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Literature summary for 1.1.1.283 extracted from

  • Borelli, G.; Fiamenghi, M.B.; Dos Santos, L.V.; Carazzolle, M.F.; Pereira, G.A.G.; Jose, J.
    Positive selection evidence in xylose-related genes suggests methylglyoxal reductase as a target for the improvement of yeasts fermentation in industry (2019), Genome Biol. Evol., 11, 1923-1938 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene CANTEDRAFT_112488 Yamadazyma tenuis
gene GRE2 Saccharomyces cerevisiae
gene GRE3 Saccharomyces cerevisiae
gene GRP2 Yarrowia lipolytica
gene PAS_chr3_0744 Komagataella phaffii

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
[Candida] boidinii 5829
-
cytosol
-
Lipomyces starkeyi 5829
-
cytosol
-
Candida tropicalis 5829
-
cytosol
-
Wickerhamomyces anomalus 5829
-
cytosol
-
Kluyveromyces lactis 5829
-
cytosol
-
Blastobotrys adeninivorans 5829
-
cytosol
-
[Candida] arabinofermentans 5829
-
cytosol
-
Saccharomyces cerevisiae 5829
-
cytosol
-
Komagataella phaffii 5829
-
cytosol
-
Yamadazyma tenuis 5829
-
cytosol
-
Yarrowia lipolytica 5829
-
cytosol
-
Candida sojae 5829
-
cytosol
-
Suhomyces tanzawaensis 5829
-
cytosol
-
Kazachstania africana 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methylglyoxal + NADPH + H+ [Candida] boidinii
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Lipomyces starkeyi
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Candida tropicalis
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Wickerhamomyces anomalus
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Kluyveromyces lactis
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Blastobotrys adeninivorans
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ [Candida] arabinofermentans
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Saccharomyces cerevisiae
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Komagataella phaffii
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yamadazyma tenuis
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yarrowia lipolytica
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Candida sojae
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Suhomyces tanzawaensis
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Kazachstania africana
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yamadazyma tenuis VKM Y-70
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yamadazyma tenuis BCRC 21748
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yamadazyma tenuis CBS 615
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Komagataella phaffii ATCC 20864
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Saccharomyces cerevisiae ATCC 204508
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yamadazyma tenuis NBRC 10315
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yamadazyma tenuis ATCC 10573
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Komagataella phaffii GS115
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yamadazyma tenuis JCM 9827
-
(S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+ Yamadazyma tenuis NRRL Y-1498
-
(S)-lactaldehyde + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Blastobotrys adeninivorans
-
Arxula adeninivorans
-
Candida sojae
-
-
-
Candida tropicalis
-
-
-
Kazachstania africana
-
-
-
Kluyveromyces lactis
-
-
-
Komagataella phaffii C4R5F8 Pichia pastoris
-
Komagataella phaffii ATCC 20864 C4R5F8 Pichia pastoris
-
Komagataella phaffii GS115 C4R5F8 Pichia pastoris
-
Lipomyces starkeyi
-
-
-
no activity in Dekkera bruxellensis
-
-
-
no activity in Schizosaccharomyces pombe
-
-
-
Saccharomyces cerevisiae P38715
-
-
Saccharomyces cerevisiae Q12068
-
-
Saccharomyces cerevisiae ATCC 204508 P38715
-
-
Saccharomyces cerevisiae ATCC 204508 Q12068
-
-
Suhomyces tanzawaensis
-
-
-
Wickerhamomyces anomalus
-
-
-
Yamadazyma tenuis G3AZL9 Yamadazyma tenuis
-
Yamadazyma tenuis ATCC 10573 G3AZL9 Yamadazyma tenuis
-
Yamadazyma tenuis BCRC 21748 G3AZL9 Yamadazyma tenuis
-
Yamadazyma tenuis CBS 615 G3AZL9 Yamadazyma tenuis
-
Yamadazyma tenuis JCM 9827 G3AZL9 Yamadazyma tenuis
-
Yamadazyma tenuis NBRC 10315 G3AZL9 Yamadazyma tenuis
-
Yamadazyma tenuis NRRL Y-1498 G3AZL9 Yamadazyma tenuis
-
Yamadazyma tenuis VKM Y-70 G3AZL9 Yamadazyma tenuis
-
Yarrowia lipolytica A0A1D8NEA1 Candida lipolytica
-
[Candida] arabinofermentans
-
-
-
[Candida] boidinii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methylglyoxal + NADPH + H+
-
[Candida] boidinii (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Lipomyces starkeyi (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Candida tropicalis (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Wickerhamomyces anomalus (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Kluyveromyces lactis (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Blastobotrys adeninivorans (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
[Candida] arabinofermentans (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Saccharomyces cerevisiae (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Komagataella phaffii (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yamadazyma tenuis (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yarrowia lipolytica (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Candida sojae (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Suhomyces tanzawaensis (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Kazachstania africana (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yamadazyma tenuis VKM Y-70 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yamadazyma tenuis BCRC 21748 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yamadazyma tenuis CBS 615 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Komagataella phaffii ATCC 20864 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Saccharomyces cerevisiae ATCC 204508 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yamadazyma tenuis NBRC 10315 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yamadazyma tenuis ATCC 10573 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Komagataella phaffii GS115 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yamadazyma tenuis JCM 9827 (S)-lactaldehyde + NADP+
-
?
methylglyoxal + NADPH + H+
-
Yamadazyma tenuis NRRL Y-1498 (S)-lactaldehyde + NADP+
-
?

Synonyms

Synonyms Comment Organism
CANTEDRAFT_112488
-
Yamadazyma tenuis
Gre2
-
Yamadazyma tenuis
Gre2
-
Saccharomyces cerevisiae
GRE3
-
Saccharomyces cerevisiae
GRP2
-
Yarrowia lipolytica
methylglyoxal reductase
-
[Candida] boidinii
methylglyoxal reductase
-
Lipomyces starkeyi
methylglyoxal reductase
-
Candida tropicalis
methylglyoxal reductase
-
Wickerhamomyces anomalus
methylglyoxal reductase
-
Kluyveromyces lactis
methylglyoxal reductase
-
Blastobotrys adeninivorans
methylglyoxal reductase
-
[Candida] arabinofermentans
methylglyoxal reductase
-
Saccharomyces cerevisiae
methylglyoxal reductase
-
Komagataella phaffii
methylglyoxal reductase
-
Yamadazyma tenuis
methylglyoxal reductase
-
Yarrowia lipolytica
methylglyoxal reductase
-
Candida sojae
methylglyoxal reductase
-
Suhomyces tanzawaensis
methylglyoxal reductase
-
Kazachstania africana
MGR
-
[Candida] boidinii
MGR
-
Lipomyces starkeyi
MGR
-
Candida tropicalis
MGR
-
Wickerhamomyces anomalus
MGR
-
Kluyveromyces lactis
MGR
-
Blastobotrys adeninivorans
MGR
-
[Candida] arabinofermentans
MGR
-
Saccharomyces cerevisiae
MGR
-
Komagataella phaffii
MGR
-
Yamadazyma tenuis
MGR
-
Yarrowia lipolytica
MGR
-
Candida sojae
MGR
-
Suhomyces tanzawaensis
MGR
-
Kazachstania africana
PAS_chr3_0744
-
Komagataella phaffii

Cofactor

Cofactor Comment Organism Structure
NADPH
-
[Candida] boidinii
NADPH
-
Lipomyces starkeyi
NADPH
-
Candida tropicalis
NADPH
-
Wickerhamomyces anomalus
NADPH
-
Kluyveromyces lactis
NADPH
-
Blastobotrys adeninivorans
NADPH
-
[Candida] arabinofermentans
NADPH
-
Saccharomyces cerevisiae
NADPH
-
Komagataella phaffii
NADPH
-
Yamadazyma tenuis
NADPH
-
Yarrowia lipolytica
NADPH
-
Candida sojae
NADPH
-
Suhomyces tanzawaensis
NADPH
-
Kazachstania africana

General Information

General Information Comment Organism
evolution the organism contains 1 MGR gene copy Lipomyces starkeyi
evolution the organism contains 2 MGR gene copies Kluyveromyces lactis
evolution the organism contains 2 MGR gene copies Yamadazyma tenuis
evolution the organism contains 3 MGR gene copies Candida sojae
evolution the organism contains 3 MGR gene copies Kazachstania africana
evolution the organism contains 4 MGR gene copies Blastobotrys adeninivorans
evolution the organism contains 4 MGR gene copies [Candida] arabinofermentans
evolution the organism contains 4 MGR gene copies Saccharomyces cerevisiae
evolution the organism contains 5 MGR gene copies [Candida] boidinii
evolution the organism contains 6 MGR gene copies Komagataella phaffii
evolution the organism contains 7 MGR gene copies Suhomyces tanzawaensis
evolution the organism contains 8 MGR gene copies Wickerhamomyces anomalus
evolution the organism contains 9 MGR gene copies Yarrowia lipolytica
evolution the organism contains diverse MGR gene copies Candida tropicalis
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview [Candida] boidinii
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Lipomyces starkeyi
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Candida tropicalis
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Wickerhamomyces anomalus
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Kluyveromyces lactis
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Blastobotrys adeninivorans
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview [Candida] arabinofermentans
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Saccharomyces cerevisiae
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Komagataella phaffii
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Yamadazyma tenuis
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Yarrowia lipolytica
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Candida sojae
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Suhomyces tanzawaensis
metabolism metabolic pathways related to xylose and glucose consumption involving methylgyoxal reductase, overview Kazachstania africana
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 [Candida] boidinii
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 Lipomyces starkeyi
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 Candida tropicalis
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 Wickerhamomyces anomalus
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 Kluyveromyces lactis
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 Blastobotrys adeninivorans
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 [Candida] arabinofermentans
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 Saccharomyces cerevisiae
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 Komagataella phaffii
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 Yamadazyma tenuis
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 Yarrowia lipolytica
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 Candida sojae
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 Suhomyces tanzawaensis
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 Kazachstania africana
physiological function model for MGR role in oxidative imbalance, overview [Candida] boidinii
physiological function model for MGR role in oxidative imbalance, overview Lipomyces starkeyi
physiological function model for MGR role in oxidative imbalance, overview Candida tropicalis
physiological function model for MGR role in oxidative imbalance, overview Wickerhamomyces anomalus
physiological function model for MGR role in oxidative imbalance, overview Kluyveromyces lactis
physiological function model for MGR role in oxidative imbalance, overview Blastobotrys adeninivorans
physiological function model for MGR role in oxidative imbalance, overview [Candida] arabinofermentans
physiological function model for MGR role in oxidative imbalance, overview Saccharomyces cerevisiae
physiological function model for MGR role in oxidative imbalance, overview Komagataella phaffii
physiological function model for MGR role in oxidative imbalance, overview Yamadazyma tenuis
physiological function model for MGR role in oxidative imbalance, overview Yarrowia lipolytica
physiological function model for MGR role in oxidative imbalance, overview Candida sojae
physiological function model for MGR role in oxidative imbalance, overview Suhomyces tanzawaensis
physiological function model for MGR role in oxidative imbalance, overview Kazachstania africana