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Literature summary for 3.3.2.13 extracted from

  • Dong, L.; Liu, Y.
    Comparative studies of the catalytic mechanisms of two chorismatases CH-fkbo and CH-Hyg5 (2017), Proteins, 85, 1146-1158 .
    View publication on PubMed
Search for more literature for 3.3.2.13

Inhibitors

Inhibitors Comment Organism Structure
3-(2-carboxyethyl)benzoate
-
 Streptomyces hygroscopicus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Streptomyces hygroscopicus Q9KID9
-
-

Reaction

Reaction Comment Organism Reaction ID
chorismate + H2O = (4R,5R)-4,5-dihydroxycyclohexa-1(6),2-diene-1-carboxylate + pyruvate catalytic mechanism, the two carboxyl groups of chorismate form a H-bond network with residues R228, Y215, Y155, and R162. These H-bonds are maintained during the whole catalytic process, which may play a role in stabilizing the negative charged substrate. The protonated E338 builds a strong H-bond with the 4-OH of chorismate. The distance between HA of E338 and C3' of chorismate is 4.00 A. Two water molecules enter the reactive center, which may function as mediators in the catalytic reaction. The reaction steps are protonation of methylene group, followed by nucleophilic attack of carbocation by (activated) water molecule W1, and cleavage of C2'-O8 bond Streptomyces hygroscopicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chorismate + H2O
-
 Streptomyces hygroscopicus (4R,5R)-4,5-dihydroxycyclohexa-1(6),2-diene-1-carboxylate + pyruvate
-
 ?

Synonyms

Synonyms Comment Organism
CH-fkbo
-
 Streptomyces hygroscopicus
fkbO
-
 Streptomyces hygroscopicus

General Information

General Information Comment Organism
additional information structure of Fkbo-substrate complex, the solvated model of CH-Fkbo is optimized to calculate the catalytic mechanism. In the reactant structure, the substrate chorismate takes the similar binding model as inhibitor 3-(2-carboxyethyl)benzoate in crystal structure and adopts a trans-pseudodiaxial conformation. The structure of Streptomyces hygroscopicus chorismatase CH-Hyg5 is very similar to that of Streptomyces hygroscopicus chorismatase CH-Fkbo, all amino acid residues in the active site are the same except residues G240Hyg5 (A244Fkb8) and C327Hyg5 (A331Fkb8) are the same. The optimized active site structure of Hyg5 complex is superpositioned with that of Fkbo, overview. Two nonconserved active site residues are responsible for the different reaction mechanism of CH-Fkbo and CH-Hyg5. In CH-Hyg5, the lack of methyl in G240Hyg5 leads to the different conformation of the side chain of E334 (or E338) in Hyg5 and Fkbo. This small change eventually decreases the ESP charge of C3 atom of the substrate, which facilitates the cleavage of C3-O8 bond in Hyg5. Furthermore, C327Hyg5 is involved in the selective product formation in Hyg5 enzyme Streptomyces hygroscopicus