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Literature summary extracted from

  • Harnvoravongchai, P.; Kobori, H.; Orita, I.; Nakamura, S.; Imanaka, T.; Fukui, T.
    Characterization and gene deletion analysis of four homologues of group 3 pyridine nucleotide disulfide oxidoreductases from Thermococcus kodakarensis (2014), Extremophiles, 18, 603-616.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.1.18 CoA activities in the presence of NADPH or NADH are completely lost in the absence of CoA–SH, demonstrating strict CoA-dependency of the enzyme for sulfur reduction. Km: 0.26 mM Thermococcus kodakarensis
1.8.1.18 CoA strict CoA-dependency Thermococcus kodakarensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.3.1 expression in Escherichia coli Thermococcus kodakarensis
1.8.1.18 expression in Escherichia coli Thermococcus kodakarensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.6.3.1 CoA NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not; NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not; NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not; NADH-dependent oxidase activities is strongly inhibited by addition of free CoA, whereas NADPH dependent activity is not Thermococcus kodakarensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.3.1 40000
-
 2 * 40000, SDS-PAGE Thermococcus kodakarensis
1.6.3.1 49000
-
 2 * 49000, SDS-PAGE Thermococcus kodakarensis
1.6.3.1 49000
-
 4 * 49000, SDS-PAGE Thermococcus kodakarensis
1.6.3.1 50000
-
 6 * 50000, SDS-PAGE Thermococcus kodakarensis
1.6.3.1 100000
-
-
 Thermococcus kodakarensis
1.6.3.1 330000
-
 gel filtration Thermococcus kodakarensis
1.8.1.18 50000
-
 6 * 50000, SDS-PAGE Thermococcus kodakarensis
1.8.1.18 100000
-
-
 Thermococcus kodakarensis
1.8.1.18 330000
-
 gel filtration Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.18 sulfur + NAD(P)H + H+ Thermococcus kodakarensis a catalytic cycle of TK1299 is proposed suggesting that CoA-SH acts to solubilize S(0) by forming CoA persulfides, followed by reduction of an enzyme-S-S-CoA intermediate produced after both enzymatic and non-enzymatic evolution of H2S from the CoA persulfide, with NADPH as an electron donor hydrogen sulfide + NAD(P)+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.6.3.1 Thermococcus kodakarensis Q5JFZ8
-
-
1.6.3.1 Thermococcus kodakarensis Q5JGF8
-
-
1.6.3.1 Thermococcus kodakarensis Q5JGP4
-
-
1.6.3.1 Thermococcus kodakarensis Q5JHY2
-
-
1.6.3.1 Thermococcus kodakarensis Q5JJB9
-
-
1.8.1.18 Thermococcus kodakarensis Q5JGF8
-
-
1.8.1.18 Thermococcus kodakarensis Q5JGP4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.3.1
-
 Thermococcus kodakarensis
1.8.1.18
-
 Thermococcus kodakarensis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.1.18 4.78
-
 pH 8.0, 70°C Thermococcus kodakarensis
1.8.1.18 14
-
 pH 8.0, 70°C Thermococcus kodakarensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.3.1 NADH + H+ + O2
-
 Thermococcus kodakarensis NAD+ + H2O2
-
 ?
1.6.3.1 NADH + H+ + O2 activity with NADPH is much lower than with NADH Thermococcus kodakarensis NAD+ + H2O2
-
 ?
1.6.3.1 NADPH + H+ + O2
-
 Thermococcus kodakarensis NADP+ + H2O2
-
 ?
1.6.3.1 NADPH + H+ + O2 activity with NADPH is much lower than with NADH Thermococcus kodakarensis NADP+ + H2O2
-
 ?
1.8.1.18 sulfur + NAD(P)H + H+
-
 Thermococcus kodakarensis hydrogen sulfide + NAD(P)+
-
 ?
1.8.1.18 sulfur + NAD(P)H + H+ a catalytic cycle of TK1299 is proposed suggesting that CoA-SH acts to solubilize S(0) by forming CoA persulfides, followed by reduction of an enzyme-S-S-CoA intermediate produced after both enzymatic and non-enzymatic evolution of H2S from the CoA persulfide, with NADPH as an electron donor Thermococcus kodakarensis hydrogen sulfide + NAD(P)+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.6.3.1 ? 2 * 40000, SDS-PAGE Thermococcus kodakarensis
1.6.3.1 homodimer
-
 Thermococcus kodakarensis
1.6.3.1 homodimer 2 * 49000, SDS-PAGE Thermococcus kodakarensis
1.6.3.1 homohexamer 6 * 50000, SDS-PAGE Thermococcus kodakarensis
1.6.3.1 homotetramer 4 * 49000, SDS-PAGE Thermococcus kodakarensis
1.8.1.18 homodimer
-
 Thermococcus kodakarensis
1.8.1.18 homohexamer 6 * 50000, SDS-PAGE Thermococcus kodakarensis

Synonyms

EC Number Synonyms Comment Organism
1.6.3.1 NAD(P)H oxidase
-
 Thermococcus kodakarensis
1.6.3.1 NOX
-
 Thermococcus kodakarensis
1.6.3.1 TK0304 locus name Thermococcus kodakarensis
1.6.3.1 TK0828 locus name Thermococcus kodakarensis
1.6.3.1 TK1186 locus name Thermococcus kodakarensis
1.6.3.1 TK1299 locus name Thermococcus kodakarensis
1.6.3.1 TK1481 locus name Thermococcus kodakarensis
1.8.1.18 CoA-dependent NAD(P)H: elemental sulfur (S0) oxidoreductase
-
 Thermococcus kodakarensis
1.8.1.18 NAD(P)H: S0 oxidoreductase
-
 Thermococcus kodakarensis
1.8.1.18 NSR
-
 Thermococcus kodakarensis
1.8.1.18 TK1186 locus name Thermococcus kodakarensis
1.8.1.18 TK1299 locus name Thermococcus kodakarensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.6.3.1 70
-
 assay at Thermococcus kodakarensis
1.8.1.18 70
-
 assay at Thermococcus kodakarensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.3.1 8
-
 assay at Thermococcus kodakarensis
1.8.1.18 8
-
 assay at Thermococcus kodakarensis

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.3.1 NADH
-
 Thermococcus kodakarensis
1.6.3.1 NADH preference to NADPH versus NADH as an electron donor during oxygen reduction Thermococcus kodakarensis
1.6.3.1 NADPH
-
 Thermococcus kodakarensis
1.6.3.1 NADPH preference to NADPH versus NADH as an electron donor during oxygen reduction Thermococcus kodakarensis
1.8.1.18 CoA activities in the presence of NADPH or NADH are completely lost in the absence of CoA–SH, demonstrating strict CoA-dependency of the enzyme for sulfur reduction. KM: 0.26 mM Thermococcus kodakarensis
1.8.1.18 CoA strict CoA-dependency Thermococcus kodakarensis
1.8.1.18 FAD addition of FAD increases the activity, potentially reflecting the promoted formation of the active holoenzyme Thermococcus kodakarensis
1.8.1.18 NADPH preference for NADPH as an electron donor Thermococcus kodakarensis
1.8.1.18 NADPH the enzyme exhibits activity with preference to NADPH as an electron donor, as indicated by higher specific activity with NADPH (14.0 U/mg) than with NADH (0.75 U/mg) NADH Thermococcus kodakarensis