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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.320 expression in BL21 DE3 cells Caenorhabditis elegans
2.1.1.321 expression in BL21 DE3 cells Caenorhabditis elegans

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.320 2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine Caenorhabditis elegans
-
 2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.320 Caenorhabditis elegans O02325
-
-
2.1.1.321 Caenorhabditis elegans Q9XW42
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.320
-
 Caenorhabditis elegans
2.1.1.321
-
 Caenorhabditis elegans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.320 2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
-
 Caenorhabditis elegans 2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
-
 ?
2.1.1.320 2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine the enzyme methylates the R508 residue Caenorhabditis elegans 2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
-
 ?
2.1.1.320 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine the enzyme methylates the R508 residue Caenorhabditis elegans S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega-methyl-L-arginine
-
 ?
2.1.1.320 S-adenosyl-L-methionine + [splicing factor SF3B2]-Nomega-L-arginine the enzyme methylates the R508 residue Caenorhabditis elegans S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
-
 ?
2.1.1.321 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
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.320 PRMT-9
-
 Caenorhabditis elegans
2.1.1.321 PRMT-7
-
 Caenorhabditis elegans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.321 15
-
-
 Caenorhabditis elegans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.1.321 25 30 the enzyme is much more active at 25°C than at 30°C Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
2.1.1.320 physiological function the enzyme (PRMT-9) may play a regulatory role in nematode alternative RNA splicing Caenorhabditis elegans