Reaction intermediate structure of Entamoeba histolytica methionine gamma-lyase 1 containing Michaelis complex and methionine imine-pyridoxamine-5'-phosphate

(2E)-2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)imino]-4-(methylsulfanyl)butanoic acid

(2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid

Crystal structure of Entamoeba histolytica methionine gamma-lyase 1

1.8M (NH4)2SO4, 0.1M cacodylate buffer, 0.1M Li3(C3H5O(COO)3), 0.1mM pyridozxal 5'-phosphate, pH 6.6, vapor diffusion, sitting drop, temperature 277K

The same protein complexed with substrate

1. ACCORDING TO AUTHOR, THE SUBSTITUTION OF LEU TO SER AT A308, B808, C1308, D1808 ARE ALLELIC VARIATION. 2. SINCE THE GENE HAD INTERNAL METHIONINE AND UPSTREAM OF THIS MET IS SIMILAR TO SHINE-DALGARNO SEQUENCE, SEVERAL NUCLEOTIDES WERE REPLACED NOT TO CHANGE THE AMINO ACID RESIDUES, BUT AVOID RIBOSOME BINDING IN E. COLI EXPRESSION SYSTEM.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

gamma-lyase, L-methionine, entamoeba histolytica, lyase