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Literature summary for 2.1.1.20 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)

Cloned (Comment) Organism
expression in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
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

Organism UniProt Comment Textmining
Rattus norvegicus P13255
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
GNMT
-
Rattus norvegicus