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Literature summary for 5.4.99.1 extracted from

  • Rommel, J.B.; Kaestner, J.
    The fragmentation-recombination mechanism of the enzyme glutamate mutase studied by QM/MM simulations (2011), J. Am. Chem. Soc., 133, 10195-10203.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium
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-
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Reaction

Reaction Comment Organism Reaction ID
L-threo-3-methylaspartate = L-glutamate radical mechanism of the conversion of glutamate to methylaspartate catalyzed by glutamate mutase by quantum mechanical/molecular mechanical simulations based on density functional theory, crystal structure analysis Clostridium cochlearium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-threo-3-methylaspartate
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Clostridium cochlearium L-glutamate
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?

Synonyms

Synonyms Comment Organism
Glutamate mutase
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Clostridium cochlearium

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin dependent on, binding structure, modeling, overview Clostridium cochlearium

General Information

General Information Comment Organism
additional information residue Glu117 and the arginine claw have a strong influence, and also residues Glu 214, Lys 322, Gln 147, Glu 330, Lys 326, and Met 294 play a catalytic role. The arginine claw keeps the intermediates in place and is probably responsible for the enantioselectivity. Glu 171 temporarily accepts a proton from the glutamyl radical intermediate and donates it back at the end of the reaction Clostridium cochlearium