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Literature summary extracted from

  • Kuznetsov, N.A.; Faleev, N.G.; Kuznetsova, A.A.; Morozova, E.A.; Revtovich, S.V.; Anufrieva, N.V.; Nikulin, A.D.; Fedorova, O.S.; Demidkina, T.V.
    Pre-steady-state kinetic and structural analysis of interaction of methionine gamma-lyase from Citrobacter freundii with inhibitors (2015), J. Biol. Chem., 290, 671-681 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.4.1.11 in complex with cycloserine Citrobacter freundii

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.4.1.11 L-Cycloserine inactivation by L-cycloserine is completely reversed by dialysis against potassium phosphate buffer (pH 8.0), containing 0.5 mM PLP and 5 mM dithiothreitol Citrobacter freundii

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.11 Citrobacter freundii Q84AR1
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.11 L-alanine
-
 Citrobacter freundii ?
-
 ?
4.4.1.11 L-norvaline
-
 Citrobacter freundii ?
-
 ?
4.4.1.11 additional information enzyme catalyzes the exchange of both Calpha-protons of glycine with high stereospecificity for pro-R-proton. The reaction mechanism includes ketimine intermediate formation Citrobacter freundii ?
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
4.4.1.11 pyridoxal 5'-phosphate
-
 Citrobacter freundii