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Literature summary for 1.1.1.1 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
Search for more literature for 1.1.1.1

Cloned(Commentary)

Cloned (Comment) Organism
gene YIM1, cloned from Saccharomyces cerevisiae strain BY4742, DNA and amino acid sequence determination and analysis, recombinant expression in Saccharomyces cerevisiae strain INVSc1 Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol 60% inhibition at 10 mM Saccharomyces cerevisiae
acetaldehyde slight inhibition Saccharomyces cerevisiae
Ag+ 80% inhibition at 1 mM Saccharomyces cerevisiae
Al3+ slight inhibition at 0.5 mM Saccharomyces cerevisiae
Ca2+ 49.0% inhibition at 2.0 mM Saccharomyces cerevisiae
Co2+ 32.0% inhibition at 1.0 mM Saccharomyces cerevisiae
Cu2+ over 90% inhibition at 0.25 mM Saccharomyces cerevisiae
Fe2+ 34.3% inhibition at 1.0 mM Saccharomyces cerevisiae
glycolaldehyde slight inhibition Saccharomyces cerevisiae
KCl slight inhibition Saccharomyces cerevisiae
Mg2+ 38.2% inhibition at 2.0 mM Saccharomyces cerevisiae
Mn2+ 94.8% inhibition at 2.0 mM Saccharomyces cerevisiae
NaCl strong inhibition Saccharomyces cerevisiae
Ni2+ 55.8% inhibition at 2.0 mM Saccharomyces cerevisiae
Zn2+ 65.2% inhibition at 0.5 mM Saccharomyces cerevisiae

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetaldehyde + NADH + H+ Saccharomyces cerevisiae
-
 ethanol + NAD+
-
 ?

Organism

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.74
-
 pH 7.0, 30°C, substrate 3.methylbutanal with NADPH Saccharomyces cerevisiae
1.12
-
 pH 7.0, 30°C, substrate benzaldehyde with NADPH Saccharomyces cerevisiae
1.74
-
 pH 7.0, 30°C, substrate 5-hydroxymethylfurfural with NADH Saccharomyces cerevisiae
5.05
-
 pH 7.0, 30°C, substrate furfural with NADH Saccharomyces cerevisiae
9.64
-
 pH 7.0, 30°C, substrate glycolaldehyde with NADH Saccharomyces cerevisiae
190.86
-
 pH 7.0, 30°C, substrate acetaldehyde with NADH Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-methylbutanal + NADPH + H+ low activity, reaction of EC 1.1.1.2 Saccharomyces cerevisiae 3-methylbutanol + NADP+
-
 ir
5-hydroxymethylfurfural + NADH + H+ low activity Saccharomyces cerevisiae 5-hydroxymethylfurfuryl alcohol + NAD+
-
 ir
acetaldehyde + NADH + H+
-
 Saccharomyces cerevisiae ethanol + NAD+
-
 ?
acetaldehyde + NADH + H+ preferred substrates Saccharomyces cerevisiae ethanol + NAD+
-
 ir
benzacetaldehyde + NADPH + H+ low activity, reaction of EC 1.1.1.2 Saccharomyces cerevisiae benzol + NADP+
-
 ir
furfural + NADH + H+ low activity Saccharomyces cerevisiae furfuryl alcohol + NAD+
-
 ir
glycolaldehyde + NADH + H+ low activity Saccharomyces cerevisiae glycol + NAD+
-
 ir
additional information the enzyme acts as aldehyde reductase with catalytic functions for reduction of at least six aldehydes, including two furan aldehydes (furfural and 5-hydroxymethylfurfural), three aliphatic aldehydes (acetaldehyde, glycolaldehyde, and 3-methylbutanal), and an aromatic aldehyde (benzaldehyde) with NADH or NADPH as the cofactor. Particularly, Ymr152wp displays the highest specific activity (190.86 U/mg), and the best catalytic rate constant (Kcat), catalytic efficiency (Kcat/Km), and affinity (Km) when acetaldehyde is used as the substrate with NADH as the cofactor. Although Ymr152wp is grouped into the QOR family, no quinone reductase activity was observed using typical quinones as the substrates. No activity with formaldehyde, propionaldehyde, butyraldehyde, glutaraldehyde, 1,2-naphthoquinone, 9,10-phenanthrenequinone, p-benzoquinone, acetone, and acetylacetone. Substrate specificity, overview Saccharomyces cerevisiae ?
-
-

Synonyms

Synonyms Comment Organism
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
25 60 inactive above Saccharomyces cerevisiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 purified recombinant enzyme 6 h, 70% activity remaining Saccharomyces cerevisiae
60
-
 purified recombinant enzyme 15 min, inactivation 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, with NADH Saccharomyces cerevisiae
36.9
-
 furfural pH 7.0, 30°C, with NADH Saccharomyces cerevisiae
313.14
-
 acetaldehyde pH 7.0, 30°C, with NADH Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
4.5 9 high catalytic activity within the range of pH 4.5-6.5, relative activity of Ymr152wp dropped quickly under alkaline conditions of pH 7.0-9.0, 40% of maximal activity at pH 4.5, 15% at pH 9.0 Saccharomyces cerevisiae

pH Stability

pH Stability pH Stability Maximum Comment Organism
8
-
 the enzyme is more stable in alkaline conditions Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
additional information no enzyme activities are detected when NAD+ or NADP+ are used as the cofactor Saccharomyces cerevisiae
NADH preferred cofactor Saccharomyces cerevisiae
NADPH low activity with, cf. Ec 1.1.1.2 Saccharomyces cerevisiae

General Information

General Information Comment Organism
evolution the enzyme belongs to the quinone oxidoreductase (QOR) subfamily of the medium-chain dehydrogenase/reductase (MDR) family based on the results of amino acid sequence analysis and phylogenetic analysis Saccharomyces cerevisiae

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.38
-
 furfural pH 7.0, 30°C, with NADH Saccharomyces cerevisiae
0.96
-
 glycolaldehyde pH 7.0, 30°C, with NADH Saccharomyces cerevisiae
423.16
-
 acetaldehyde pH 7.0, 30°C, with NADH Saccharomyces cerevisiae