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Literature summary extracted from

  • Zhang, Y.; Zhang, H.; Zheng, Q.
    How chorismatases regulate distinct reaction channels in a single conserved active pocket mechanistic analysis with QM/MM (ONIOM) investigations (2019), Chemistry, 25, 1326-1336 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.3.2.13 A244G site-directed mutagenesis Streptomyces hygroscopicus
3.3.2.13 V209Q site-directed mutagenesis Streptomyces hygroscopicus
4.1.3.45 G240A site-directed mutagenesis Streptomyces hygroscopicus
4.1.3.45 Q201V site-directed mutagenesis Streptomyces hygroscopicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.3.2.13 chorismate + H2O Streptomyces hygroscopicus
-
 (4R,5R)-4,5-dihydroxycyclohexa-1(6),2-diene-1-carboxylate + pyruvate
-
 ?
4.1.3.45 chorismate Streptomyces hygroscopicus
-
 3-hydroxybenzoate + pyruvate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.13 Streptomyces hygroscopicus Q9KID9
-
-
4.1.3.45 Streptomyces hygroscopicus O30478
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.3.2.13 chorismate + H2O = (4R,5R)-4,5-dihydroxycyclohexa-1(6),2-diene-1-carboxylate + pyruvate reaction steps are: 1. the protonation of the methylene group of chorismate, 2. nucleophilic attack by activated water at the C2' carbocation, and 3. the elimination of pyruvate Streptomyces hygroscopicus
a
4.1.3.45 chorismate = 3-hydroxybenzoate + pyruvate intramolecular mechanism catalyzed by enzyme Hyg5, overview. Reaction steps are: 1. the protonation of the methylene group of CHO, 2. nucleophilic attack of the activated 4-hydroxyl group, and 3. rearrangement of the arene oxide Streptomyces hygroscopicus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.13 chorismate + H2O
-
 Streptomyces hygroscopicus (4R,5R)-4,5-dihydroxycyclohexa-1(6),2-diene-1-carboxylate + pyruvate
-
 ?
3.3.2.13 chorismate + H2O substrate binding structure analysis Streptomyces hygroscopicus (4R,5R)-4,5-dihydroxycyclohexa-1(6),2-diene-1-carboxylate + pyruvate
-
 ?
4.1.3.45 chorismate
-
 Streptomyces hygroscopicus 3-hydroxybenzoate + pyruvate
-
 ?
4.1.3.45 chorismate substrate binding structure analysis Streptomyces hygroscopicus 3-hydroxybenzoate + pyruvate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.3.2.13 CH-fkbo
-
 Streptomyces hygroscopicus
3.3.2.13 fkbO
-
 Streptomyces hygroscopicus
4.1.3.45 CH-Hyg5
-
 Streptomyces hygroscopicus
4.1.3.45 chorismatase/3-hydroxybenzoate synthase
-
 Streptomyces hygroscopicus
4.1.3.45 hyg5
-
 Streptomyces hygroscopicus

General Information

EC Number General Information Comment Organism
3.3.2.13 additional information analysis of catalytic mechanisms of chorismatases EC 3.3.2.13 and EC 4.1.3.45 by molecular dynamics simulations and hybrid quantum mechanical/molecular mechanical (QM/MM) calculations of the Michaelis complexes of two wild-type models (FkbO and Hyg5) and four mutant models with chorismate as substrate, comparison of the catalytic mechanisms between FkbO and Hyg5, overview. The A/G residue group (A244FkbO/G240Hyg5) causes changes in the binding states of the substrate and the orientation of the catalytic glutamate, but only these changes affect the product selectivity in chorismatases limitedly. The distal V/Q residue group, which determines the internal water self-regulating ability at the active site, has significant impact on the selectivity of the catalytic mechanisms. The V/Q residue group is suggested to be an important factor to control the catalytic activities in chorismatases Streptomyces hygroscopicus
4.1.3.45 additional information analysis of catalytic mechanisms of chorismatases EC 3.3.2.13 and EC 4.1.3.45 by molecular dynamics simulations and hybrid quantum mechanical/molecular mechanical (QM/MM) calculations of the Michaelis complexes of two wild-type models (FkbO and Hyg5) and four mutants models with chorismate as substrate, comparison of the catalytic mechanisms between FkbO and Hyg5, overview. The A/G residue group (A244FkbO/G240Hyg5) causes changes in the binding states of the substrate and the orientation of the catalytic glutamate, but only these changes affect the product selectivity in chorismatases limitedly. The distal V/Q residue group, which determines the internal water self-regulating ability at the active site, has significant impact on the selectivity of the catalytic mechanisms. The V/Q residue group is suggested to be an important factor to control the catalytic activities in chorismatases Streptomyces hygroscopicus