Literature summary 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.

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.4.99.1	Clostridium cochlearium	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
5.4.99.1	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	a

Substrates and Products (Substrate)

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

Synonyms

EC Number	Synonyms	Comment	Organism
5.4.99.1	Glutamate mutase	-	Clostridium cochlearium

Cofactor

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

General Information

EC Number	General Information	Comment	Organism
5.4.99.1	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

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Release 2023.1 (January 2023)