| Identification |
|---|
| HMDB Protein ID
| HMDBP12301 |
| Secondary Accession Numbers
| None |
| Name
| Aldo-keto reductase family 1 member A1 |
| Synonyms
|
- Alcohol dehydrogenase [NADP(+)]
- Aldehyde reductase
- Glucuronate reductase
- Glucuronolactone reductase
|
| Gene Name
| AKR1A1 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (By similarity). Plays an important role in ascorbic acid biosynthesis by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone (By similarity). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Displays no reductase activity towards retinoids (PubMed:12732097). |
| Pathways
|
- Ascorbate and aldarate metabolism
- Biosynthesis of cofactors
- Chemical carcinogenesis - reactive oxygen species
- Gluconeogenesis
- Glycerolipid metabolism
- Pentose and glucuronate interconversions
- Pyruvate metabolism
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| cellular detoxification of aldehyde |
| aldehyde catabolic process |
| D-glucuronate catabolic process |
| L-ascorbic acid biosynthetic process |
| Cellular Component |
| cytosol |
| apical plasma membrane |
| Molecular Function |
| alditol:NADP+ 1-oxidoreductase activity |
| allyl-alcohol dehydrogenase activity |
| D-threo-aldose 1-dehydrogenase activity |
| glucuronolactone reductase activity |
| glycerol dehydrogenase [NADP+] activity |
| methylglyoxal reductase (NADPH-dependent, acetol producing) |
| mevaldate reductase (NADPH) activity |
| L-glucuronate reductase activity |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 325 |
| Molecular Weight
| 36581.71 |
| Theoretical pI
| 6.996 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P50578 |
| UniProtKB/Swiss-Prot Entry Name
| AK1A1_PIG |
| PDB IDs
|
|
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Flynn TG, Green NC, Bhatia MB, el-Kabbani O: Structure and mechanism of aldehyde reductase. Adv Exp Med Biol. 1995;372:193-201. doi: 10.1007/978-1-4615-1965-2_25. [PubMed:7484379 ]
- el-Kabbani O, Judge K, Ginell SL, Myles DA, DeLucas LJ, Flynn TG: Structure of porcine aldehyde reductase holoenzyme. Nat Struct Biol. 1995 Aug;2(8):687-92. doi: 10.1038/nsb0895-687. [PubMed:7552731 ]
- el-Kabbani O, Carper DA, McGowan MH, Devedjiev Y, Rees-Milton KJ, Flynn TG: Studies on the inhibitor-binding site of porcine aldehyde reductase: crystal structure of the holoenzyme-inhibitor ternary complex. Proteins. 1997 Oct;29(2):186-92. doi: 10.1002/(sici)1097-0134(199710)29:2<186::aid-prot6>3.0.co;2-b. [PubMed:9329083 ]
- Crosas B, Hyndman DJ, Gallego O, Martras S, Pares X, Flynn TG, Farres J: Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism. Biochem J. 2003 Aug 1;373(Pt 3):973-9. doi: 10.1042/BJ20021818. [PubMed:12732097 ]
|
