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Literature summary for 5.1.1.3 extracted from

  • Puig, E.; Garcia-Viloca, M.; Gonzalez-Lafont, A.; Lluch, J.M.
    On the ionization state of the substrate in the active site of glutamate racemase. A QM/MM study about the importance of being zwitterionic (2006), J. Phys. Chem. A, 110, 717-725.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Aquifex pyrophilus
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-
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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 computer simulations on a QM/MM (quantum mechanics/molecular mechanics) potential energy surface are carried out to gain insights into the catalytic mechanism of glutamate racemase (MurI). Results suggest at least two possible roles for MurI as a catalyst: (1) to activate the bound substrate by donating a proton to its carboxylate main chain in a step prior to the racemization process and (2) to optimize the differential stabilization of the intermediate relative to the reactant via an intermolecular effect that comes, partly, from a desolvation effect on the reactant in going from water to the enzyme environment and, partly, from a stabilization effect on the intermediate by the enzymatic residues. Thus, the catalytic effect of glutamate racemase is achieved without resorting to covalent bond formation between the enzyme or cofactor and the transition state. Aquifex pyrophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
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 Aquifex pyrophilus D-glutamate
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 ?

Synonyms

Synonyms Comment Organism
glutamate racemase
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 Aquifex pyrophilus
MurI
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 Aquifex pyrophilus