the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
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
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
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)
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
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)
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
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
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