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Literature summary for 1.1.1.71 extracted from

  • Sugimoto, C.; Takeda, K.; Kariya, Y.; Matsumura, H.; Yohda, M.; Ohno, H.; Nakamura, N.
    A method of expression for an oxygen-tolerant group III alcohol dehydrogenase from Pyrococcus horikoshii OT3 (2017), J. Biol. Inorg. Chem., 22, 527-534 .
    View publication on PubMed
Search for more literature for 1.1.1.71

Cloned(Commentary)

Cloned (Comment) Organism
gene PH0743, recombinant expression of StrepII-tagged enzyme in Escherichia coli strain BL21(DE3) Pyrococcus horikoshii

Inhibitors

Inhibitors Comment Organism Structure
additional information the Fe2+-reconstituted Ni-PhADH was sensitively and rapidly inactivated by dioxygen gas. The enzyme is inactivated by the replacement of the ferrous ion in the active site with another metal ion such as a zinc ion, which has been considered an inhibitor of iron-activating group III ADHs Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Pyrococcus horikoshii
0.011
-
 NADH substrates NADH and butanal, pH 5.5, 30°C Pyrococcus horikoshii
0.03
-
 NAD+ substrates NAD+ and 1-butanol, pH 9.0, 30°C Pyrococcus horikoshii
0.09
-
 pentanal substrates NADH and pentanal, pH 5.5, 30°C Pyrococcus horikoshii
0.25
-
 Butanal substrates NADH and butanal, pH 5.5, 30°C Pyrococcus horikoshii
0.52
-
 1-butanol substrates NAD+ and 1-butanol, pH 9.0, 30°C Pyrococcus horikoshii
0.52
-
 NADPH substrates NADPH and butanal, pH 5.5, 30°C Pyrococcus horikoshii
2.77
-
 propanal substrates NADH and propanal, pH 5.5, 30°C Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol Pyrococcus horikoshii
Fe2+ moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol Pyrococcus horikoshii
Fe3+ moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol Pyrococcus horikoshii
Mn2+ moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol Pyrococcus horikoshii
additional information no activity with Ca2+, Mg2+, Zn2+, and Cu2+. The Fe2+-reconstituted Ni-PhADH is sensitively and rapidly inactivated by dioxygen gas. The activity of apoform o-PhADH is significantly lower than that of Ni2+-bound PhADH. The enzyme is inactivated by the replacement of the ferrous ion in the active site with another metal ion such as a zinc ion, which has been considered an inhibitor of iron-activating group III ADHs Pyrococcus horikoshii
Ni2+ required for reduction of butanal, activates, but only slightly in oxidation of 1-butanol Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58517
-
-
Pyrococcus horikoshii ATCC 700860 O58517
-
-
Pyrococcus horikoshii DSM 12428 O58517
-
-
Pyrococcus horikoshii JCM 9974 O58517
-
-
Pyrococcus horikoshii NBRC 100139 O58517
-
-
Pyrococcus horikoshii OT-3 O58517
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant StrepII-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography, ultrafiltration, and gel filtration Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-propanediol + NAD+
-
 Pyrococcus horikoshii ? + NADH + H+
-
 r
1,3-propanediol + NAD+
-
 Pyrococcus horikoshii ? + NADH + H+
-
 r
1,4-butanediol + NAD+
-
 Pyrococcus horikoshii ? + NADH + H+
-
 r
1-butanol + NAD+
-
 Pyrococcus horikoshii butanal + NADH + H+
-
 r
1-butanol + NAD+
-
 Pyrococcus horikoshii DSM 12428 butanal + NADH + H+
-
 r
1-butanol + NAD+
-
 Pyrococcus horikoshii NBRC 100139 butanal + NADH + H+
-
 r
1-butanol + NAD+
-
 Pyrococcus horikoshii JCM 9974 butanal + NADH + H+
-
 r
1-butanol + NAD+
-
 Pyrococcus horikoshii ATCC 700860 butanal + NADH + H+
-
 r
1-butanol + NAD+
-
 Pyrococcus horikoshii OT-3 butanal + NADH + H+
-
 r
1-butanol + NADP+
-
 Pyrococcus horikoshii butanal + NADPH + H+
-
 r
1-heptanol + NAD+
-
 Pyrococcus horikoshii heptanal + NADH + H+
-
 r
1-heptanol + NAD+
-
 Pyrococcus horikoshii DSM 12428 heptanal + NADH + H+
-
 r
1-heptanol + NAD+
-
 Pyrococcus horikoshii NBRC 100139 heptanal + NADH + H+
-
 r
1-heptanol + NAD+
-
 Pyrococcus horikoshii JCM 9974 heptanal + NADH + H+
-
 r
1-heptanol + NAD+
-
 Pyrococcus horikoshii ATCC 700860 heptanal + NADH + H+
-
 r
1-heptanol + NAD+
-
 Pyrococcus horikoshii OT-3 heptanal + NADH + H+
-
 r
1-hexanol + NAD+
-
 Pyrococcus horikoshii hexanal + NADH + H+
-
 r
1-hexanol + NAD+
-
 Pyrococcus horikoshii DSM 12428 hexanal + NADH + H+
-
 r
1-hexanol + NAD+
-
 Pyrococcus horikoshii NBRC 100139 hexanal + NADH + H+
-
 r
1-hexanol + NAD+
-
 Pyrococcus horikoshii JCM 9974 hexanal + NADH + H+
-
 r
1-hexanol + NAD+
-
 Pyrococcus horikoshii ATCC 700860 hexanal + NADH + H+
-
 r
1-hexanol + NAD+
-
 Pyrococcus horikoshii OT-3 hexanal + NADH + H+
-
 r
1-octanol + NAD+
-
 Pyrococcus horikoshii octanal + NADH + H+
-
 r
1-pentanol + NAD+
-
 Pyrococcus horikoshii pentanal + NADH + H+
-
 r
1-propanol + NAD+
-
 Pyrococcus horikoshii propanal + NADH + H+
-
 r
benzylalcohol + NAD+
-
 Pyrococcus horikoshii benzaldehyde + NADH + H+
-
 r
cyclohexanol + NAD+
-
 Pyrococcus horikoshii cyclohexanone + NADH + H+
-
 r
ethanol + NAD+
-
 Pyrococcus horikoshii acetaldehyde + NADH + H+
-
 r
methanol + NAD+
-
 Pyrococcus horikoshii formaldehyde + NADH + H+
-
 r
methanol + NAD+
-
 Pyrococcus horikoshii DSM 12428 formaldehyde + NADH + H+
-
 r
methanol + NAD+
-
 Pyrococcus horikoshii NBRC 100139 formaldehyde + NADH + H+
-
 r
methanol + NAD+
-
 Pyrococcus horikoshii JCM 9974 formaldehyde + NADH + H+
-
 r
methanol + NAD+
-
 Pyrococcus horikoshii ATCC 700860 formaldehyde + NADH + H+
-
 r
methanol + NAD+
-
 Pyrococcus horikoshii OT-3 formaldehyde + NADH + H+
-
 r
additional information substrate specificity of Ni-PhADH for alcohol oxidation reactions and aldehyde reduction reactions, overview. No activity with 2-butanol, tert-butanol, and 2,3-butanediol Pyrococcus horikoshii ?
-
-
additional information substrate specificity of Ni-PhADH for alcohol oxidation reactions and aldehyde reduction reactions, overview. No activity with 2-butanol, tert-butanol, and 2,3-butanediol Pyrococcus horikoshii DSM 12428 ?
-
-
additional information substrate specificity of Ni-PhADH for alcohol oxidation reactions and aldehyde reduction reactions, overview. No activity with 2-butanol, tert-butanol, and 2,3-butanediol Pyrococcus horikoshii NBRC 100139 ?
-
-
additional information substrate specificity of Ni-PhADH for alcohol oxidation reactions and aldehyde reduction reactions, overview. No activity with 2-butanol, tert-butanol, and 2,3-butanediol Pyrococcus horikoshii JCM 9974 ?
-
-
additional information substrate specificity of Ni-PhADH for alcohol oxidation reactions and aldehyde reduction reactions, overview. No activity with 2-butanol, tert-butanol, and 2,3-butanediol Pyrococcus horikoshii ATCC 700860 ?
-
-
additional information substrate specificity of Ni-PhADH for alcohol oxidation reactions and aldehyde reduction reactions, overview. No activity with 2-butanol, tert-butanol, and 2,3-butanediol Pyrococcus horikoshii OT-3 ?
-
-

Synonyms

Synonyms Comment Organism
PH0743
-
 Pyrococcus horikoshii
PhADH
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Pyrococcus horikoshii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70 95 the enzyme activity is slightly decreased by 1 h incubation at 70°C (2.6%), 80°C (4.7%), 90°C (7.9%), and 95°C (18.8%), 50% loss of activity after approximately 6 h at 95°C Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.48
-
 1-butanol substrates NAD+ and 1-butanol, pH 9.0, 30°C Pyrococcus horikoshii
0.5
-
 NAD+ substrates NAD+ and 1-butanol, pH 9.0, 30°C Pyrococcus horikoshii
0.82
-
 Butanal substrates NADH and butanal, pH 5.5, 30°C Pyrococcus horikoshii
6.66
-
 propanal substrates NADH and propanal, pH 5.5, 30°C Pyrococcus horikoshii
6.96
-
 pentanal substrates NADH and pentanal, pH 5.5, 30°C Pyrococcus horikoshii
7.4
-
 NADH substrates NADH and butanal, pH 5.5, 30°C Pyrococcus horikoshii
7.87
-
 NADPH substrates NADPH and butanal, pH 5.5, 30°C Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 aldehyde reduction assay at Pyrococcus horikoshii
9
-
 alcohol oxidation assay at Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Pyrococcus horikoshii
NADH
-
 Pyrococcus horikoshii

General Information

General Information Comment Organism
evolution NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes Pyrococcus horikoshii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.92
-
 1-butanol substrates NAD+ and 1-butanol, pH 9.0, 30°C Pyrococcus horikoshii
2.4
-
 propanal substrates NADH and propanal, pH 5.5, 30°C Pyrococcus horikoshii
3.82
-
 Butanal substrates NADH and butanal, pH 5.5, 30°C Pyrococcus horikoshii
15.14
-
 NADPH substrates NADPH and butanal, pH 5.5, 30°C Pyrococcus horikoshii
16.67
-
 NAD+ substrates NAD+ and 1-butanol, pH 9.0, 30°C Pyrococcus horikoshii
77.33
-
 pentanal substrates NADH and pentanal, pH 5.5, 30°C Pyrococcus horikoshii
672.7
-
 NADH substrates NADH and butanal, pH 5.5, 30°C Pyrococcus horikoshii