Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.8.1.18 extracted from

  • Toth, A.; Takacs, M.; Groma, G.; Rakhely, G.; Kovacs, K.L.
    A novel NADPH-dependent oxidoreductase with a unique domain structure in the hyperthermophilic Archaeon, Thermococcus litoralis (2008), FEMS Microbiol. Lett., 282, 8-14.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Thermococcus litoralis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.087
-
NADPH pH 8.9, 65°C Thermococcus litoralis
0.54
-
polysulfide(n) pH 8.9, 65°C Thermococcus litoralis

Organism

Organism UniProt Comment Textmining
Thermococcus litoralis B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0 B2BSJ7: alpha subunit, B2BSJ6: beta subunit, B2BSJ5: gamma subunit, B2BSK0: delta subunit
-
Thermococcus litoralis DSM 5473 B2BSJ7 and B2BSJ6 and B2BSJ5 and B2BSK0 B2BSJ7: alpha subunit, B2BSJ6: beta subunit, B2BSJ5: gamma subunit, B2BSK0: delta subunit
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermococcus litoralis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.35
-
pH 8.9, 65°C, purified recombinant subunit NsoC, oxidation of NADPH in the presence of polysulfide Thermococcus litoralis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
polysulfide(n) + NADPH + H+ NADH can not replace NADPH, the purified recombinant enzyme catalyzes the reduction of polysulfide with NADPH as an electron donor and it also reduces oxygen Thermococcus litoralis hydrogen sulfide + polysulfide(n-1) + NADP+
-
?
polysulfide(n) + NADPH + H+ NADH can not replace NADPH, the purified recombinant enzyme catalyzes the reduction of polysulfide with NADPH as an electron donor and it also reduces oxygen Thermococcus litoralis DSM 5473 hydrogen sulfide + polysulfide(n-1) + NADP+
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
assay at, the temperature optimum of the enzyme can not be determined due to the significant thermolability of NADPH above 80°C Thermococcus litoralis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.9
-
assay at Thermococcus litoralis

Cofactor

Cofactor Comment Organism Structure
FAD the purified recombinant NsoC contains one FAD cofactor per protein molecule Thermococcus litoralis
NADPH NADH can not replace NADPH Thermococcus litoralis