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Literature summary for 4.2.1.113 extracted from

  • Sanchez-Tarin, M.; Swiderek, K.; Roca, M.; Tunon, I.
    Enzyme promiscuity in enolase superfamily. Theoretical study of o-succinylbenzoate synthase using QM/MM methods (2015), J. Phys. Chem. B, 119, 1899-1911 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate Amycolatopsis sp.
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2-succinylbenzoate + H2O
-
?

Organism

Organism UniProt Comment Textmining
Amycolatopsis sp. Q44244
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate
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Amycolatopsis sp. 2-succinylbenzoate + H2O
-
?
additional information the enzyme catalyzes not only the dehydration of (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate but also catalyzes racemization of different acylamino acids, with N-succinyl-R-phenylglycine being the best substrate, molecular mechanisms for both reactions exploring the potential energy surface, and molecular dynamics simulations to obtain the free energy profiles and the averaged interaction energies of enzymatic residues with the reacting system, overview Amycolatopsis sp. ?
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?

Synonyms

Synonyms Comment Organism
menC
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Amycolatopsis sp.
OSBS
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Amycolatopsis sp.

General Information

General Information Comment Organism
additional information enzyme promiscuity in enolase superfamily is analyzed by using quantum mechanics/molecular mechanics (QM/MM) methods, using both density functional theory and semiempirical Hamiltonians. Presence of flexible loops in the active site and the selection of structural modifications in the substrate seem to be key elements to promote the promiscuity of this enzyme, role played by the different residues in each of the two possible reactions, overview Amycolatopsis sp.