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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Rattus norvegicus

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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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Rattus norvegicus
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The taxonomic range for the selected organisms is: Rattus norvegicus
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
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-
-
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ADH
-
-
-
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ADH-A2
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-
-
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ADH-B2
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-
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ADH-C2
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-
-
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ADH-HT
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-
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ADH3
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alcohol dehydrogenase
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alcohol dehydrogenase (NAD)
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alcohol dehydrogenase 5
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Alcohol dehydrogenase-B2
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aldehyde reductase
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aliphatic alcohol dehydrogenase
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dehydrogenase, alcohol
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ethanol dehydrogenase
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FALDH
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FDH
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-
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Gastric alcohol dehydrogenase
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-
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Glutathione-dependent formaldehyde dehydrogenase
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-
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GSH-FDH
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-
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NAD-dependent alcohol dehydrogenase
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-
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NAD-specific aromatic alcohol dehydrogenase
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-
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NADH-alcohol dehydrogenase
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-
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NADH-aldehyde dehydrogenase
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-
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Octanol dehydrogenase
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-
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primary alcohol dehydrogenase
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-
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Retinol dehydrogenase
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yeast alcohol dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
12-hydroxydodecanoate + NAD+
12-oxododecanoic acid + NADH
show the reaction diagram
-
-
-
-
?
2-butene-1-ol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
3-oxo-5beta-androstan-17beta-ol + NADH
3beta,17beta-dihydroxy-5beta-androstane + NAD+
show the reaction diagram
-
-
-
-
?
3beta,12alpha-dihydroxy-5beta-cholanoic acid + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
3beta,7alpha,12alpha-trihydroxy-5beta-cholanoic acid + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
3beta,7alpha-dihydroxy-5beta-cholanoic acid + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
3beta-7alpha-dihydroxy-5beta-cholanoate + NAD+
17-hydroxy-3-oxo-5beta-cholanoate + NADH + H+
show the reaction diagram
-
-
-
-
r
3beta-hydroxy-5beta-androstan-17-one + NAD+
5beta-androstan-3,17-dione + NADH
show the reaction diagram
-
-
-
-
?
5alpha-androstan-17beta-ol-3-one + NADH + H+
3beta,17beta-dihydroxy-5alpha-androstan + NAD+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
show the reaction diagram
benzyl alcohol + NAD+
benzaldehyde + NADH
show the reaction diagram
-
oxidation with isoenzyme ADH-1 and ADH-3, no activity with isoenzyme ADH-2
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-
?
butanol + NAD+
butyraldehyde + NADH
show the reaction diagram
-
pH 10.0: oxidized by ADH-1 and ADH-3, no activity with isoenzyme ADH-2
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-
?
cyclohexanol + NAD+
cyclohexanone + NADH
show the reaction diagram
-
-
-
-
?
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
m-nitrobenzaldehyde + NADH + H+
m-nitrobenzyl alcohol + NAD+
show the reaction diagram
-
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
show the reaction diagram
-
oxidized with ADH-3, no activity with ADH-1 and ADH-2
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-
?
octan-1-ol + NAD+
n-octanal + NADH
show the reaction diagram
-
-
-
-
?
octanal + NADH + H+
octanol + NAD+
show the reaction diagram
-
-
-
-
?
pentanol + NAD+
n-pentanal + NADH
show the reaction diagram
-
-
-
-
?
phytol + NAD+
phytenal + NADH + H+
show the reaction diagram
-
-
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
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ADH-1 contains 3.9 mol of zinc per mol of subunit, ADH-2 contains 4.2 mol of zinc per mol of subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-methoxypyrazole
pyrazole
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.17 - 230
1-butanol
0.025 - 0.51
1-Octanol
0.08 - 78
1-Pentanol
0.013 - 1.4
12-hydroxydodecanoate
0.35 - 60
2-Buten-1-ol
0.128 - 0.31
3beta,12alpha-dihydroxy-5beta-cholanoate
0.149 - 0.182
3beta,7alpha,12alpha-trihydroxy-5beta-cholanoate
0.35
3beta,7alpha-12alpha-trihydroxy-5beta-cholanoate
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isoenzyme 4
0.032 - 0.071
3beta-7alpha-dihydroxy-5beta-cholanoate
0.021 - 0.04
5alpha-androstan-17beta-ol-3-one
0.123 - 0.164
5beta-androstan-3beta-ol-17 one
0.217 - 0.31
acetaldehyde
0.05 - 1.4
benzyl alcohol
3
Butanal
-
isoenzyme ADH-1, pH 7.5
2.2 - 1900
Cyclohexanol
0.76 - 5000
ethanol
1.4
m-nitrobenzaldehyde
-
isoenzyme ADH-1, pH 7.5
0.04 - 0.25
NAD+
0.0017 - 0.091
NADH
0.3 - 3.5
octanal
1.6
Octanol
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isoenzyme ADH-2, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.833 - 48.8
1-butanol
1 - 60.8
1-Octanol
1.17 - 48.8
1-Pentanol
1.27 - 20
12-hydroxydodecanoate
1.67 - 213
2-Buten-1-ol
1 - 89.7
benzyl alcohol
0.383 - 1.75
Cyclohexanol
1 - 62.7
ethanol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
-
isoenzyme 4
0.12
-
isoenzyme 1
0.2
-
isoenzyme 3
0.62
-
isoenzyme 2
1.14
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ADH-2
32.5
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ADH-1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.7
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oxidation of ethanol, isoenzyme 2, 3 and 4
11
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oxidation of octanol
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
low expression level of ADH5
Manually annotated by BRENDA team
-
low expression level of ADH5
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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enzyme is involved in phytol degradation
additional information
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ADH5 molecular modeling and molecular dynamics simulations, and comparison to human ADH1 enzyme, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADH1_RAT
376
0
39645
Swiss-Prot
other Location (Reliability: 2)
ADH6_RAT
376
0
39726
Swiss-Prot
other Location (Reliability: 3)
ADH7_RAT
374
0
40105
Swiss-Prot
other Location (Reliability: 3)
ADHX_RAT
374
0
39576
Swiss-Prot
other Location (Reliability: 3)
Q64564_RAT
133
0
14018
TrEMBL
other Location (Reliability: 2)
Q7TQ90_RAT
872
0
93847
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
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2 * 39000, ADH-2, SDS-PAGE
40000
-
2 * 40000, ADH-3, SDS-PAGE
43000
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2 * 43000, ADH-1, SDS-PAGE
80000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ADH-1, ADH-2 and ADH-3
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isoenzyme 1, 2, 3, and 4
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of rat ADH5 in an in vitro transcription/translation system, GFP-tagged ADH5 in COS cells, but no soluble ADH5 protein from heterologously expression in Escherichia coli cells with expression systems successfully used for other mammalian ADHs, including fused to glutathione-S-transferase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Herrera, E.; Zorzano, A.; Fresneda, V.
Comparative kinetics of human and rat liver alcohol dehydrogenase
Biochem. Soc. Trans.
11
729-730
1983
Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Julia, P.; Farres, J.; Pares, X.
Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties
Eur. J. Biochem.
162
179-189
1987
Rattus norvegicus
Manually annotated by BRENDA team
Pares, X.; Moreno, A.; Cederlund, E.; Hoeoeg, J.O.; Joernvall, H.
Class IV mammalian alcohol dehydrogenase. Structural data of the rat stomach enzyme reveal a new class well separated from those already characterized
FEBS Lett.
277
115-118
1990
Rattus norvegicus
Manually annotated by BRENDA team
Mezey, E.; Potter, J.J.
Separation and partial characterization of multiple forms of rat liver alcohol dehydrogenase
Arch. Biochem. Biophys.
225
787-794
1983
Rattus norvegicus
Manually annotated by BRENDA team
Westerlund, M.; Galter, D.; Carmine, A.; Olson, L.
Tissue- and species-specific expression patterns of class I, III, and IV Adh and Aldh 1 mRNAs in rodent embryos
Cell Tissue Res.
322
227-236
2005
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Quintanilla, M.E.; Tampier, L.; Sapag, A.; Gerdtzen, Z.; Israel, Y.
Sex differences, alcohol dehydrogenase, acetaldehyde burst, and aversion to ethanol in the rat: a systems perspective
Am. J. Physiol. Endocrinol. Metab.
293
E531-E537
2007
Rattus norvegicus
Manually annotated by BRENDA team
Muralidharan, F.N.; Muralidharan, V.B.
Characterization of phytol-phytanate conversion activity in rat liver
Biochim. Biophys. Acta
883
54-62
1986
Rattus norvegicus
Manually annotated by BRENDA team
Ostberg, L.J.; Stroemberg, P.; Hedberg, J.J.; Persson, B.; Hoeoeg, J.O.
Analysis of mammalian alcohol dehydrogenase 5 (ADH5): Characterisation of rat ADH5 with comparisons to the corresponding human variant
Chem. Biol. Interact.
202
97-103
2013
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team