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Literature summary extracted from

  • Huang, Y.; Komoto, J.; Konishi, K.; Takata, Y.; Ogawa, H.; Gomi, T.; Fujioka, M.; Takusagawa, F.
    Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: Crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes (2000), J. Mol. Biol., 298, 149-162.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.20 including R175K mutant Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.20 R175K crystal structure: N-terminal domains of subunits have moved out of the active sites of adjacent subunits Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.20 Rattus norvegicus P13255
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Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.20 S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine mechanism Rattus norvegicus