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Overview for MACiE Entry M0256

Version history

General Information

EC Number: 1.1.1.1 (A member of the Oxidoreductases, Acting on the CH-OH group of donors, With NAD+ or NADP+ as acceptor)

Enzyme Name: alcohol dehydrogenase

Biological Species: Equus caballus (Horse)

Catalytic Chain UniprotKB Accession Codes:

  • P00327 - Alcohol dehydrogenase E chain

Representative PDB Code: 1qlh - HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NAD DOUBLEMUTANT OF GLY 293 ALA AND PRO 295 THR (Resolution = 2.07 Å).

Catalytic CATH Codes:

  • 3.90.180.10 - Medium-chain alcohol dehydrogenases, catalytic domain

"Other" CATH Codes:

Display structure information

Overall Reaction:

Image of alcohol

Image of NAD

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Image of proton

Image of an aldehyde or ketone

Image of NADH

alcohol
C00069
CHEBI:30879
NAD
C00003
CHEBI:15846
proton
C00080
CHEBI:24636
an aldehyde or ketone
C01450
CHEBI:23019
NADH
C00004
CHEBI:16908

Overall Comment: This alcohol dehydrogenase is zinc-dependent and belongs to the class I zinc-containing ADH superfamily. Whilst this enzyme binds two zinc ions, only one of these is actively involved in catalysis. It has been noted that that many ADHs that lack a His at position 51 often have an analogous histidine at position 47 which can perform the same function (PMID: 10970744), i.e. activating the Ser/Thr 48 for its catalytic function, also that the residue at position 48 is interchangabe between serine and threonine (acts as a general base to deprotonate the OH group of the alcohol substrate).


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Stepwise Description of the Reaction

Step 1Bulk water initiates the deprotonation of Ser48 via His51, the ribose ring of NAD377. Ser48 deprotonates the alcohol group, which is activated by Zn(II), initiating hydride transfer to NAD377.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Ser 48 A Side Chain
His 51 A Side Chain

Organic Cofactors for M0256

Type Identity Chain
NAD NAD 377 A Overview

Metal Cofactors for M0256

Type Het group Number Chain
zinc ZN 375 A Overview
zinc ZN 376 A Overview

References

  1. H. Eklund et al. (1982), J. Biol. Chem., 257, 14349-14358. .
    Medline: 6754727
  2. S. Ramaswamy et al. (1999), Biochemistry, 38, 13951-13959. Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer.
    Medline: 10529241
  3. R. Ladenstein et al. (2008), Cell. Mol. Life Sci., 65, 3918-3935. Structure-function relationships in short-chain alcohol dehydrogenases.
    Medline: 19011748
  4. S. Svensson et al. (2000), J. Mol. Biol., 302, 441-453. .
    Medline: 10970744

Homologue information for M0256 (1qlh)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with the same EC number (different mechanisms):

MACiE Entry Enzyme Name PDB code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0255 alcohol dehydrogenase 1mg5 0.931 0.225 Compare

Compare of the other reactions in MACiE with EC number 1.1.1.1


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

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