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Literature summary extracted from

  • Savage, H.; Montoya, G.; Svensson, C.; Schwenn, J.D.; Sinning, I.
    Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases (1997), Structure, 5, 895-906.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.8.4.8 crystal structure at 2.0 A. The enzyme shows striking similarity to the structure of the ATP pyrophosphatase domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold 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 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin Escherichia coli essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth ?
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 ?

Organism

EC Number Organism UniProt Comment Textmining
1.8.4.8 Escherichia coli
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.4.8 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin
-
 Escherichia coli adenosine-3',5'-bisphosphate + oxidized thioredoxin + sulfite
-
 ?
1.8.4.8 5-Phosphoadenosine 3-phosphosulfate + reduced thioredoxin essential step in the biosynthesis of Cys in E. coli. Blocking of the enzyme inhibits cell growth Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.4.8 dimer homodimer, each monomer consisting of a six-stranded beta-sheet surrounded by alpha-helices, crystallographic date Escherichia coli