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Literature summary 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)

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

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.79 0.38
-
 glyoxylate with NADPH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti
1.1.1.79 0.58
-
 glyoxylate with NADH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti
1.1.1.79 309
-
 glycolate with NAD+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
1.1.1.79 334
-
 glycolate with NADP+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.79 Acetobacter aceti
-
-
-
1.1.1.79 Acetobacter aceti JCM20276
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.79 463
-
 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
1.1.1.79 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.79 glycolate + NAD+ the reaction occurs only at pH 9.0 Acetobacter aceti glyoxylate + NADH + H+
-
 ?
1.1.1.79 glycolate + NAD+ the reaction occurs only at pH 9.0 Acetobacter aceti JCM20276 glyoxylate + NADH + H+
-
 ?
1.1.1.79 glycolate + NADP+ the reaction occurs only at pH 9.0 Acetobacter aceti glyoxylate + NAPDH + H+
-
 ?
1.1.1.79 glycolate + NADP+ the reaction occurs only at pH 9.0 Acetobacter aceti JCM20276 glyoxylate + NAPDH + H+
-
 ?
1.1.1.79 glyoxylate + NADH + H+ the specific activity with NADPH is slightly higher as that with NADH Acetobacter aceti glycolate + NAD+
-
 ?
1.1.1.79 glyoxylate + NADH + H+ the specific activity with NADPH is slightly higher as that with NADH Acetobacter aceti JCM20276 glycolate + NAD+
-
 ?
1.1.1.79 glyoxylate + NADPH + H+ the specific activity with NADPH is slightly higher as that with NADH Acetobacter aceti glycolate + NADP+
-
 ?
1.1.1.79 glyoxylate + NADPH + H+ the specific activity with NADPH is slightly higher as that with NADH Acetobacter aceti JCM20276 glycolate + NADP+
-
 ?
1.1.1.79 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 ?
-
-
1.1.1.79 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

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.79 45
-
-
 Acetobacter aceti

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.79 30 45 the enzyme shows relatively high activity over a broad temperature range (30-45°C) Acetobacter aceti

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.79 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.79 4.8
-
 glycolate with NAD+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
1.1.1.79 10
-
 glycolate with NADP+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
1.1.1.79 530
-
 glyoxylate with NADH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti
1.1.1.79 570
-
 glyoxylate with NADPH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.79 4
-
-
 Acetobacter aceti

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.79 3.5 8 approximately 50% of the activity is retained at a pH of 3.5 and 8.0, respectively Acetobacter aceti

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.79 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

EC Number Cofactor Comment Organism Structure
1.1.1.79 NADH
-
 Acetobacter aceti
1.1.1.79 NADPH
-
 Acetobacter aceti

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.79 0.048
-
 glycolate with NAD+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
1.1.1.79 0.1
-
 glycolate with NADP+ as cosubstrate, at pH 9.0 and 45°C Acetobacter aceti
1.1.1.79 910
-
 glyoxylate with NADH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti
1.1.1.79 1500
-
 glyoxylate with NADPH as cosubstrate, at pH 4.0 and 45°C Acetobacter aceti