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Literature summary for 5.3.3.1 extracted from

  • Yun, Y.S.; Lee, T.H.; Nam, G.H.; Jang, D.S.; Shin, S.; Oh, B.H.; Choi, K.Y.
    Origin of the different pH activity profile in two homologous ketosteroid isomerases (2003), J. Biol. Chem., 278, 28229-28236.
    View publication on PubMed
Search for more literature for 5.3.3.1

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals of mutant enzyme F116W are grown by hanging-drop method Comamonas testosteroni

Protein Variants

Protein Variants Comment Organism
F116W the turnover-number for 5-androstene-3,17-dione is lowered 4.42fold, the KM-value is 3.1fold lower than the Km-value of the wild-type enzyme Comamonas testosteroni

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0486
-
 5-androstene-3,17-dione 25°C, pH 7.0, mutant enzyme F116W Comamonas testosteroni
0.1528
-
 5-androstene-3,17-dione 25°C, pH 7.0, wild-type enzyme Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni P00947
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5(10)-estrene-3,17-dione nonsticky substrate Comamonas testosteroni estr-4-en-3,17-dione
-
 ?
5-Androstene-3,17-dione
-
 Comamonas testosteroni 4-Androstene-3,17-dione
-
 ?

Synonyms

Synonyms Comment Organism
TI-WT
-
 Comamonas testosteroni

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7155
-
 5-androstene-3,17-dione 25°C, pH 7.0, mutant enzyme F116W Comamonas testosteroni
7160
-
 5-androstene-3,17-dione 25°C, pH 7.0, mutant enzyme F116W Comamonas testosteroni
31680
-
 5-androstene-3,17-dione 25°C, pH 7.0, wild-type enzyme Comamonas testosteroni
31700
-
 5-androstene-3,17-dione 25°C, pH 7.0, wild-type enzyme Comamonas testosteroni