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Literature summary for 5.4.99.5 extracted from

  • Zhang, S.; Pohnert, G.; Kongsaeree, P.; Wilson, D.B.; Clardy, J.; Ganem, B.
    Chorismate mutase-prephenate dehydratase from Escherichia coli. Study of catalytic and regulatory domains using genetically engineered proteins (1998), J. Biol. Chem., 273, 6248-6253.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
additional information proteins containing residues 1-285 and residues 1-300 retain full chorismate mutase activity and prephenate dehydratase activity, but exhibit no feedback inhibition. Proteins containing residues 101-386 and residues 101-300 retain full prephenate dehydratase activity, but lack mutase activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 bifunctional enzyme chorismate mutase/prephenate dehydratase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Chorismate
-
 Escherichia coli Prephenate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
54
-
 1 h, 50% loss of activity, wild-type enzyme Escherichia coli
58
-
 1 h, 50% inactivation, genetically engineered enzyme with amino acid residues 1-285 Escherichia coli
62
-
 1 h, 50% inactivation, genetically engineered enzyme with amino acid residues 1-300 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
39
-
 chorismate wild-type enzyme Escherichia coli
40.7
-
 chorismate genetically engineered enzyme containg the amino acid residues 1-300 Escherichia coli
44.3
-
 chorismate genetically engineered enzyme containg the amino acid residues 1-285 Escherichia coli