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Literature summary extracted from

  • Tars, K.; Olin, B.; Mannervik, B.
    Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases (2010), J. Mol. Biol., 397, 332-340.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.3.1
-
Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.3.1 GST A3-3 in complex with DELTA5-androstene-3,17-dione, using 100 mM Tris-HCl pH 7.8, 18% (v/v) PEG 4000, and 2 mM dithiothreitol Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
5.3.3.1 Homo sapiens Q16772
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.3.1 glutathione-Sepharose column chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.3.1 5-Androstene-3,17-dione
-
Homo sapiens 4-Androstene-3,17-dione
-
?
5.3.3.1 additional information human GST A3-3 does not stabilize a dienolate by an oxyanion hole in the active site Homo sapiens ?
-
?

Synonyms

EC Number Synonyms Comment Organism
5.3.3.1 3-Oxosteroid DELTA5-DELTA4-isomerase
-
Homo sapiens
5.3.3.1 3beta-HSD
-
Homo sapiens
5.3.3.1 DELTA5-3-ketosteroid isomerase
-
Homo sapiens
5.3.3.1 glutathione transferase A3-3
-
Homo sapiens
5.3.3.1 GST A3-3
-
Homo sapiens