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2.1.1.20: glycine N-methyltransferase

This is an abbreviated version!
For detailed information about glycine N-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.20

Reaction

S-adenosyl-L-methionine
+
glycine
=
S-adenosyl-L-homocysteine
 +
sarcosine

Synonyms

4S polycyclic aromatic hydrocarbon binding protein, glycine methyltransferase, glycine N-methyltransferase, glycine-N methyltransferase, GNMT, Gnmt gene product, methyltransferase, glycine, S-adenosyl-L-methionine:glycine methyltransferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.20 glycine N-methyltransferase

Crystallization

Crystallization on EC 2.1.1.20 - glycine N-methyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown at 4°C by hanging drop vapor diffusion method
-
wild type and H176N mutant enzyme as cocrystals with a citrate molecule bound in the active site
crystals are grown at 22°C by hanging drop vapor diffusion method, crystallized in two crystal forms, a monoclinic form and a tetragonal form, P2(1) and P4(1)2(1)2
-
crystallized by the sitting drop method in complex with (6S)-5-methyltetrahydrofolat monoglutamate
GNMT complexed with 5-methyltetrahydrofolate, by the sitting drop method at room temperature, two folate binding sites in the intersubunit areas of the tetramer, each folate binding site is formed primarily by two 1-7 N-terminal regions of one pair of subunits and two 205-218 regions of the other pair of subunits. Both the pteridine and p-aminobenzoyl rings are located in the hydrophobic cavities formed by Tyr5, Leu207, and Met215 residues of all subunits
hanging drop method of vapor diffusion, crystal structure of the enzyme complexed with S-adenosyl-L-methionine and acetate (a potent competitive inhibitor of Gly) and the R175K mutated enzyme complexed with S-adenosyl-L-methionine are determined at 2.8 A and 3.0 A resolution, respectively
including R175K mutant
native and recombinant protein, to 2.55 A resolution. The native rat liver GNMT contains an acetylated N-terminal valine and is inhibited much more efficiently compared to the recombinant protein. In the folate-GNMT complexes with the native enzyme, two folate molecules establish three and four hydrogen bonds with the protein. In the folate-recombinant GNMT complex only one hydrogen bond is established. This difference results in more effective inhibition by folate of the native liver GNMT activity compared to the recombinant enzyme
sitting-drop vapor diffusion method in complex with 5-methyltetrahydrofolate pentaglutamate, two molecules of inhibitor bound to a tetramer