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Literature summary for 2.1.1.2 extracted from

  • Komoto, J.; Takata, Y.; Yamada, T.; Konishi, K.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
    Monoclinic guanidinoacetate methyltransferase and gadolinium ion-binding characteristics (2003), Acta Crystallogr. Sect. D, 59, 1589-1596.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant enzyme truncated at amino acid 37 from N-terminus Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with S-adenosyl-L-methionine in monoclinic and tetragonal modification Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
Y136F retains considerable activity, structural changes compared to wild-type Rattus norvegicus
Y136V loss of activity, structural changes compared to wild-type Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
recombinant enzyme truncated at amino acid 37 from N-terminus
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Subunits

Subunits Comment Organism
dimer crystallization data Rattus norvegicus