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Literature summary for 1.1.1.79 extracted from

  • Kumsab, J.; Tobe, R.; Kurihara, T.; Hirose, Y.; Omori, T.; Mihara, H.
    Characterization of a novel class of glyoxylate reductase belonging to the beta-hydroxyacid dehydrogenase family in Acetobacter aceti (2020), Biosci. Biotechnol. Biochem., 84, 2303-2310 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Acetobacter aceti

Inhibitors

Inhibitors Comment Organism Structure
ethanol enzyme activity is decreased to 20% by incubation with 60% (v/v) ethanol Acetobacter aceti
Fe3+ 15% inhibition at 1 mM Acetobacter aceti
Hg2+ 30% inhibition at 1 mM Acetobacter aceti

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.38
-
glyoxylate with NADPH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti
0.58
-
glyoxylate with NADH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti
309
-
glycolate with NAD+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
334
-
glycolate with NADP+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glyoxylate + NADH + H+ Acetobacter aceti the specific activity with NADPH is slightly higher as that with NADH glycolate + NAD+
-
?
glyoxylate + NADH + H+ Acetobacter aceti JCM20276 the specific activity with NADPH is slightly higher as that with NADH glycolate + NAD+
-
?
glyoxylate + NADPH + H+ Acetobacter aceti the specific activity with NADPH is slightly higher as that with NADH glycolate + NADP+
-
?
glyoxylate + NADPH + H+ Acetobacter aceti JCM20276 the specific activity with NADPH is slightly higher as that with NADH glycolate + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Acetobacter aceti
-
-
-
Acetobacter aceti JCM20276
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Acetobacter aceti

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
463
-
crude extract, the reaction mixture contains 100 mM citrate buffer (pH 4.0), 1 mM glyoxylate, and 0.15 mM NADPH at 45°C Acetobacter aceti
1300
-
after 2.81fold purification, the reaction mixture contains 100 mM citrate buffer (pH 4.0), 1 mM glyoxylate, and 0.15 mM NADPH at 45°C Acetobacter aceti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycolate + NAD+ the reaction occurs only at pH 9.0 Acetobacter aceti glyoxylate + NADH + H+
-
?
glycolate + NAD+ the reaction occurs only at pH 9.0 Acetobacter aceti JCM20276 glyoxylate + NADH + H+
-
?
glycolate + NADP+ the reaction occurs only at pH 9.0 Acetobacter aceti glyoxylate + NAPDH + H+
-
?
glycolate + NADP+ the reaction occurs only at pH 9.0 Acetobacter aceti JCM20276 glyoxylate + NAPDH + H+
-
?
glyoxylate + NADH + H+ the specific activity with NADPH is slightly higher as that with NADH Acetobacter aceti glycolate + NAD+
-
?
glyoxylate + NADH + H+ the specific activity with NADPH is slightly higher as that with NADH Acetobacter aceti JCM20276 glycolate + NAD+
-
?
glyoxylate + NADPH + H+ the specific activity with NADPH is slightly higher as that with NADH Acetobacter aceti glycolate + NADP+
-
?
glyoxylate + NADPH + H+ the specific activity with NADPH is slightly higher as that with NADH Acetobacter aceti JCM20276 glycolate + NADP+
-
?
additional information the enzyme exhibits no activity against succinic semialdehyde, hydroxypyruvate, formate, acetate, oxalate, 3-hydroxypropionate, DL-glycerate, pyruvate, and phenylpyruvate, formaldehyde, acetaldehyde, glutaraldehyde, glyoxal, methylglyoxal, and phenylglyoxal. The enzyme does not catalyze NAD(P)+-dependent glycolate oxidation at pH 4.0 and 7.0. DL-lactate, L-malate, (S)-hydroxyisobutyrate, and (R)-hydroxyisobutyrate, D-serine, L-serine, D-threonine, and L-threonine are inert as substrates of the enzyme when examined at pH of 4.0, 6.0, and 9.0 Acetobacter aceti ?
-
-
additional information the enzyme exhibits no activity against succinic semialdehyde, hydroxypyruvate, formate, acetate, oxalate, 3-hydroxypropionate, DL-glycerate, pyruvate, and phenylpyruvate, formaldehyde, acetaldehyde, glutaraldehyde, glyoxal, methylglyoxal, and phenylglyoxal. The enzyme does not catalyze NAD(P)+-dependent glycolate oxidation at pH 4.0 and 7.0. DL-lactate, L-malate, (S)-hydroxyisobutyrate, and (R)-hydroxyisobutyrate, D-serine, L-serine, D-threonine, and L-threonine are inert as substrates of the enzyme when examined at pH of 4.0, 6.0, and 9.0 Acetobacter aceti JCM20276 ?
-
-

Subunits

Subunits Comment Organism
? x * 328000, calculated from amino acid sequence Acetobacter aceti
? x * 330000, SDS-PAGE Acetobacter aceti

Synonyms

Synonyms Comment Organism
aac4036
-
Acetobacter aceti
glyoxylate reductase
-
Acetobacter aceti
NAD(P)H-dependent GR
-
Acetobacter aceti

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
Acetobacter aceti

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 45 the enzyme shows relatively high activity over a broad temperature range (30-45°C) Acetobacter aceti

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
the enzyme retains 90% activity at up to 65°C for 10 min and inactivated rapidly when the temperature exceeds 70°C Acetobacter aceti

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.8
-
glycolate with NAD+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
10
-
glycolate with NADP+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
530
-
glyoxylate with NADH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti
570
-
glyoxylate with NADPH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
-
Acetobacter aceti

pH Range

pH Minimum pH Maximum Comment Organism
3.5 8 approximately 50% of the activity is retained at a pH of 3.5 and 8.0, respectively Acetobacter aceti

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 11 more than 80% of the activity is retained over the pH range of 4.0-11.0 for 1 h on ice Acetobacter aceti

Cofactor

Cofactor Comment Organism Structure
NADH
-
Acetobacter aceti
NADPH
-
Acetobacter aceti

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.048
-
glycolate with NAD+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
0.1
-
glycolate with NADP+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
910
-
glyoxylate with NADH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti
1500
-
glyoxylate with NADPH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti