Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.265 extracted from

  • Ouyang, Y.; Li, Q.; Kuang, X.; Wang, H.; Wu, J.; Ayepa, E.; Chen, H.; Abrha, G.; Zhang, Z.; Li, X.; Ma, M.
    YMR152W from Saccharomyces cerevisiae encoding a novel aldehyde reductase for detoxification of aldehydes derived from lignocellulosic biomass (2021), J. Biosci. Bioeng., 131, 39-46 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene YMR152W, sequence comparison and phylogenetic analysis Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol inhibition level depends on the substrate used, about 40% inhibition at 10 mM Saccharomyces cerevisiae
Ag+
-
Saccharomyces cerevisiae
Al3+
-
Saccharomyces cerevisiae
Ca2+ slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate Saccharomyces cerevisiae
Co2+
-
Saccharomyces cerevisiae
Cu2+
-
Saccharomyces cerevisiae
Fe3+
-
Saccharomyces cerevisiae
KCl
-
Saccharomyces cerevisiae
Mg2+ slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate Saccharomyces cerevisiae
Mn2+
-
Saccharomyces cerevisiae
additional information the strength of inhibition by metal ions depends on the substrate used, overview Saccharomyces cerevisiae
NaCl
-
Saccharomyces cerevisiae
Ni2+
-
Saccharomyces cerevisiae
Zn2+
-
Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.74
-
acetaldehyde pH 7.0, 30┬░C Saccharomyces cerevisiae
16.11
-
glycolaldehyde pH 7.0, 30┬░C Saccharomyces cerevisiae
97.37
-
furfural pH 7.0, 30┬░C Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Saccharomyces cerevisiae 5783
-
lipid droplet
-
Saccharomyces cerevisiae 5811
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate Saccharomyces cerevisiae
Mg2+ slight inhibition at 2 mM, slight activation at 0.5 mM, dependent on the substrate Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-methylbutanal + NADPH + H+ Saccharomyces cerevisiae
-
3-methylbutanol + NADP+
-
r
5-hydroxymethylfurfural + NADH + H+ Saccharomyces cerevisiae
-
2,5-dihydroxymethylfurane + NAD+
-
r
acetaldehyde + NADH + H+ Saccharomyces cerevisiae
-
ethanol + NAD+
-
r
acetaldehyde + NADH + H+ Saccharomyces cerevisiae ATCC 204508
-
ethanol + NAD+
-
r
benzaldehyde + NADPH + H+ Saccharomyces cerevisiae
-
benzylalcohol + NADP+
-
r
benzaldehyde + NADPH + H+ Saccharomyces cerevisiae ATCC 204508
-
benzylalcohol + NADP+
-
r
furfural + NADH + H+ Saccharomyces cerevisiae
-
furfuryl alcohol + NAD+
-
r
furfural + NADH + H+ Saccharomyces cerevisiae ATCC 204508
-
furfuryl alcohol + NAD+
-
r
glycolaldehyde + NADH + H+ Saccharomyces cerevisiae
-
ethylene glycol + NAD+
-
r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P28625
-
-
Saccharomyces cerevisiae ATCC 204508 P28625
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [┬Ámol/min/mg] Specific Activity Maximum [┬Ámol/min/mg] Comment Organism
0.74
-
substrate 3-methylbutanal, pH 7.0, 30┬░C Saccharomyces cerevisiae
1.12
-
substrate benzaldehyde, pH 7.0, 30┬░C Saccharomyces cerevisiae
1.74
-
substrate 5-hydroxymethylfurfural, pH 7.0, 30┬░C Saccharomyces cerevisiae
5.05
-
substrate furfural, pH 7.0, 30┬░C Saccharomyces cerevisiae
9.64
-
substrate glycolaldehyde, pH 7.0, 30┬░C Saccharomyces cerevisiae
190.86
-
substrate acetaldegyde, pH 7.0, 30┬░C Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methylbutanal + NADPH + H+
-
Saccharomyces cerevisiae 3-methylbutanol + NADP+
-
r
3-methylbutanal + NADPH + H+ low activity Saccharomyces cerevisiae 3-methylbutanol + NADP+
-
r
5-hydroxymethylfurfural + NADH + H+
-
Saccharomyces cerevisiae 2,5-dihydroxymethylfurane + NAD+
-
r
acetaldehyde + NADH + H+
-
Saccharomyces cerevisiae ethanol + NAD+
-
r
acetaldehyde + NADH + H+ best substrate Saccharomyces cerevisiae ethanol + NAD+
-
r
acetaldehyde + NADH + H+
-
Saccharomyces cerevisiae ATCC 204508 ethanol + NAD+
-
r
acetaldehyde + NADH + H+ best substrate Saccharomyces cerevisiae ATCC 204508 ethanol + NAD+
-
r
benzaldehyde + NADPH + H+
-
Saccharomyces cerevisiae benzylalcohol + NADP+
-
r
benzaldehyde + NADPH + H+ low activity Saccharomyces cerevisiae benzylalcohol + NADP+
-
r
benzaldehyde + NADPH + H+
-
Saccharomyces cerevisiae ATCC 204508 benzylalcohol + NADP+
-
r
furfural + NADH + H+
-
Saccharomyces cerevisiae furfuryl alcohol + NAD+
-
r
furfural + NADH + H+
-
Saccharomyces cerevisiae ATCC 204508 furfuryl alcohol + NAD+
-
r
glycolaldehyde + NADH + H+
-
Saccharomyces cerevisiae ethylene glycol + NAD+
-
r
additional information Ymr152wp catalyzes reactions for reduction of acetaldehyde, glycolaldehyde, furfural, and 5-hydroxymethylfurfural (HMF) when NADH is used as the cofactor. Besides, enzyme activity is detected for reduction of benzaldehyde (BZA) and 3-methylbutanal (MBA) when NADPH is used as the cofactor. Ymr152wp shows the highest specific enzyme activity (190.86 U/mg) for reduction of acetaldehyde, followed by glycolaldehyde (9.64 U/mg), furfural (5.05 U/mg), HMF (1.74 U/mg), BZA (1.12 U/mg), and MBA (0.74 U/mg). No activity with formaldehyde, propionaldehyde, butyraldehyde, glutaraldehyde, quinone, 1,2-naphthoquinone, 9,10-phenanthrenequinone, 4-benzoquinone, acetone, and acetylacetone, neither with NADH, nor with NADPH Saccharomyces cerevisiae ?
-
-
additional information Ymr152wp catalyzes reactions for reduction of acetaldehyde, glycolaldehyde, furfural, and 5-hydroxymethylfurfural (HMF) when NADH is used as the cofactor. Besides, enzyme activity is detected for reduction of benzaldehyde (BZA) and 3-methylbutanal (MBA) when NADPH is used as the cofactor. Ymr152wp shows the highest specific enzyme activity (190.86 U/mg) for reduction of acetaldehyde, followed by glycolaldehyde (9.64 U/mg), furfural (5.05 U/mg), HMF (1.74 U/mg), BZA (1.12 U/mg), and MBA (0.74 U/mg). No activity with formaldehyde, propionaldehyde, butyraldehyde, glutaraldehyde, quinone, 1,2-naphthoquinone, 9,10-phenanthrenequinone, 4-benzoquinone, acetone, and acetylacetone, neither with NADH, nor with NADPH Saccharomyces cerevisiae ATCC 204508 ?
-
-

Synonyms

Synonyms Comment Organism
aldehyde reductase
-
Saccharomyces cerevisiae
protein YIM1
-
Saccharomyces cerevisiae
YIM1
-
Saccharomyces cerevisiae
YMR152W
-
Saccharomyces cerevisiae
Ymr152wp
-
Saccharomyces cerevisiae

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
25 30
-
Saccharomyces cerevisiae

Temperature Range [┬░C]

Temperature Minimum [┬░C] Temperature Maximum [┬░C] Comment Organism
20 50 70% of maximal activity at 20┬░C, maximal activity at 25-30┬░C, low activity at 60┬░C Saccharomyces cerevisiae

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
60
-
Ymr152wp completely loses its catalytic activities for reduction of furfural after incubation at 60┬░C for 15 min, and for reduction of acetaldehyde and glycolaldehyde after incubation at 60┬░C for 30 min Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
15.44
-
glycolaldehyde pH 7.0, 30┬░C Saccharomyces cerevisiae
36.9
-
furfural pH 7.0, 30┬░C Saccharomyces cerevisiae
313.14
-
acetaldehyde pH 7.0, 30┬░C Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 6 optimum pH of Ymr152wp is acidic at pH 5.0-6.0, but this enzyme is more stable in alkaline conditions at pH 8.0, relative activity of Ymr152wp drops quickly under alkaline conditions from pH 7.0 to pH 9.0. The highest enzyme activity of Ymr152wp is observed at pH 5.5 with furfural as substrate, 15% of maximal activity at pH 9.0, 40% at pH 6.5. The optimum pH for reduction of glycolaldehyde is pH 6.0.showing more than 80% of its maximal enzyme activity at pH 4.5-8.5 Saccharomyces cerevisiae

pH Stability

pH Stability pH Stability Maximum Comment Organism
8
-
optimum pH of Ymr152wp is acidic at pH 5.0-6.0, but this enzyme is more stable in alkaline conditions at pH 8.0 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces cerevisiae
NADP+
-
Saccharomyces cerevisiae
NADPH
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution phylogenetic analysis indicates that Ymr152wp and selected proteins similar to Ymr152wp are classified into the MDR family, which is close to the QOR subfamily and the LTD subfamily, but is far from the zinc-containing subfamilies of the ADH subfamily, the CADH subfamily, and the YADH subfamily in the genetic tree Saccharomyces cerevisiae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.39
-
furfural pH 7.0, 30┬░C Saccharomyces cerevisiae
0.96
-
glycolaldehyde pH 7.0, 30┬░C Saccharomyces cerevisiae
423.16
-
acetaldehyde pH 7.0, 30┬░C Saccharomyces cerevisiae