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Literature summary extracted from

  • Hu, P.; Wang, S.; Zhang, Y.
    How do SET-domain protein lysine methyltransferases achieve the methylation state specificity? Revisited by ab initio QM/MM molecular dynamics simulations (2008), J. Am. Chem. Soc., 130, 3806-3813.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.1.127 enzyme in complex with S-adenosyl-L-methionine, crystal structure analysis Pisum sativum

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.127 Y305F the SET7/9 Y305F mutant not only has a high efficiency for mono-methylation but also becomes a dimethylase. The Y305F mutation leads to a less tight active site Pisum sativum

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.127 Pisum sativum
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.127 additional information LSMT has both mono-and di-methylation activities. Determination of free energy reaction profiles and transition state geometries using the crystal structure and on-the-fly ab initio QM/MM MD simulations in two simulation systems: LSMTAdoMet-Lys and LSMT-AdoMet-MeLys, which are enzyme-substrate complexes for mono- and di-methylation reactions in LSMT, method, overview. Methylation state specificity, overview Pisum sativum ?
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Synonyms

EC Number Synonyms Comment Organism
2.1.1.127 LSMT
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 Pisum sativum
2.1.1.127 PKMT
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 Pisum sativum
2.1.1.127 protein lysine methyltransferase
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 Pisum sativum
2.1.1.127 Rubisco large subunit methyltransferase
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 Pisum sativum
2.1.1.127 SET-domain protein lysine methyltransferase
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 Pisum sativum