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Liver alcohol dehydrogenase

alcohol dehydrogenase
Protein ADH5 PDB 1m6h.png
Crystallographic structure of the
homodimer of human ADH5.
Identifiers
EC number 1.1.1.1
CAS number 9031-72-5
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
alcohol dehydrogenase 1A,
α polypeptide
Identifiers
Symbol ADH1A
Alt. symbols ADH1
Entrez 124
HUGO 249
OMIM 103700
RefSeq NM_000667
UniProt P07327
Other data
EC number 1.1.1.1
Locus Chr. 4 q23
alcohol dehydrogenase 1B,
β polypeptide
Identifiers
Symbol ADH1B
Alt. symbols ADH2
Entrez 125
HUGO 250
OMIM 103720
RefSeq NM_000668
UniProt P00325
Other data
EC number 1.1.1.1
Locus Chr. 4 q23
alcohol dehydrogenase 1C,
γ polypeptide
Identifiers
Symbol ADH1C
Alt. symbols ADH3
Entrez 126
HUGO 251
OMIM 103730
RefSeq NM_000669
UniProt P00326
Other data
EC number 1.1.1.1
Locus Chr. 4 q23
alcohol dehydrogenase 4
(class II), π polypeptide
Identifiers
Symbol ADH4
Entrez 127
HUGO 252
OMIM 103740
RefSeq NM_000670
UniProt P08319
Other data
EC number 1.1.1.1
Locus Chr. 4 q22
alcohol dehydrogenase 5
(class III), χ polypeptide
Identifiers
Symbol ADH5
Entrez 128
HUGO 253
OMIM 103710
RefSeq NM_000671
UniProt P11766
Other data
EC number 1.1.1.1
Locus Chr. 4 q23
alcohol dehydrogenase 6
(class V)
Identifiers
Symbol ADH6
Entrez 130
HUGO 255
OMIM 103735
RefSeq NM_000672
UniProt P28332
Other data
EC number 1.1.1.1
Locus Chr. 4 q23
alcohol dehydrogenase 7
(class IV), μ or σ polypeptide
Identifiers
Symbol ADH7
Entrez 131
HUGO 256
OMIM 600086
RefSeq NM_000673
UniProt P40394
Other data
EC number 1.1.1.1
Locus Chr. 4 q23-q24
Iron-containing alcohol dehydrogenase
PDB 1jqa EBI.jpg
bacillus stearothermophilus glycerol dehydrogenase complex with glycerol
Identifiers
Symbol Fe-ADH
Pfam PF00465
Pfam clan CL0224
InterPro IPR001670
PROSITE PDOC00059
SCOP 1jqa
SUPERFAMILY 1jqa

Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.

Genetic evidence from comparisons of multiple organisms showed that a glutathione-dependent formaldehyde dehydrogenase, identical to a class III alcohol dehydrogenase (ADH-3/ADH5), is presumed to be the ancestral enzyme for the entire ADH family. Early on in evolution, an effective method for eliminating both endogenous and exogenous formaldehyde was important and this capacity has conserved the ancestral ADH-3 through time. Gene duplication of ADH-3, followed by series of mutations, the other ADHs evolved.

The ability to produce ethanol from sugar (which is the basis of how alcoholic beverages are made) is believed to have initially evolved in yeast. Though this feature is not adaptive from an energy point of view, by making alcohol in such high concentrations so that they would be toxic to other organisms, yeast cells could effectively eliminate their competition. Since rotting fruit can contain more than 4% of ethanol, animals eating the fruit needed a system to metabolize exogenous ethanol. This was thought to explain the conservation of ethanol active ADH in other species than yeast, though ADH-3 is now known to also have a major role in nitric oxide signaling.


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