15339
aldehyde
C00071
CHEBI:17478
water
C00001
CHEBI:15377
2 proton
C00080
CHEBI:24636
carboxylic acid
C00060
CHEBI:33575
reduced acceptor
C00030
CHEBI:17499

It is unknown whether this reaction is reversible or not.

Overall Comment: This molybdenum hydroxylase was shown to be part of an electron-transfer chain comprising four different soluble proteins from D. gigas with a total of 11 discrete redox centres.


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Stepwise Description of the Reaction

Step 1Glu869 deprotonates the water in the coordination sphere of Mo(VI), which initiates a nucleophilic attack on the aldehyde in a substitution reaction, which eliminates a hydride ion, which adds to the sulfur dianion which is also in the Mo(VI) coordination sphere, eventually reducing Mo(VI) to Mo(IV).
Step 2Water deprotonates Glu869, which initiates a nucleophilic attack on the Mo(IV) centre, displacing the carboxylic acid product in a substitution reaction.
Step 3A single electron is transferred from Mo(IV) to an acceptor via two iron-sulfur clusters.
Step 4Water deprotonates the thiolate group part of the Mo(V) coordination sphere, causing the elimination of Glu869 from the Mo(V) coordination sphere, and transfer of the second electron from Mo(V) to the acceptor via two iron-sulfur clusters.

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Catalytic Residues Involved

Type Number Chain Location of Function
Glu 869 A Side Chain

Metal Cofactors for M0105

Type Het group Number Chain
iron FES 908 x Overview
iron FES 909 x Overview
molybdenum PCD 921 x Overview

References

  1. C. Kisker et al. (1997), Annu. Rev. Biochem., 66, 233-267. Molybdenum-cofactor-containing enzymes: structure and mechanism.
    Medline: 9242907
  2. B. A. S. Barata et al. (1993), Biochemistry, 32, 11559-11568. Aldehyde oxidoreductase activity in Desulfovibrio gigas: in vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen.
    Medline: 8218223
  3. R. Huber et al. (1996), Proc. Natl Acad. Sci. USA, 93, 8846-8851. A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes.
    Medline: 8799115

Homologue information for M0105 (1vlb)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0107 carbon-monoxide dehydrogenase (acceptor)
1.2.99.2
1n62 3.30.365.10
3.10.20.30
1.10.150.120
3.90.1170.50
0.34540.5258Compare

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

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electron carrier activity (molecular function)
oxidoreductase activity (molecular function)
aldehyde dehydrogenase (FAD-independent) activity (molecular function)
metal ion binding (molecular function)
iron-sulfur cluster binding (molecular function)
2 iron, 2 sulfur cluster binding (molecular function)
oxidation-reduction process (biological process)
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