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Literature summary for 1.8.4.8 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
Search for more literature for 1.8.4.8

Activating Compound

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

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3'-phosphoadenylyl-sulfate + glutaredoxin Escherichia coli
-
 adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
 ?
3'-phosphoadenylyl-sulfate + thioredoxin Escherichia coli
-
 adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
 ?
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Reaction

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phosphoadenylyl-sulfate + glutaredoxin
-
 Escherichia coli adenosine 3',5'-bisphosphate + glutaredoxin disulfide + sulfite
-
 ?
3'-phosphoadenylyl-sulfate + thioredoxin
-
 Escherichia coli adenosine 3',5'-bisphosphate + thioredoxin disulfide + sulfite
-
 ?
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

Synonyms Comment Organism
3'-Phosphoadenylylsulfate reductase
-
 Escherichia coli
PAPS reductase
-
 Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
glutaredoxin
-
 Escherichia coli
thioredoxin
-
 Escherichia coli