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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Pseudomonas aeruginosa

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.1 alcohol dehydrogenase
IUBMB Comments
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
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This record set is specific for:
Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adh, alcohol dehydrogenase, aldehyde dehydrogenase, adh1b, short-chain dehydrogenase/reductase, ssadh, adh1c, yeast alcohol dehydrogenase, retinol dehydrogenase, faldh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 kDa allergen
-
-
-
-
ADH-A2
-
-
-
-
ADH-B2
-
-
-
-
ADH-C2
-
-
-
-
ADH-HT
-
-
-
-
ADH3
-
-
-
-
alcohol dehydrogenase (NAD)
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-
-
-
Alcohol dehydrogenase-B2
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-
-
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aldehyde reductase
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-
-
-
aliphatic alcohol dehydrogenase
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-
-
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dehydrogenase, alcohol
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-
-
-
ethanol dehydrogenase
-
-
-
-
FALDH
-
-
-
-
FDH
-
-
-
-
Gastric alcohol dehydrogenase
-
-
-
-
Glutathione-dependent formaldehyde dehydrogenase
-
-
-
-
GSH-FDH
-
-
-
-
NAD-dependent alcohol dehydrogenase
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-
-
-
NAD-specific aromatic alcohol dehydrogenase
-
-
-
-
NADH-alcohol dehydrogenase
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-
-
-
NADH-aldehyde dehydrogenase
-
-
-
-
Octanol dehydrogenase
-
-
-
-
primary alcohol dehydrogenase
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-
-
-
Retinol dehydrogenase
-
-
-
-
yeast alcohol dehydrogenase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a primary alcohol + NAD+ = an aldehyde + NADH + H+
show the reaction diagram
the catalytic triad consists of Cys44, His67, and Cys154, active site structure
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
alcohol:NAD+ oxidoreductase
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-72-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
-
-
-
-
?
ethylene glycol + NAD+
?
show the reaction diagram
-
poor substrate
-
-
r
primary or secondary alcohol + NAD+
aldehyde or ketone + NADH
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
1 catalytic and 1 structural zinc ion per subunit, coordination complex geometry
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Methylpyrazole
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.64
ethanol
-
-
200
ethylene glycol
-
above
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5
ethylene glycol
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.64
4-Methylpyrazole
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A8G7LFG1_PSEAI
342
0
35883
TrEMBL
-
A0A8G2R0W6_PSEAI
342
0
35959
TrEMBL
-
A0A485EMH1_PSEAI
161
0
17066
TrEMBL
-
A0A4P0TMJ2_PSEAI
451
0
48287
TrEMBL
-
A0A7M3AS69_PSEAI
342
0
35855
TrEMBL
-
A0A8G4GBV4_PSEAI
342
0
35925
TrEMBL
-
A0A8G3AJP7_PSEAI
342
0
35966
TrEMBL
-
A0A6A9JV87_PSEAI
342
0
35842
TrEMBL
-
A0A8F8R1D8_PSEAI
342
0
35969
TrEMBL
-
A0A8F9JY30_PSEAI
342
0
35888
TrEMBL
-
A0A6B1YC63_PSEAI
342
0
35881
TrEMBL
-
A0A8G4AVK4_PSEAI
342
0
35959
TrEMBL
-
A0A8G3D5J0_PSEAI
342
0
35883
TrEMBL
-
A0A8G7JJN7_PSEAI
342
0
35969
TrEMBL
-
A0A0A8RME7_PSEAI
366
0
38591
TrEMBL
-
A0A8G4A8S9_PSEAI
342
0
35925
TrEMBL
-
A0A8H0X7U5_PSEAI
342
0
35941
TrEMBL
-
A0A0C6F4Y3_PSEAI
342
0
35883
TrEMBL
-
A0A3S0J2B9_PSEAI
342
0
35910
TrEMBL
-
A0A8G2QQ09_PSEAI
342
0
35883
TrEMBL
-
A0A8H2F1U7_PSEAI
342
0
35881
TrEMBL
-
A0A8G2Q7X9_PSEAI
342
0
35925
TrEMBL
-
A0A8G6HF14_PSEAI
342
0
35923
TrEMBL
-
A0A8G5D008_PSEAI
342
0
35925
TrEMBL
-
H6WRS7_PSEAI
342
0
35911
TrEMBL
-
A0A8G3P5V2_PSEAI
342
0
35964
TrEMBL
-
A0A8G7A3U2_PSEAI
342
0
35883
TrEMBL
-
A0A8G2RRD4_PSEAI
342
0
35924
TrEMBL
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
quaternary organization and stability, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ternary complex of enzyme with NADH and ethylene glycol, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain TG-1
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Levin, I.; Meiri, G.; Peretz, M.; Burstein, Y.; Frolow, F.
The ternary complex of Pseudomonas aeruginosa alcohol dehydrogenase with NADH and ethylene glycol
Protein Sci.
13
1547-1556
2004
Pseudomonas aeruginosa, Pseudomonas aeruginosa PaADH
Manually annotated by BRENDA team
Nosova, T.; Jousimies-Somer, H.; Kaihovaara, P.; Jokelainen, K.; Heine, R.; Salaspuro, M.
Characteristics of alcohol dehydrogenases of certain aerobic bacteria representing human colonic flora
Alcohol. Clin. Exp. Res.
21
489-494
1997
Escherichia coli, Hafnia alvei, Klebsiella oxytoca, Klebsiella pneumoniae, Pseudomonas aeruginosa
Manually annotated by BRENDA team