All-trans-retinol dehydrogenase [NAD(+)] ADH1B

Function

Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism. In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal. Catalyzes in the oxidative direction with higher efficiency. Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal.

Classification

Family (Pfam)

PF08240 ADH_N, PF00107 ADH_zinc_N

InterPro

ADH-like_C, ADH-like_N, ADH_Zn_CS, ER, GroES-like_sf, NAD(P)-bd_dom_sf

Functional cluster

Oxidoreductases & Polyketide Synthases

Experimental structures · PDB · 9

• 1DEH X-ray 2.20A
• 1HDX X-ray 2.50A
• 1HDY X-ray 2.50A
• 1HDZ X-ray 2.50A
• 1HSZ X-ray 2.20A
• 1HTB X-ray 2.40A
• 1U3U X-ray 1.60A
• 1U3V X-ray 1.65A
• 3HUD X-ray 3.20A

A predicted model is available from AlphaFold.

Gene Ontology · 7

• GO:0005829 cytosol
• GO:0004022 alcohol dehydrogenase (NAD+) activity
• GO:0004745 all-trans-retinol dehydrogenase (NAD+) activity
• GO:0008270 zinc ion binding
• GO:0042573 retinoic acid metabolic process
• GO:0001523 retinoid metabolic process
• GO:0042572 retinol metabolic process

Disease associations

• OMIM:103720 RAW:OMIM_103720

Drugs targeting this protein · 2

• FOMEPIZOLE inhibitor
• NITREFAZOLE inhibitor

Related proteins · sequence + function similarity

• All-trans-retinol dehydrogenase [NAD(+)] ADH1B 1.00
• Alcohol dehydrogenase 1C 0.99
• All-trans-retinol dehydrogenase [NAD(+)] ADH1B 0.99
• Alcohol dehydrogenase 1C 0.99
• Alcohol dehydrogenase 1 0.99
• Alcohol dehydrogenase S chain 0.99
• Alcohol dehydrogenase 1A 0.98
• Alcohol dehydrogenase 1A 0.98
• Alcohol dehydrogenase 1 0.98
• Alcohol dehydrogenase 1A 0.98
• Alcohol dehydrogenase E chain 0.98
• Alcohol dehydrogenase 1 0.98

Co-cited proteins · studied together in the literature

• All-trans-retinol dehydrogenase [NAD(+)] ADH7 2 shared papers
• Alcohol dehydrogenase 1A 2 shared papers
• Alcohol dehydrogenase 1C 2 shared papers

Literature · 21 cited papers

• An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J. Proteomics · 2014
• Comparative functional analysis of human medium-chain dehydrogenases, short-chain dehydrogenases/reductases and aldo-keto reductases with retinoids. Biochem. J. · 2006
• Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature · 2005
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. · 2004
• Kinetics of human alcohol dehydrogenase with ring-oxidized retinoids: effect of Tween 80. Arch. Biochem. Biophys. · 2004
• Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat. Genet. · 2004
• Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. · 2001
• Genetic polymorphism of alcohol dehydrogenase in Europeans: the ADH2*2 allele decreases the risk for alcoholism and is associated with ADH3*1. Hepatology · 2000
• X-ray structure of human beta3beta3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J. Biol. Chem. · 1996
• Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences. J. Mol. Biol. · 1994
• Human liver alcohol dehydrogenase. 1. The primary structure of the beta 1 beta 1 isoenzyme. Eur. J. Biochem. · 1984
• Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzyme. Proc. Natl. Acad. Sci. U.S.A. · 1984
• … and 9 more in the literature graph