1.1.1.283: methylglyoxal reductase (NADPH)
This is an abbreviated version!
For detailed information about methylglyoxal reductase (NADPH), go to the full flat file.
Word Map on EC 1.1.1.283
Reaction
Synonyms
AKR, aldo-keto reductase, AlrA, CaGre2, CANTEDRAFT_112488, D-lactaldehyde dehydrogenase, EC 1.1.1.78, Gre2, GRE2 gene product, GRE2/YOL151W, Gre2p, GRE3, GRP2, Lbuc_0522, MeGR, Mer, methylglyoxal reductase, methylglyoxal reductase (NADPH dependent), methylglyoxal/isovaleraldehyde reductase, MG reductase, MG-specific aldolase reductase, MGR, More, NADPH-dependent methylglyoxal reductase, NADPH-linked aldolase reductase, PAS_chr3_0744, SakR1, YGL039w1, YGL039w2, YOL151W, YOL151w gene product
ECTree
1.1.1.283 methylglyoxal reductase (NADPH)Advanced search results
results (
results (General Information
General Information on EC 1.1.1.283 - methylglyoxal reductase (NADPH)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
glutathione (GSH)-deprived Dictyostelium discoideum accumulates methylglyoxal (MG) and reactive oxygen species (ROS) during vegetative growth. MG increases after the mound stage in this strain, with a 2.6fold increase compared to early developmental stages. gamma-Glutamylcysteine synthetase overexpressing (gcsAOE) slugs trigger glutahione reductase (Gsr) and aldolase reductase activity to detoxify MG, while superoxide dismutase overexpressing (sod2OE) and catalase overexpressing (catAOE) slugs mainly decrease cellular ROS levels. The MG-specific activity of NADPH-linked aldolase reductase shows a noticeable increase in the gcsAOE slugs, indicating enhanced MG-scavenging reductase activity in gcsAOE slugs. In contrast to the increase observed in migrating sod2OE and catAOE slugs by treatment with MG and H2O2, the migration of gcsAOE slugs appeas unaffected. This behavior is caused by MG-triggered Gsr and NADPH-linked aldolase reductase activity, suggesting that GSH biosynthesis in gcsAOE slugs is specifically used for MG-scavenging activity
metabolism
physiological function
additional information
evolution
the enzyme belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, which includes various oxidoreductases, some isomerases and lyases
evolution
the enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. The 3D structures of SDR enzymes all display a typical Rossman fold for cofactor binding with highly similar alpha/beta patterns and a central beta-sheet. Furthermore, the key active site, a catalytic triad of Tyr, Lys, and Ser, is found in almost all SDR forms
evolution
-
the enzyme is a member of the short-chain dehydrogenase/reductase (SDR) superfamily. The 3D structures of SDR enzymes all display a typical Rossman fold for cofactor binding with highly similar alpha/beta patterns and a central beta-sheet. Furthermore, the key active site, a catalytic triad of Tyr, Lys, and Ser, is found in almost all SDR forms
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
Yamadazyma tenuis BCRC 21748
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
Yamadazyma tenuis NBRC 10315
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
metabolism
-
metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview
-
physiological function
in strains lacking Gre2 activity, which are subjected to environmental stress straining the cell membrane, growth is significantly and exclusively reduced. No compensatory mechanisms are activated due to loss of Gre2p during growth in favourable conditions (synthetic defined media, no stress), but a striking and highly specific induction of the ergosterol biosynthesis pathway, enzymes Erg10, Erg19 and Erg6, is observed in Gre2 mutant strains during growth in a stress conditions in which lack of Gre2 significantly affects growth. Mutant strains display vastly impaired tolerance exclusively to agents targeting the ergosterol biosynthesis
physiological function
the Saccharomyces cerevisiae enzyme serves as a versatile enzyme that catalyzes the stereoselective reduction of a broad range of substrates including aliphatic and aromatic ketones, diketones, as well as aldehydes, using NADPH as the cofactor
physiological function
Gre2 is a key enzyme in the methylglyoxal detoxification pathway. It uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde
physiological function
methylglyoxal (MG) upregulates slug migration via MG-scavenging-mediated differentiation
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
model for MGR role in oxidative imbalance, overview
physiological function
model for MGR role in oxidative imbalance, overview
physiological function
model for MGR role in oxidative imbalance, overview
physiological function
model for MGR role in oxidative imbalance, overview
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
-
model for MGR role in oxidative imbalance, overview
physiological function
-
the enzyme is involved in detoxification of methylglyoxal (MG), a cytotoxic by-product of glycolysis that is identified as a potential glycolytic inhibitor, which inhibits the growth of glucose-fermenting yeast cells by promoting degradation of the glucose sensors. The MG reductase gene has been reported to play a critical role in maintaining redox balance during ethanol fermentation in yeasts
physiological function
-
model for MGR role in oxidative imbalance, overview
-
physiological function
-
the enzyme is involved in detoxification of methylglyoxal (MG), a cytotoxic by-product of glycolysis that is identified as a potential glycolytic inhibitor, which inhibits the growth of glucose-fermenting yeast cells by promoting degradation of the glucose sensors. The MG reductase gene has been reported to play a critical role in maintaining redox balance during ethanol fermentation in yeasts
-
physiological function
Yamadazyma tenuis BCRC 21748
-
model for MGR role in oxidative imbalance, overview
-
physiological function
-
model for MGR role in oxidative imbalance, overview
-
physiological function
-
model for MGR role in oxidative imbalance, overview
-
physiological function
-
Gre2 is a key enzyme in the methylglyoxal detoxification pathway. It uses NADPH or NADH as an electron donor to reduce the cytotoxic methylglyoxal to lactaldehyde
-
physiological function
-
model for MGR role in oxidative imbalance, overview
-
physiological function
Yamadazyma tenuis NBRC 10315
-
model for MGR role in oxidative imbalance, overview
-
physiological function
-
model for MGR role in oxidative imbalance, overview
-
physiological function
-
model for MGR role in oxidative imbalance, overview
-
physiological function
-
model for MGR role in oxidative imbalance, overview
-
physiological function
-
model for MGR role in oxidative imbalance, overview
-
additional information
Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate. The substrate-binding pocket structure determines the stringent substrate stereoselectivity for catalysis
additional information
-
Gre2 forms a homodimer, each subunit of which contains an N-terminal Rossmann-fold domain and a variable C-terminal domain, which participates in substrate recognition. The induced fit upon binding to the cofactor NADPH makes the two domains shift toward each other, producing an interdomain cleft that better fits the substrate. The substrate-binding pocket structure determines the stringent substrate stereoselectivity for catalysis
additional information
enzyme sequence and structure comparisons, overview
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
Yamadazyma tenuis BCRC 21748
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
enzyme sequence and structure comparisons, overview
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
Yamadazyma tenuis NBRC 10315
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
additional information
-
evolutionary analysis suited for comparative genomics of xylose-consuming yeasts, searching for of positive selection on genes associated with glucose and xylose metabolism in the xylose-fermenters' clade. Expansion, positive selectionmarks, and convergence as evidence supporting the hypothesis that natural selection is shaping the evolution of the methylglyoxal reductases. A metabolic model suggests that selected codons among these proteins cause a putative change in cofactor preference from NADPH to NADH that alleviates cellular redox imbalance
-
