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Information on EC 1.1.1.1 - alcohol dehydrogenase

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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:
UNIPROT: Q70YJ9
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Word Map
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
AdhE
bifunctional enzyme, containing both aldehyde dehydrogenase and alcohol dehydrogenase activities
40 kDa allergen
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ADH
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ADH-A2
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ADH-B2
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ADH-C2
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ADH-HT
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ADH3
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alcohol dehydrogenase (NAD)
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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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Gastric alcohol dehydrogenase
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Glutathione-dependent formaldehyde dehydrogenase
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GSH-FDH
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NAD-dependent alcohol dehydrogenase
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NAD-specific aromatic alcohol dehydrogenase
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NADH-alcohol dehydrogenase
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NADH-aldehyde dehydrogenase
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Octanol dehydrogenase
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primary alcohol dehydrogenase
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Retinol dehydrogenase
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yeast alcohol dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.98
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
higher enzyme level in mitochondria from cells grown at pH 6.0 than in mitochondria from cells grown at pH 3.7
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
ADHE can be involved either in ethanol production or assimilation, or both, depending upon environmental conditions
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q70YJ9_9CHLO
885
0
91484
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85000
x * 85000, SDS-PAGE
91480
calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is strongly influenced by the pH of the culture medium. Expression in cells grown on ethanol is higher at pH 6.0 than at pH 3.7
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Atteia, A.; van Lis, R.; Mendoza-Hernndez, G.; Henze, K.; Martin, W.; Riveros-Rosas, H.; Gonzlez-Halphen, D.
Bifunctional aldehyde/alcohol dehydrogenase (ADHE) in chlorophyte algal mitochondria
Plant Mol. Biol.
53
175-188
2003
Polytomella sp. Pringsheim 198.80 (Q70YJ9)
Manually annotated by BRENDA team