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

BRENDA support

Literature summary for 1.8.1.B4 extracted from

  • Pedone, E.; Limauro, D.; D'Alterio, R.; Rossi, M.; Bartolucci, S.
    Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus (2006), FEBS J., 273, 5407-5420.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharolobus solfataricus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0003
-
[protein disulfide oxidoreductase]-disulfide pH 7.0, 60°C Saccharolobus solfataricus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[protein disulfide oxidoreductase]-disulfide + NADPH + H+ Saccharolobus solfataricus the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus [protein disulfide oxidoreductase]-dithiol + NADP+
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+ Saccharolobus solfataricus P2 the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus [protein disulfide oxidoreductase]-dithiol + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97W27
-
-
Saccharolobus solfataricus P2 Q97W27
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[protein disulfide oxidoreductase]-disulfide + NADPH + H+ the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus Saccharolobus solfataricus [protein disulfide oxidoreductase]-dithiol + NADP+
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+ the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors. The enzyme is not active with the putative thioredoxins TRxA1 (SSO0368) and TRxA2 (SSO2232) Saccharolobus solfataricus [protein disulfide oxidoreductase]-dithiol + NADP+
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+ the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus Saccharolobus solfataricus P2 [protein disulfide oxidoreductase]-dithiol + NADP+
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+ the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors. The enzyme is not active with the putative thioredoxins TRxA1 (SSO0368) and TRxA2 (SSO2232) Saccharolobus solfataricus P2 [protein disulfide oxidoreductase]-dithiol + NADP+
-
?

Synonyms

Synonyms Comment Organism
SSO2416 locus name Saccharolobus solfataricus
SsTR
-
Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
assay at Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Saccharolobus solfataricus

Cofactor

Cofactor Comment Organism Structure
FAD the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors Saccharolobus solfataricus