Center for Bioinformatics
Oxidoreductases | Transferases | Hydrolases | Lyases | Isomerases | Ligases

Basic Information

Enzyme Number

1.1.1.1

Official Name

alcohol dehydrogenase

Name from literature

alcohol dehydrogenase

Pathway from literature

alcohol oxidation

Pathway from KEGG

Xenobiotics Biodegradation and Metabolism; Metabolism of xenobiotics by cytochrome P450; map00980

Metabolism of Cofactors and Vitamins; Retinol metabolism; map00830

Lipid Metabolism; Fatty acid metabolism; map00071

Carbohydrate Metabolism; Glycolysis / Gluconeogenesis; map00010

Amino Acid Metabolism; Tyrosine metabolism; map00350

Xenobiotics Biodegradation and Metabolism; 3-Chloroacrylic acid degradation; map00641

Lipid Metabolism; Bile acid biosynthesis; map00120

Xenobiotics Biodegradation and Metabolism; 1- and 2-Methylnaphthalene degradation; map00624

Xenobiotics Biodegradation and Metabolism; Drug metabolism - cytochrome P450; map00982

Organisms

Rat (10116)

Genome localization

2q44[29646 ], 2q44[171178 ], 2q44[24172 ],

Comments

A zinc protein. Acts on primary or secondary alcohols or hemi-acetals; the animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.

Rate-limiting Description

"Since the electron flux in the respiratory chain is controlled by the ADP supply, alcohol dehydrogenase-dependent ethanol metabolism can be activated by perturbations which circumvent the rate-limiting step, such as artificial electron acceptors, gluconeogenic precursors, and uncoupling agents." (1096557)

"Rates of exchange catalysed by alcohol dehydrogenase were determined in vivo in order to find rate-limiting steps in ethanol metabolism." (4038269)

"These results suggest that ethanol oxidation by cytosolic alcohol dehydrogenase may be regulated in part by the hepatic acetaldehyde concentration achieved during ethanol metabolism rather than NADH reoxidation, either to supply NAD for the dehydrogenase, or to reduce inhibition of the enzyme by NADH, being a rate-limiting factor in ethanol metabolism in fasted rats.." (2932116)

"At ethanol concentrations above 10 mM, substrate inhibition, consistent with the formation a dead-end ADH-NADH-ethanol complex, also becomes a rate-limiting factor." (6356161)

"Qualitatively, therefore, alcohol dehydrogenase activity appears to be a major rate-limiting factor in ethanol metabolism." (6370140)

Regulatory Information

Upstream transcription factor

24253;25301;24252

Regulatory type

Detail

phosphorylation;

Q5XI95

phosphorylation;

Q64563:from_uniprot:30_Phosphoserine

transcriptional factor;"C/EBP(24252),enhancer binding proteins beta(24253),enhancer binding proteins gamma(25301)"

"rat hepatic Class I ADH gene expression is regulated in vivo by ethanol in a mechanism involving the C/EBP site and the enhancer binding proteins beta and gamma" (12213809)

Gene ontology

Gene ontology

GO:0008270 (F) zinc ion binding [Q5XI95, P06757, P12711, Q64563, P41682 ];
GO:0051287 (F) NAD binding [Q64564 ];
GO:0035276 (F) ethanol binding [Q64564 ];
GO:0005829 (C) cytosol [Q64564 ];
GO:0005737 (C) cytoplasm [Q5XI95, P06757, P12711, Q64563, P41682 ];
GO:0046186 (P) acetaldehyde biosynthetic process [Q64564 ];
GO:0004022 (F) alcohol dehydrogenase activity [Q5XI95, Q64564, P06757, P12711, Q64563 ];
GO:0006069 (P) ethanol oxidation [Q64564 ];
GO:0051903 (F) S-(hydroxymethyl)glutathione dehydrogenase ... [P12711 ];
GO:0005625 (C) soluble fraction [Q64564 ];
GO:0008144 (F) drug binding [Q64564 ];
GO:0055114 (P) oxidation reduction [Q5XI95, P06757, P12711, Q64563, P41682 ];

Subcellular localization

Localization

cytoplasm [Q5XI95, P06757, P12711, Q64563, P41682 ];

Links

SwissProt

P06757; P12711; P41682; Q5XI95; Q64563; Q64564

Entrez Gene

171178; 24172; 29646



  Copyright 2009, Center for Bioinformatics 
  Last Modified: 2009-03-24  
  Design by Zhao Min