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  • 11.0 [archived version]
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DHRS3 DHRS3 BCO1 BCO1 CYP2B6 CYP2B6 ALDH1A2 ALDH1A2 CYP26C1 CYP26C1 RDH16 RDH16 CYP26A1 CYP26A1 RDH12 RDH12 CYP26B1 CYP26B1 RDH11 RDH11 RDH5 RDH5
"ALDH1A2" - Retinal dehydrogenase 2 in Homo sapiens
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experimentally determined
Predicted Interactions
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textmining
co-expression
protein homology
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ALDH1A2Retinal dehydrogenase 2; Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity); Belongs to the aldehyde dehydrogenase family (518 aa)    
Predicted Functional Partners:
CYP26A1
Cytochrome P450 26A1; Plays a key role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA. Capable of both 4-hydroxylation and 18- hydroxylation. Responsible for generation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA; Belongs to the cytochrome P450 family (497 aa)
       
  0.991
CYP26B1
Cytochrome P450 26B1; Involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation. Involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates- all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH- RA. Essential for postnatal survival. Plays a central role in germ cell development- acts by degrading RA in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required [...] (512 aa)
       
  0.978
CYP26C1
Cytochrome P450 26C1; Plays a role in retinoic acid metabolism. Acts on retinoids, including all-trans-retinoic acid (RA) and its stereoisomer 9-cis-RA (preferred substrate); Belongs to the cytochrome P450 family (522 aa)
       
  0.964
RDH11
Retinol dehydrogenase 11; Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity towards 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected (318 aa)
     
  0.962
RDH12
Retinol dehydrogenase 12; Exhibits an oxidoreductive catalytic activity towards retinoids. Most efficient as an NADPH-dependent retinal reductase. Displays high activity toward 9-cis and all-trans-retinol. Also involved in the metabolism of short-chain aldehydes. No steroid dehydrogenase activity detected. Might be the key enzyme in the formation of 11-cis-retinal from 11-cis-retinol during regeneration of the cone visual pigments (316 aa)
     
  0.958
RDH5
11-cis retinol dehydrogenase; Stereospecific 11-cis retinol dehydrogenase, which catalyzes the final step in the biosynthesis of 11-cis retinaldehyde, the universal chromophore of visual pigments. Also able to oxidize 9-cis-retinol and 13-cis-retinol, but not all- trans-retinol. Active in the presence of NAD as cofactor but not in the presence of NADP; Short chain dehydrogenase/reductase superfamily (318 aa)
     
 
  0.954
DHRS3
Short-chain dehydrogenase/reductase 3; Catalyzes the reduction of all-trans-retinal to all- trans-retinol in the presence of NADPH; Short chain dehydrogenase/reductase superfamily (302 aa)
     
  0.951
RDH16
Retinol dehydrogenase 16; Oxidoreductase with a preference for NAD. Oxidizes all- trans-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotestosterone and androstanedione. Can also catalyze the reverse reaction; Short chain dehydrogenase/reductase superfamily (317 aa)
     
 
  0.943
BCO1
Beta,beta-carotene 15,15’-dioxygenase; Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism; Belongs to the carotenoid oxygenase family (547 aa)
     
 
  0.932
CYP2B6
Cytochrome P450 2B6; Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,4-cineole 2-exo-monooxygenase (491 aa)
     
  0.932
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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