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Literature summary for 2.1.1.321 extracted from

  • Hadjikyriacou, A.; Clarke, S.G.
    Caenorhabditis elegans PRMT-7 and PRMT-9 are evolutionarily conserved protein arginine methyltransferases with distinct substrate specificities (2017), Biochemistry, 56, 2612-2626 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in BL21 DE3 cells Caenorhabditis elegans

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc ion is present in a zinc finger motif Caenorhabditis elegans

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans Q9XW42
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Caenorhabditis elegans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + [human histone H2B peptide]-L-arginine Caenorhabditis elegans PRMT-7 is able to methylate synthetic human histone H2B peptides containing residues 23-37. The C. elegans enzyme recognizes the human peptide better than the Caenorhabditis elegans peptide. The histone H2B R29K peptide reduces methylation counts to a level about 40%, of that of the wild type peptide sequence. The R31K and R33K mutant peptides further decrease the activity to about 10% and 22% respectively, signifying the importance of arginine residues in a sequential R-X-R motif Caenorhabditis elegans S-adenosyl-L-homocysteine + [human histone H2B peptide]-Nomega-methyl-L-arginine
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 ?

Synonyms

Synonyms Comment Organism
PRMT-7
-
 Caenorhabditis elegans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
15
-
-
 Caenorhabditis elegans

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 30 the enzyme is much more active at 25°C than at 30°C Caenorhabditis elegans