P38715 · GRE3_YEAST
- ProteinNADPH-dependent aldose reductase GRE3
- GeneGRE3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids327 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Aldose reductase with a broad substrate specificity. Reduces the cytotoxic compound methylglyoxal (MG) to acetol and (R)-lactaldehyde under stress conditions. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation (PubMed:11525399).
In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction (Probable) (PubMed:11722921).
In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction (Probable) (PubMed:11722921).
Miscellaneous
Present with 12851 molecules/cell in log phase SD medium.
'De respuesta a estres' means stress response in Spanish.
Catalytic activity
- an alditol + NAD+ = an aldose + H+ + NADH
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.046 mM | p-nitrobenzaldehyde | |||||
1.44 mM | D-L-glyceraldehyde | |||||
1.57 mM | D-glyceraldehyde | |||||
6.38 mM | L-glyceraldehyde | |||||
27.9 mM | D-xylose | |||||
32.63 mM | L-arabinose | |||||
9.34 mM | D-glucose | |||||
0.013 mM | NADPH |
pH Dependence
Optimum pH is 5.
Features
Showing features for active site, site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | aldose reductase (NADPH) activity | |
Molecular Function | D-xylose reductase (NADPH) activity | |
Molecular Function | mRNA binding | |
Biological Process | arabinose catabolic process | |
Biological Process | cellular response to osmotic stress | |
Biological Process | cellular response to oxidative stress | |
Biological Process | D-xylose catabolic process | |
Biological Process | galactose catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADPH-dependent aldose reductase GRE3
- EC number
- Short namesAR
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38715
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000124678 | 2-327 | NADPH-dependent aldose reductase GRE3 | |||
Sequence: SSLVTLNNGLKMPLVGLGCWKIDKKVCANQIYEAIKLGYRLFDGACDYGNEKEVGEGIRKAISEGLVSRKDIFVVSKLWNNFHHPDHVKLALKKTLSDMGLDYLDLYYIHFPIAFKYVPFEEKYPPGFYTGADDEKKGHITEAHVPIIDTYRALEECVDEGLIKSIGVSNFQGSLIQDLLRGCRIKPVALQIEHHPYLTQEHLVEFCKLHDIQVVAYSSFGPQSFIEMDLQLAKTTPTLFENDVIKKVSQNHPGSTTSQVLLRWATQRGIAVIPKSSKKERLLGNLEIEKKFTLTEQELKDISALNANIRFNDPWTWLDGKFPTFA |
Proteomic databases
PTM databases
Expression
Induction
By osmotic, ionic, oxidative and heat stress.
Structure
Sequence
- Sequence statusComplete
- Length327
- Mass (Da)37,119
- Last updated1995-02-01 v1
- ChecksumAFE72B8E2DFB91C8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00059 EMBL· GenBank· DDBJ | AAB68858.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006934 EMBL· GenBank· DDBJ | DAA06798.1 EMBL· GenBank· DDBJ | Genomic DNA |