Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.320 extracted from

  • Antonysamy, S.; Bonday, Z.; Campbell, R.M.; Doyle, B.; Druzina, Z.; Gheyi, T.; Han, B.; Jungheim, L.N.; Qian, Y.; Rauch, C.; Russell, M.; Sauder, J.M.; Wasserman, S.R.; Weichert, K.; Willard, F.S.; Zhang, A.; Emtage, S.
    Crystal structure of the human PRMT5:MEP50 complex (2012), Proc. Natl. Acad. Sci. USA, 109, 17960-17965.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.320

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of isoform PRMT5 in complex with methylosome protein MEP50, bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.000022
-
 S-adenosyl-L-methionine isoform PRMT5, presence of 0.001 mM histone H4 peptide, 22°C, pH not specified in the publication Homo sapiens
0.001
-
 S-adenosyl-L-methionine isoform PRMT5 in complex with MEP50, presence of 0.001 mM histone H4 peptide, 22°C, pH not specified in the publication Homo sapiens
0.0042
-
 [histone H4 peptide]-L-arginine isoform PRMT5, presence of 0.01 mM S-adenosyl-L-methionine, 22°C, pH not specified in the publication Homo sapiens
0.0102
-
 [histone H4 peptide]-L-arginine isoform PRMT5 in complex with MEP50,presence of 0.01 mM S-adenosyl-L-methionine, 22°C, pH not specified in the publication Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O14744 isoform PRMT5
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + [histone H4 peptide]-L-arginine
-
 Homo sapiens 2 S-adenosyl-L-homocysteine + [histone H4 peptide]-Nomega,Nomega'-dimethyl-L-arginine both PRMT5 alone and PRMT5 in complex with MEP50 are able to generate di-methylated H4 peptide product. The PRMT5:MEP50 complex consistently has a higher level of methyltransferase activity compared with PRMT5 ?
additional information PRMT5 has a nonprocessive enzymatic mechanism for peptide substrates Homo sapiens ?
-
 ?

General Information

General Information Comment Organism
physiological function both PRMT5 alone and PRMT5 in complex with MEP50 are able to generate di-methylated H4 peptide product. The PRMT5:MEP50 complex consistently has a higher level of methyltransferase activity compared with PRMT5 Homo sapiens