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Literature summary extracted from

  • Luka, Z.; Pakhomova, S.; Loukachevitch, L.; Newcomer, M.; Wagner, C.
    Differences in folate-protein interactions result in differing inhibition of native rat liver and recombinant glycine N-methyltransferase by 5-methyltetrahydrofolate (2012), Biochim. Biophys. Acta, 1824, 286-291.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.20 expression in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.20 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 Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.20 folate the native rat liver GNMT contains an acetylated N-terminal valine and is inhibited much more efficiently compared to the recombinant protein Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.20 Rattus norvegicus P13255
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.20 liver
-
 Rattus norvegicus
-

Synonyms

EC Number Synonyms Comment Organism
2.1.1.20 GNMT
-
 Rattus norvegicus