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Literature summary for 5.4.99.1 extracted from

  • Rommel, J.B.; Liu, Y.; Werner, H.J.; Kaestner, J.
    Role of tunneling in the enzyme glutamate mutase (2012), J. Phys. Chem. B, 116, 13682-13689.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2S,3S)-3-methylaspartate Clostridium cochlearium
-
L-glutamate
-
r

Organism

Organism UniProt Comment Textmining
Clostridium cochlearium
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-threo-3-methylaspartate = L-glutamate conversion of glutamate to methylaspartate catalyzed by glutamate mutase is investigated by quantum mechanical/molecular mechanical simulations based on coupled cluster and density functional calculations, overview. Binding of the Glu substrate induces a homolytic cleavage of the cobalt-carbon bond of the cofactor, which yields a 5'-deoxyadenosyl radical and cob(II)alamin, atom tunneling mechanism Clostridium cochlearium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2S,3S)-3-methylaspartate
-
Clostridium cochlearium L-glutamate
-
r

Synonyms

Synonyms Comment Organism
Glutamate mutase
-
Clostridium cochlearium

Cofactor

Cofactor Comment Organism Structure
5'-deoxyadenosylcobalamin dependent on Clostridium cochlearium