Information on EC 2.1.1.320 - type II protein arginine methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.320
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RECOMMENDED NAME
GeneOntology No.
type II protein arginine methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
overall reaction
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-
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S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
show the reaction diagram
(1a)
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-
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S-adenosyl-L-methionine + [protein]-Nomega-methyl-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
(1b)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega,Nomega'-dimethyl-L-arginine-forming)
The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform PRMT5
UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + [D2 dopamine receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [D2 dopamine receptor]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
recombinant fragment of the third intracellular loop of D2, corresponding to amino acid residues 211 to 241 fused to glutathione S-transferase. Residues Arg217 and Arg219 are key methylation sites within this region
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-
?
2 S-adenosyl-L-methionine + [DOP-3 receptor]-L-arginine
2 S-adenosyl-L-homocysteine + [DOP-3 receptor]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
recombinant fragment of the third intracellular loop of Caenorhabditis elegans DOP-3, amino acid residues 202 to 232 fused to GST. Residues Arg208 and Arg210 are key methylation sites within this region
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-
?
2 S-adenosyl-L-methionine + [golgin GM130]-L-arginine
2 S-adenosyl-L-homocysteine + [golgin GM130]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
-
overall reaction
-
?
2 S-adenosyl-L-methionine + [histone H3]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H3]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
isoform PRMT5 bound to nuclear protein COPR5 methylates histone histone H3 at residue R8. Methylation of histone H4 is preferred over histone H3
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?
2 S-adenosyl-L-methionine + [histone H4 peptide]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4 peptide]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
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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
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?
2 S-adenosyl-L-methionine + [histone H4]-L-arginine
2 S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
2 S-adenosyl-L-methionine + [SmD3 protein]-L-arginine
2 S-adenosyl-L-homocysteine + [SmD3 protein]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
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-
PRMT5 alone methylates both histone H4 and SmD3 proteins while PRMT5 complexed with p44 and pICln methylates SmD3 but not histone H4
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?
2 S-adenosyl-L-methionine + [splicing factor SF3B2]-L-arginine
2 S-adenosyl-L-homocysteine + [splicing factor SF3B2]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
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overall reaction, isoform PRMT9 symmetrically dimethylates arginine residues on splicing factor SF3B2. A peptide containing the methylatable Arg508 of SF3B2 is not recognized by PRMT9 in vitro. Amino acid substitutions of residues surrounding Arg508 have no great effect on PRMT9 recognition of SF3B2, but moving the arginine residue within this sequence abolishes methylation
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?
S-adenosyl-L-methionine + [GST-fibrillarin]-L-arginine
S-adenosyl-L-homocysteine + [GST-fibrillarin]-Nomega-methyl-L-arginine
show the reaction diagram
substrate is amino terminus of fibrillarin fused to glutathione S-transferase
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-
?
S-adenosyl-L-methionine + [GST-fibrillarin]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-fibrillarin]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega-methyl-L-arginine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + [GST-GAR]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
show the reaction diagram
histone H2A from calf thymus
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-
?
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [histone H2A]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [protein]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
symmetric dimethylation is only observed when enzyme and the methyl-accepting substrate are incubated for extended times
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?
S-adenosyl-L-methionine + [histone H4]-L-arginine
S-adenosyl-L-homocysteine + [histone H4]-Nomega-methyl-L-arginine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [histone H4]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone H4]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [histone]-L-arginine
S-adenosyl-L-homocysteine + [histone]-Nomega-methyl-L-arginine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [histone]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [histone]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [myelin basic protein]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
S-adenosyl-L-methionine + [nucleoplasmin]-L-arginine
S-adenosyl-L-homocysteine + [nucleoplasmin]-Nomega-methyl-L-arginine
show the reaction diagram
-
nucleoplasmin is a potent substrate and is monomethylated and symmetrically dimethylated at Arg187
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?
S-adenosyl-L-methionine + [nucleoplasmin]-Nomega-methyl-L-arginine
S-adenosyl-L-homocysteine + [nucleoplasmin]-Nomega,Nomega'-dimethyl-L-arginine
show the reaction diagram
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nucleoplasmin is a potent substrate and is monomethylated and symmetrically dimethylated at Arg187
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?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000022 - 0.001
S-adenosyl-L-methionine
0.0042 - 0.0102
[histone H4 peptide]-L-arginine
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PRMT5 expression gradually increases throughout postnatal brain development, coinciding with the period of active myelination
Manually annotated by BRENDA team
histone H2A and nucleoplasmin methylation appears late in oogenesis and is most abundant in the laid egg
Manually annotated by BRENDA team
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isoform PRMT5 is abundantly expressed in the germ cells of both male and female gonads
Manually annotated by BRENDA team
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lung carcinoma
Manually annotated by BRENDA team
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skeletal muscle stem cell
Manually annotated by BRENDA team
additional information
Prmt7 transcripts and protein are maternally deposited and ubiquitously expressed through gastrulation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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coexpression of candidate tumor suppressor gene RASSF1A and PRMT5 leads to a redistribution of PRMT5 from the cytosol to stabilized microtubules
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
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sedimentation analysis
158000
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sedimentation analysis
240000
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sedimentation analysis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 72000, SDS-PAGE
monomer
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1 * 72000, SDS-PAGE
tetramer
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4 * 72000, SDS-PAGE
additional information
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PRMT5 forms distinct homooligomeric complexes, including a dimer and tetramer. The PRMT5 homo-oligomers are dissociated into a monomer in the presence of a reducing agent, whereas a monomer, dimer, and multimer are detected in the absence or at low concentrations of a reducing agent
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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in a structural model, the carboxylate group of the position 4 Asp258 points away from the substrate arginine, possibly to coordinate the binding of one or both of the two lysine residues adjacent to the methylated arginine in the FKRKY sequence of substrate SF3B2
complex of isoform PRMT5, methylosome protein MEP50 and S-adenosylhomocysteine. PRMT5-MEP50 forms an unusual tetramer of heterodimers with substantial surface negative charge. MEP50 is required for PRMT5-catalyzed histone H2A and H4 methyltransferase activity and binds substrates independently. MEP50 binds to the substrate distal of the target arginine and orients the unstructured substrate tail towards the catalytic site of the PRMT5 molecule that is not directly coupled to the substrate-bound MEP50
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform PRMT5 expression is regulated by the circadian clock and responds to both light and temperature cues
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D258G
mutation mimics type I enzymes, complete loss of activity
DELTA365-369
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deletion of the sequence GAGRG, residues 365-369 in the -adenosyl-L-methionine-binding motif I, leads to dramatic reduction in catalytic activity
G260E
mutation mimics isoform PRMT7, complete loss of activity
additional information
construction of deletion mutant, in which the TPR motif or the N terminus is missing, and two C-terminal mutants. No activity is observed with any of the mutants
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine