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Literature summary for 1.8.1.18 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
Search for more literature for 1.8.1.18

Activating Compound

Activating Compound Comment Organism Structure
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
CoA strict CoA-dependency Thermococcus kodakarensis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 6 * 50000, SDS-PAGE Thermococcus kodakarensis
100000
-
-
 Thermococcus kodakarensis
330000
-
 gel filtration Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JGF8
-
-
Thermococcus kodakarensis Q5JGP4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermococcus kodakarensis

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sulfur + NAD(P)H + H+
-
 Thermococcus kodakarensis hydrogen sulfide + NAD(P)+
-
 ?
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

Subunits Comment Organism
homodimer
-
 Thermococcus kodakarensis
homohexamer 6 * 50000, SDS-PAGE Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
CoA-dependent NAD(P)H: elemental sulfur (S0) oxidoreductase
-
 Thermococcus kodakarensis
NAD(P)H: S0 oxidoreductase
-
 Thermococcus kodakarensis
NSR
-
 Thermococcus kodakarensis
TK1186 locus name Thermococcus kodakarensis
TK1299 locus name Thermococcus kodakarensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
70
-
 assay at Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Thermococcus kodakarensis

Cofactor

Cofactor Comment Organism Structure
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
CoA strict CoA-dependency Thermococcus kodakarensis
FAD addition of FAD increases the activity, potentially reflecting the promoted formation of the active holoenzyme Thermococcus kodakarensis
NADPH preference for NADPH as an electron donor Thermococcus kodakarensis
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