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Literature summary for 1.8.4.8 extracted from

  • Berndt, C.; Schwenn, J.; Lillig, C.
    The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity (2015), Chem. Sci., 6, 7049-7058 .
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0137
-
thioredoxin Trx1 pH 8.0, temperature not specified in the publication Escherichia coli
0.0149
-
glutaredoxin Grx1 pH 8.0, temperature not specified in the publication Escherichia coli
0.0178
-
thioredoxin TrxH3 pH 8.0, temperature not specified in the publication Escherichia coli
0.0261
-
thioredoxin TrxH4 pH 8.0, temperature not specified in the publication Escherichia coli
0.0342
-
thioredoxin Trx2 pH 8.0, temperature not specified in the publication Escherichia coli
0.0431
-
thioredoxin TrxH2 pH 8.0, temperature not specified in the publication Escherichia coli
0.059
-
thioredoxin TrxH1 pH 8.0, temperature not specified in the publication Escherichia coli
0.0637
-
glutaredoxin Grx pH 8.0, temperature not specified in the publication Escherichia coli
0.0681
-
thioredoxin hTrx1 pH 8.0, temperature not specified in the publication Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phosphoadenylyl sulfate + glutaredoxin Grx poplar glutaredoxin, 33% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + glutaredoxin Grx disulfide
-
?
3'-phosphoadenylyl sulfate + glutaredoxin Grx1 Escherichia coli glutaredoxin, 70% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + glutaredoxin Grx1 disulfide
-
?
3'-phosphoadenylyl sulfate + thioredoxin hTrx1 human thioredoxin, 59% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin hTrx1 disulfide
-
?
3'-phosphoadenylyl sulfate + thioredoxin Trx1 Escherichia coli thioredoxin Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin Trx1 disulfide
-
?
3'-phosphoadenylyl sulfate + thioredoxin Trx2 Escherichia coli thioredoxin, 38% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin Trx2 disulfide
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH1 Arabidopsis thaliana thioredoxin, 18% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH1 disulfide
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH2 Arabidopsis thaliana thioredoxin, 23% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH2 disulfide
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH3 Arabidopsis thaliana thioredoxin, 154% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH3 disulfide
-
?
3'-phosphoadenylyl sulfate + thioredoxin TrxH4 Arabidopsis thaliana thioredoxin, 45% of the activity with thioredoxin Trx1 Escherichia coli adenosine 3',5'-bisphosphate + sulfite + thioredoxin TrxH4 disulfide
-
?
additional information the redox potential does not determine specificity nor efficiency of the redoxins as reductant. The efficiency of PAPS reductase with various redoxins correlates strongly to the extent of a negative electric field of the redoxins reaching into the solvent outside the active site, and electrostatic and geometric complementary contact surfaces Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
PAPS reductase
-
Escherichia coli