Information on EC 2.1.1.321 - type III protein arginine methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.321
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RECOMMENDED NAME
GeneOntology No.
type III protein arginine methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-Nomega-methyl-L-arginine
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega-methyl-L-arginine-forming)
Type III protein arginine methyltransferases catalyse the single methylation of one of the terminal nitrogen atoms of the guanidino group in an L-arginine residue within a protein. Unlike type I and type II protein arginine methyltransferases, which also catalyse this reaction, type III enzymes do not methylate the substrate any further. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, and EC 2.1.1.322, type IV protein arginine methyltransferase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
S-adenosyl-L-methionine + acetyl-GGRGG-NH2
S-adenosyl-L-homocysteine + acetyl-GG-(Nomega-methyl-)RGG-NH2
show the reaction diagram
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substrate is a synthetic peptide
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-
?
S-adenosyl-L-methionine + GGFGGRGGFG-NH2
S-adenosyl-L-homocysteine + GGFGG-(Nomega-methyl-)RGGFG-NH2
show the reaction diagram
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substrate is a synthetic peptide
product is monomethylated at residue R6
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?
S-adenosyl-L-methionine + GGPGGRGGPGG-NH2
S-adenosyl-L-homocysteine + GGPGG-Nomega-methyl-RGGPGG
show the reaction diagram
substrate is a synthetic peptide
enzyme catalyzes monomethylation of Arg-residues
-
?
S-adenosyl-L-methionine + [AGRGRGKAAILKAQVAARGRGRGMGRGN-NH2]-L-arginine
S-adenosyl-L-homocysteine + [AGRGRGKAAILKAQVAARGRGRGMGRGN-NH2]Nomega-methyl-L-arginine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [GST-GAR]-L-arginine
S-adenosyl-L-homocysteine + [GST-GAR]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [histone H2A]-L-arginine
S-adenosyl-L-homocysteine + [histone H2A]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [histone H2B peptide 23-37]-L-arginine
S-adenosyl-L-homocysteine + [histone H2B peptide 23-37]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [histone H2B]-L-arginine
S-adenosyl-L-homocysteine + [histone H2B]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [histone H3]-L-arginine
S-adenosyl-L-homocysteine + [histone H3]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [histone H4 peptide 1-20]-L-arginine
S-adenosyl-L-homocysteine + [histone H4 peptide 1-20]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [histone H4 peptide 14-22]-L-arginine
S-adenosyl-L-homocysteine + [histone H4 peptide 14-22]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + [myelin basic protein]-L-arginine
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [SG-(Nomega-methyl-)RGKGGKGLGKGGAKRHRK-NH2]-L-arginine
S-adenosyl-L-homocysteine + [SG-(Nomega-methyl-)RGKGGKGLGKGGAKRHRK-NH2]Nomega-methyl-L-arginine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [SGRGKGGKGLGKGGAKRHRK-NH2]-L-arginine
S-adenosyl-L-homocysteine + [SGRGKGGKGLGKGGAKRHRK-NH2]Nomega-methyl-L-arginine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [Smb protein]-L-arginine
S-adenosyl-L-homocysteine + [Smb protein]-Nomega-methyl-L-arginine
show the reaction diagram
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-
-
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?
additional information
?
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069
[histone H2B peptide 23-37]-L-arginine
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pH 7.5, 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
[histone H2B peptide 23-37]-L-arginine
Mus musculus
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pH 7.5, 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5
[histone H2B peptide 23-37]-L-arginine
Mus musculus
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pH 7.5, 22°C
206854
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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isoform PRMT7 is expressed during embryonic testis development and interacts with imprinting control region-binding protein CTCFL/BORIS
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78000
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x * 78000, calculated
80000
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x * 80000, SDS-PAGE, x * 81200, calculated
81200
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x * 80000, SDS-PAGE, x * 81200, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of full-length PRMT7 at 1.7 A resolution. The PRMT7 structure is composed of two catalytic modules in tandem forming a pseudo-dimer and contains only one AdoHcy molecule bound to the N-terminal module. The second active site is frozen in an inactive state by a conserved zinc finger located at the junction between the two PRMT modules and by the collapse of two degenerated AdoMet-binding loops
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in insect cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform PRMT7 expression is significantly upregulated in both primary breast tumour tissues and in breast cancer lymph node metastases
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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isoform PRMT7 expression is significantly upregulated in both primary breast tumour tissues and in breast cancer lymph node metastases. Reducing PRMT7 levels in invasive breast cancer cells using RNA interference significantly decreases cell invasion in vitro and metastasis in vivo. Overexpression of PRMT7 in non-aggressive MCF-7 cells enhances their invasiveness. PRMT7 induces the expression of matrix metalloproteinase MMP9. Invasion of aggressive breast cancer cells depleted of PRMT7 may be rescued by the exogenous expression of MMP9