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Literature summary for 1.6.3.1 extracted from

  • Wu, X.; Kobori, H.; Orita, I.; Zhang, C.; Imanaka, T.; Xing, X.H.; Fukui, T.
    Application of a novel thermostable NAD(P)H oxidase from hyperthermophilic archaeon for the regeneration of both NAD+ and NADP+ (2012), Biotechnol. Bioeng., 109, 53-62.
    View publication on PubMed
Search for more literature for 1.6.3.1

Application

Application Comment Organism
synthesis usage of the enzyme for regeneration of both NADP+ and NAD+ in alcohol dehydrogenase-catalyzed enantioselective oxidation of racemic 1-phenylethanol. NADP+ regeneration at 30°C by TkNOX coupled with (R)-specific ADH from Lactobacillus kefir results in successful acquisition of optically pure (S)-1-phenylethanol, or at 45-60°C with moderately thermostable (S)-specific ADH from Rhodococcus erythropolis in optically pure (R)-1-phenylethanol, giving the possibility to operate the enantioselective bioconversion accompanying NAD+ regeneration at high temperatures, advantage of the combination of thermostable enzymes Thermococcus kodakarensis

Cloned(Commentary)

Cloned (Comment) Organism
gene tk0304, functional expression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermococcus kodakarensis KOD1 (TkNOX) catalyzes oxidation of NADH and NADPH with oxygen from atmospheric air as an electron acceptor ?
-
 ?
NADH + H+ + O2 Thermococcus kodakarensis
-
 NAD+ + H2O2
-
 ?
NADPH + H+ + O2 Thermococcus kodakarensis
-
 NADP+ + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JFZ8 gene tk0304
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RIL partially by heat treatment at 65°C for 15 min Thermococcus kodakarensis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.16
-
 purified recombinant enzyme, with NADPH in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, pH 7.0, 30°C Thermococcus kodakarensis
0.38
-
 purified recombinant enzyme, with NADH in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, pH 7.0, 30°C Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information KOD1 (TkNOX) catalyzes oxidation of NADH and NADPH with oxygen from atmospheric air as an electron acceptor Thermococcus kodakarensis ?
-
 ?
NADH + H+ + O2
-
 Thermococcus kodakarensis NAD+ + H2O2
-
 ?
NADPH + H+ + O2
-
 Thermococcus kodakarensis NADP+ + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
KOD1
-
 Thermococcus kodakarensis
NOX
-
 Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
 above Thermococcus kodakarensis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 90 and above, activity range, profile overview Thermococcus kodakarensis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 the enzyme shows a 25% loss of activity after incubation at 65°C for 1 h Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Thermococcus kodakarensis

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 the partially purified ReADH shows a preference for an alkaline pH range for the oxidation of (RS)-1-phenylethanol in a coupled reaction with (S)-specific ADH from Rhodococcus erythropolis, the highest activity occurs at pH 12.0 Thermococcus kodakarensis

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Thermococcus kodakarensis
NADH
-
 Thermococcus kodakarensis
NADPH
-
 Thermococcus kodakarensis