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Literature summary extracted from

  • Lillig, C.H.; Potamitou, A.; Schwenn, J.D.; Vlamis-Gardikas, A.; Holmgren, A.
    Redox regulation of 3'-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins (2003), J. Biol. Chem., 278, 22325-22330.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.8.4.8 glutaredoxin required, reverses enzyme inhibition by oxidized glutathione, glutathione together with glutaredoxin exhibits regulatory function in vivo Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.4.8 overexpression in strain BL21(DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.8.4.8 additional information a mutant lacking glutathione reductase and glutaredoxins does barely grow on sulfate, strains containing a mutant C9S/C12S glutaredoxin grow poorly Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.8.4.8 oxidized glutathione reversible inhibition, forms mixed disulfides with the enzymes active site residue Cys239, inactivation kinetics, inhibition is reversible by glutaredoxin, not by DTT, glutaredoxin together with glutathione exhibits regulatory function in vivo Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.4.8 3'-phosphoadenylyl-sulfate + glutaredoxin Escherichia coli
-
adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
?
1.8.4.8 3'-phosphoadenylyl-sulfate + thioredoxin Escherichia coli
-
adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
?
1.8.4.8 additional information Escherichia coli enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.8 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.4.8 recombinant enzyme from strain BL21(DE3) Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.8.4.8 adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin ping pong type reaction mechanism, Cys239 is the active site residue Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.8 3'-phosphoadenylyl-sulfate + glutaredoxin
-
Escherichia coli adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
?
1.8.4.8 3'-phosphoadenylyl-sulfate + thioredoxin
-
Escherichia coli adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
?
1.8.4.8 additional information enzyme is involved in sulfate assimilation requiring reduced glutathione and glutaredoxins, redox regulation of the enzyme by glutathione and glutaredoxins, overview Escherichia coli ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.8.4.8 3'-Phosphoadenylylsulfate reductase
-
Escherichia coli
1.8.4.8 PAPS reductase
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.8.4.8 30
-
assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.8.4.8 8
-
assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.4.8 glutaredoxin
-
Escherichia coli
1.8.4.8 thioredoxin
-
Escherichia coli