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Literature summary for 5.4.99.5 extracted from

  • Görisch, H.; Lingens, F.
    Chorismate mutase from Streptomyces aureofaciens: a heat-stable enzyme (1973), J. Bacteriol., 114, 645-651.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.53
-
chorismate
-
Kitasatospora aureofaciens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
sucrose density gradient centrifugation Kitasatospora aureofaciens

Organism

Organism UniProt Comment Textmining
Kitasatospora aureofaciens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Kitasatospora aureofaciens

Renatured (Commentary)

Renatured (Comment) Organism
renaturation of heat-denatured enzyme Kitasatospora aureofaciens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
Kitasatospora aureofaciens Prephenate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
reversible heat inactivation above Kitasatospora aureofaciens
100
-
15 min, activity can be restored Kitasatospora aureofaciens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8
-
Kitasatospora aureofaciens