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Literature summary for 2.1.1.127 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)

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

Protein Variants

Protein Variants Comment Organism
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

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

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