AKR1B1
entrez
231
canonical
uniprot
P15121
canonical
ensembl
ENSG00000085662
resolver
ensp
ENSP00000285930
resolver
ensp
ENSP00000586242
resolver
enst
ENST00000285930
resolver
genesymbol
AKR1B1
resolver
genesymbol_syn
ALDR1
resolver
genesymbol_syn
ALR2
resolver
hgnc
HGNC:381
resolver
uniprot
B2R8N3
resolver
uniprot
Q5U031
resolver
uniprot
Q6FGA4
resolver
uniprot
Q6ICP2
resolver
uniprot
Q9BS21
resolver
uniprot
Q9UCI9
resolver
uniprot_entry
ALDR_HUMAN
resolver
uniprot_sec
B2R8N3
resolver
uniprot_sec
Q5U031
resolver
uniprot_sec
Q6FGA4
resolver
uniprot_sec
Q6ICP2
resolver
uniprot_sec
Q9BS21
resolver
uniprot_sec
Q9UCI9
resolver
activity_regulation
ACTIVITY REGULATION: Cys-299 acts as a redox-sensitive regulatory site (PubMed:1332968, PubMed:19061876, PubMed:21084309, PubMed:8343525). Its thiol group undergoes reversible oxidative and nitrosative modifications (S-nitrosylation, S-glutathiolation) that modulate enzyme activity, linking AKR1B1 function to the cellular redox environment (PubMed:19061876, PubMed:21084309, PubMed:8343525). Tolrestat inhibits retinal reduction (PubMed:12732097). {ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:1332968, ECO:0000269|PubMed:19061876, ECO:0000269|PubMed:21084309, ECO:0000269|PubMed:8343525}.
uniprot
proteins
amino_acid_sequence
MASRLLLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALLSCTSHKDYPFHEEF
uniprot
proteins
ec_number
1.1.1.21
uniprot
proteins
ec_number
1.1.1.300
uniprot
proteins
ec_number
1.1.1.372
uniprot
proteins
ec_number
1.1.1.54
uniprot
proteins
function
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, bile acids and xenobiotics substrates (PubMed:10510318, PubMed:12732097, PubMed:1332968, PubMed:21329684, PubMed:8245005, PubMed:4402695, PubMed:1936586). It catalyzes the reduction of glucose to sorbitol, the first step of the polyol pathway, an alternative route of glucose metabolism that converts glucose to fructose (PubMed:4402695, PubMed:1936586). This pathway becomes highly active under elevated glucose levels, such as during hyperglycemia (PubMed:1936586). Reduces steroids and their derivatives and prostaglandins. Displays low enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:19010934, PubMed:8343525). Catalyzes the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2-(5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related phospholipid aldehydes that are generated from the oxydation of phosphotidylcholine and phosphatdyleethanolamides (PubMed:17381426). Plays a role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:21329684). {ECO:0000269|PubMed:10510318, ECO:0000269|PubMed:12732097, ECO:0000269|PubMed:1332968, ECO:0000269|PubMed:17381426, ECO:0000269|PubMed:19010934, ECO:0000269|PubMed:1936586, ECO:0000269|PubMed:21329684, ECO:0000269|PubMed:8245005, ECO:0000269|PubMed:8343525}.
uniprot
proteins
mass_dalton
35853
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="D->N: Reduced glyceraldehyde oxidoreductase activity."; /evidence="ECO:0000269|PubMed:8245005"; MUTAGEN 49; /note="Y->F: Complete loss of glyceraldehyde oxidoreductase activity."; /evidence="ECO:0000269|PubMed:8245005"; MUTAGEN 78; /note="K->M: Reduced glyceraldehyde oxidoreductase activity."; /evidence="ECO:0000269|PubMed:8245005"; MUTAGEN 81; /note="C->S: Reduces kcat and increases Km for D,L-glyceraldehyde."; /evidence="ECO:0000269|PubMed:1332968"; MUTAGEN 111; /note="H->N: Reduced glyceraldehyde oxidoreductase activity."; /evidence="ECO:0000269|PubMed:8245005"; MUTAGEN 299; /note="C->S: Reduced affinity for NADP. Does not affect the binding affinity of NADP(+). Reduced the affinity for D,L-glyceraldehyde, D-glucose and HNE. kcat is increased for D,L-glyceraldehyde. kcat is reduced for D-glucose and HNE, and increased for benzyl alcohol."; /evidence="ECO:0000269|PubMed:1332968, ECO:0000269|PubMed:21084309"; MUTAGEN 304; /note="C->S: Reduces kcat and increases Km for D,L-glyceraldehyde."; /evidence="ECO:0000269|PubMed:1332968
uniprot
proteins
protein_family
Aldo/keto reductase family
uniprot
proteins
pubmed
10510318
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12732097
uniprot
proteins
pubmed
1332968
uniprot
proteins
pubmed
1447221
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14996095
uniprot
proteins
pubmed
15146478
uniprot
proteins
pubmed
15272156
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1621098
uniprot
proteins
pubmed
16337231
uniprot
proteins
pubmed
17368668
uniprot
proteins
pubmed
17381426
uniprot
proteins
pubmed
17418233
uniprot
proteins
pubmed
17505104
uniprot
proteins
pubmed
19010934
uniprot
proteins
pubmed
1901857
uniprot
proteins
pubmed
19061876
uniprot
proteins
pubmed
1936586
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21084309
uniprot
proteins
pubmed
2111143
uniprot
proteins
pubmed
2112546
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21329680
uniprot
proteins
pubmed
21329684
uniprot
proteins
pubmed
2492527
uniprot
proteins
pubmed
2498333
uniprot
proteins
pubmed
2504709
uniprot
proteins
pubmed
2510130
uniprot
proteins
pubmed
4402695
uniprot
proteins
pubmed
8234324
uniprot
proteins
pubmed
8245005
uniprot
proteins
pubmed
8281941
uniprot
proteins
pubmed
8343525
uniprot
proteins
pubmed
8435445
uniprot
proteins
pubmed
9195951
uniprot
proteins
pubmed
9405046
uniprot
proteins
sequence_length
316
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm.
uniprot
proteins