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Literature summary for 5.4.99.5 extracted from

  • Lassila, J.K.; Keeffe, J.R.; Kast, P.; Mayo, S.L.
    Exhaustive mutagenesis of six secondary active-site residues in Escherichia coli chorismate mutase shows the importance of hydrophobic side chains and a helix N-capping position for stability and catalysis (2007), Biochemistry, 46, 6883-6891.
    View publication on PubMed

Application

Application Comment Organism
analysis As an intramolecular reaction that appears to be catalyzed without intermediate steps, covalent catalysis, or modification of the reaction pathway, the chorismate-prephenate rearrangement has become an important model system for theoretical approaches to the study of enzyme catalysis Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information EcCM active-site residues (Leu7, Ala32, Val35, Asp48, Ile81, Val85) that mutated in our previous computational design experiment. Each of the 114 variants tested for complementation of the chorismate mutase deficiency of the auxotrophic Escherichia coli KA12/pKIMP-UAUC system. 34% of all single mutants are scored as biological active Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information The Km of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Chorismate Escherichia coli
-
Prephenate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9J8
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
chorismate mutase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
The melting point of the active complementations (changes in position 7, 32, 35, 48, 81 and 85) is shown Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information The kcat of the active complementations (position 7, 32, 35, 48, 81 and 85) is shown Escherichia coli