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Literature summary for 5.4.3.9 extracted from

  • Chen, D.; Tanem, J.; Frey, P.A.
    Basis for the equilibrium constant in the interconversion of L-lysine and L-beta-lysine by lysine 2,3-aminomutase (2007), Biochim. Biophys. Acta, 1774, 297-302.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.4.3.9

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
beta-glutamate Clostridium subterminale
-
 3-aminopentanedioate
-
 ?
beta-glutamate Clostridium subterminale SB4
-
 3-aminopentanedioate
-
 ?
L-glutamate Clostridium subterminale
-
 3-aminopentanedioate
-
 ?
L-glutamate Clostridium subterminale SB4
-
 3-aminopentanedioate
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridium subterminale
-
-
-
Clostridium subterminale SB4
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-glutamate
-
 Clostridium subterminale 3-aminopentanedioate
-
 ?
beta-glutamate
-
 Clostridium subterminale SB4 3-aminopentanedioate
-
 ?
L-glutamate
-
 Clostridium subterminale 3-aminopentanedioate
-
 ?
L-glutamate
-
 Clostridium subterminale SB4 3-aminopentanedioate
-
 ?
additional information equilibrium constants for reaction of glutamate 2,3-aminomutase favor the beta-isomer, structural aspects of enantioselectivity, overview. Greater enthalpic stability of beta-glutamate relative to L-glutamate Clostridium subterminale ?
-
 ?
additional information equilibrium constants for reaction of glutamate 2,3-aminomutase favor the beta-isomer, structural aspects of enantioselectivity, overview. Greater enthalpic stability of beta-glutamate relative to L-glutamate Clostridium subterminale SB4 ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Clostridium subterminale