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Information on EC 2.1.1.127 - [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
for references in articles please use BRENDA:EC2.1.1.127
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.127 [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
IUBMB Comments
The enzyme catalyses three successive methylations of Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39). Only the three methylated form is observed . The enzyme from pea (Pisum sativum) also three-methylates a specific lysine in the chloroplastic isoforms of fructose-bisphosphate aldolase (EC 4.1.2.13) .
The enzyme appears in viruses and cellular organisms
- 2.1.1.127
- histone
- methyltransferases
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pkmts
- adomet
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monomethylation
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non-histone
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adohcy
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tri-methylation
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lysine-14
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trithorax
-
suv39h2
Reaction Schemes
show3
+
=
3
+
3
+
=
3
+
Synonyms
protein lysine methyltransferase, rubisco lsmt, rubisco large subunit methyltransferase, rbcmt, protein-lysine methyltransferase, rubisco ls methyltransferase, rubisco large-subunit dimethyltransferase, rlsmt, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LSMT
Methyltransferase, ribulose diphosphate carboxylase large subunit(lysine)
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rbcMT
Ribulose 1,5-bisphosphate carboxylase/oxygenase large subunit Nepsilon-methyltransferase
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Ribulose bisphosphate carboxylase large subunit methyltransferase
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Ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit epsilonN-methyltransferase
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Ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase
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Rubisco large subunit epsilonN-methyltransferase
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Rubisco LSMT
Rubisco methyltransferase
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[Ribulose-bisphosphate-carboxylase]-lysine N-methyltransferase
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additional information
rbcMT
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Rubisco LSMT
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additional information
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Rubisco LSMT is a SET domain protein methyltransferase
additional information
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Rubisco LSMT is a SET domain protein methyltransferase
additional information
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Rubisco LSMT is a SET domain protein methyltransferase
additional information
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Rubisco LSMT is a SET domain protein methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine
S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine
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3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine
catalytic reaction mechanism and specificity, molecular dynamics and hybrid quantum mechanics/molecular mechanics, overview
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3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6,N6,N6-trimethyl-L-lysine
substrate binding, leucine-rich motifscontribute to the contact surface with Rubisco, overview
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S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
catalytic mechanism
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S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
substrate and inhibitor binding site
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S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
amino acid sequence comparison
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S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
enzyme is encoded on genes containing the SET-domain sequence, substrate specificity is connected to SET sequence
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S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
SET structure
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S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[3-phospho-D-glycerate-carboxy-lyase (dimerizing)]-lysine N6-methyltransferase
The enzyme catalyses three successive methylations of Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39). Only the three methylated form is observed [3]. The enzyme from pea (Pisum sativum) also three-methylates a specific lysine in the chloroplastic isoforms of fructose-bisphosphate aldolase (EC 4.1.2.13) [5].
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CAS REGISTRY NUMBER
COMMENTARY
139171-98-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3 S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase]-L-lysine
3 S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
Substrates: reaction of EC 2.1.1.259
Products: -
Products: -
?
3 S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6,N6,N6-trimethyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
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Substrates: -
Products: -
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?
S-adenosyl-L-methionine + L-Lys
S-adenosyl-L-homocysteine + methyl-L-Lys
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + methyl-L-Lys
S-adenosyl-L-homocysteine + dimethyl-L-Lys + trimethyl-L-Lys
Substrates: about 2fold higher activity than with Lys
Products: -
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S-adenosyl-L-methionine + ribulose-1,5-bisphosphate carboxylase
?
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Substrates: ribulose-1,5-bisphosphate carboxylase from Spinacia sp.
Products: -
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?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [fructose-1,6-bisphosphate aldolase]-lysine
S-adenosyl-L-homocysteine + [fructose-1,6-bisphosphate aldolase]-N6-methyl-L-lysine
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-lysine
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
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Substrates: methylation is required for gamma-tocopherol methyltransferase activity
Products: -
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S-adenosyl-L-methionine + [large subunit of Rubisco]-L-lysine
S-adenosyl-L-homocysteine + [large subunit of Rubisco]-N6-methyl-L-lysine
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Substrates: methylation occurs at Lys-394
Products: -
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S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
?
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Substrates: the enzyme catalyzes the posttranslational methylation of the epsilon-amino group of Lys-14 in the large subunit of Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: Rubisco LSMT utilizes a processive reaction mechanism to catalyse exclusively trimethylation of Lys14 without disassociation from Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: methylation of lysine 14 of the large subunit
Products: -
Products: -
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S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: Rubisco LSMT utilizes a processive reaction mechanism to catalyse exclusively trimethylation of Lys14 without disassociation from Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: methylation of lysine 14 of the large subunit
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: LSMT transfers one or two methyl groups to a single lysine
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: LSMT transfers two methyl groups to a single lysine
Products: -
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?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: Rubisco LSMT utilizes a processive reaction mechanism to catalyse exclusively trimethylation of Lys14 without disassociation from Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: methylation of lysine 14 of the large subunit
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: Rubisco from spinach or tobacco leaves. LSMT transfers one or two methyl groups to a single lysine
Products: -
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?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: Rubisco LSMT utilizes a processive reaction mechanism to catalyse exclusively trimethylation of Lys14 without disassociation from Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: methylation of lysine 14 of the large subunit
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
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Substrates: the enzyme does not distinguish between the enzyme form activated by Mg2+ and CO2 and the unactivated enzyme form
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
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Substrates: inactive on ribulose-bisphosphate-carboxylases that contain trimethyllysyl residues at position 14 in the large subunit
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S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
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Substrates: catalyzes methylation of the epsilon-amino group of Lys-14 in the large subunit of ribulose-bisphosphate-carboxylase from Spinacia oleracea
Products: -
Products: -
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S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
-
Substrates: catalyzes methylation of the epsilon-amino group of Lys-14 in the large subunit of ribulose-bisphosphate-carboxylase from Spinacia oleracea
Products: -
Products: -
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S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
Substrates: specifically methylates Lys14 of the large subunit of ribulose-1,5-bisphosphate-carboxylase
Products: -
Products: -
?
additional information
?
-
-
Substrates: in Arabidopsis, the large subunit of Rubisco is not naturally methylated. LSMT-L is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive
Products: -
Products: -
?
additional information
?
-
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Substrates: histone methylation has significant effects on heterochromatin formation and transcriptional regulation
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additional information
?
-
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Substrates: LSMT has both mono-and di-methylation activities. Determination of free energy reaction profiles and transition state geometries using the crystal structure and on-the-fly ab initio QM/MM MD simulations in two simulation systems: LSMTAdoMet-Lys and LSMT-AdoMet-MeLys, which are enzyme-substrate complexes for mono- and di-methylation reactions in LSMT, method, overview. Methylation state specificity, overview
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additional information
?
-
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Substrates: several chloroplast-localized proteins are potential protein substrates for Rubisco LSMT
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additional information
?
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Substrates: bifunctional enzyme that catalyzes methylation of both the alpha-amino group of the small subunit of ribulose-1,5-bisphosphate-carboxylase
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additional information
?
-
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Substrates: bifunctional enzyme that catalyzes methylation of both the alpha-amino group of the small subunit of ribulose-1,5-bisphosphate-carboxylase
Products: -
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + histone L-lysine
S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine
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Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [fructose-1,6-bisphosphate aldolase]-lysine
S-adenosyl-L-homocysteine + [fructose-1,6-bisphosphate aldolase]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [large subunit of Rubisco]-L-lysine
S-adenosyl-L-homocysteine + [large subunit of Rubisco]-N6-methyl-L-lysine
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Substrates: methylation occurs at Lys-394
Products: -
Products: -
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S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
?
-
Substrates: the enzyme catalyzes the posttranslational methylation of the epsilon-amino group of Lys-14 in the large subunit of Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
S-adenosyl-L-homocysteine + [chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
-
Substrates: Rubisco LSMT utilizes a processive reaction mechanism to catalyse exclusively trimethylation of Lys14 without disassociation from Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
-
Substrates: Rubisco LSMT utilizes a processive reaction mechanism to catalyse exclusively trimethylation of Lys14 without disassociation from Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: LSMT transfers one or two methyl groups to a single lysine
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
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Substrates: LSMT transfers two methyl groups to a single lysine
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
-
Substrates: Rubisco LSMT utilizes a processive reaction mechanism to catalyse exclusively trimethylation of Lys14 without disassociation from Rubisco
Products: -
Products: -
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
-
Substrates: Rubisco LSMT utilizes a processive reaction mechanism to catalyse exclusively trimethylation of Lys14 without disassociation from Rubisco
Products: -
Products: -
?
additional information
?
-
-
Substrates: in Arabidopsis, the large subunit of Rubisco is not naturally methylated. LSMT-L is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive
Products: -
Products: -
?
additional information
?
-
-
Substrates: histone methylation has significant effects on heterochromatin formation and transcriptional regulation
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Protein lysine methyltransferase SMYD3 is involved in tumorigenesis through regulation of HER2 homodimerization.
Carcinoma
Overexpression of SET and MYND Domain-Containing Protein 2 (SMYD2) Is Associated with Tumor Progression and Poor Prognosis in Patients with Papillary Thyroid Carcinoma.
Carcinoma
WHSC1L1 drives cell cycle progression through transcriptional regulation of CDC6 and CDK2 in squamous cell carcinoma of the head and neck.
Carcinoma, Squamous Cell
WHSC1L1 drives cell cycle progression through transcriptional regulation of CDC6 and CDK2 in squamous cell carcinoma of the head and neck.
Infections
The methyltransferase Setdb2 mediates virus-induced susceptibility to bacterial superinfection.
Influenza, Human
The methyltransferase Setdb2 mediates virus-induced susceptibility to bacterial superinfection.
Intellectual Disability
Identification of protoberberine alkaloids as novel histone methyltransferase G9a inhibitors by structure-based virtual screening.
Leukemia
SETDB2 Links E2A-PBX1 to Cell-Cycle Dysregulation in Acute Leukemia through CDKN2C Repression.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
Targeting protein lysine methyltransferase G9A impairs self-renewal of chronic myelogenous leukemia stem cells via upregulation of SOX6.
Neoplasm Metastasis
Downregulation of NSD3 (WHSC1L1) inhibits cell proliferation and migration via ERK1/2 deactivation and decreasing CAPG expression in colorectal cancer cells.
Neoplasm Metastasis
Kinetic isotope effects reveal early transition state of protein lysine methyltransferase SET8.
Neoplasms
Analysis of the Substrate Specificity of the SMYD2 Protein Lysine Methyltransferase and Discovery of Novel Non-Histone Substrates.
Neoplasms
Downregulation of NSD3 (WHSC1L1) inhibits cell proliferation and migration via ERK1/2 deactivation and decreasing CAPG expression in colorectal cancer cells.
Neoplasms
Identification of protoberberine alkaloids as novel histone methyltransferase G9a inhibitors by structure-based virtual screening.
Neoplasms
Inhibition of SMYD2 Sensitized Cisplatin to Resistant Cells in NSCLC Through Activating p53 Pathway.
Neoplasms
Kinetic isotope effects reveal early transition state of protein lysine methyltransferase SET8.
Neoplasms
Overexpression of SET and MYND Domain-Containing Protein 2 (SMYD2) Is Associated with Tumor Progression and Poor Prognosis in Patients with Papillary Thyroid Carcinoma.
Neoplasms
Protein lysine methyltransferase G9a inhibitors: design, synthesis, and structure activity relationships of 2,4-diamino-7-aminoalkoxy-quinazolines.
Neoplasms
Somatic Cancer Mutations in the SUV420H1 Protein Lysine Methyltransferase Modulate Its Catalytic Activity.
Neoplasms
The Discovery of Novel Histone Lysine Methyltransferase G9a Inhibitors (Part 1): Molecular Design Based on a Series of Substituted 2,4-Diamino-7-aminoalkoxyquinazoline by Molecular-Docking-Guided 3D Quantitative Structure-Activity Relationship Studies.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0129
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
-
at pH 7.8 and 30Ā°C
-
0.0138
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
-
at pH 7.8 and 30Ā°C
-
0.014
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
-
at pH 7.8 and 30Ā°C
-
0.0148
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
-
at pH 7.8 and 30Ā°C
-
0.314
[gamma-tocopherol methyltransferase]-L-lysine
-
at pH 7.8 and 30Ā°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.05
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
-
at pH 7.8 and 30Ā°C
-
1.32
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
-
at pH 7.8 and 30Ā°C
-
0.57
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
-
at pH 7.8 and 30Ā°C
-
0.933
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
-
at pH 7.8 and 30Ā°C
-
1.05
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
-
at pH 7.8 and 30Ā°C
-
0.033
[gamma-tocopherol methyltransferase]-L-lysine
-
at pH 7.8 and 30Ā°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme that catalyzes methylation of both the alpha-amino group of the small subunit of ribulose-1,5-bisphosphate-carboxylase
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RBCMT_PEA
489
0
55110
Swiss-Prot
Chloroplast (Reliability: 2)
RBCMT_TOBAC
491
0
56000
Swiss-Prot
Chloroplast (Reliability: 4)
B9S910_RICCO
502
0
56639
TrEMBL
Chloroplast (Reliability: 3)
A0A2I0AI40_9ASPA
500
1
57611
TrEMBL
Chloroplast (Reliability: 1)
G0QN52_ICHMG
Ichthyophthirius multifiliis (strain G5)
165
0
19459
TrEMBL
other Location (Reliability: 1)
G0QJF8_ICHMG
Ichthyophthirius multifiliis (strain G5)
326
1
39486
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2P6SJV3_ROSCH
458
0
52137
TrEMBL
Mitochondrion (Reliability: 1)
A0A2G9FWH2_9LAMI
413
0
47785
TrEMBL
other Location (Reliability: 2)
G0QJF9_ICHMG
Ichthyophthirius multifiliis (strain G5)
176
0
21198
TrEMBL
other Location (Reliability: 2)
G0QRF1_ICHMG
Ichthyophthirius multifiliis (strain G5)
417
0
49306
TrEMBL
other Location (Reliability: 3)
A0A7C9AW57_OPUST
512
0
57246
TrEMBL
Chloroplast (Reliability: 1)
A0A0D2MHW5_9CHLO
268
0
28505
TrEMBL
other Location (Reliability: 2)
A0A5B7ARD1_DAVIN
160
0
17943
TrEMBL
Mitochondrion (Reliability: 4)
A0A7C9CP85_OPUST
301
0
34727
TrEMBL
other Location (Reliability: 1)
A0A2P6R2T9_ROSCH
495
0
55780
TrEMBL
Chloroplast (Reliability: 1)
G7INE0_MEDTR
480
0
55323
TrEMBL
Mitochondrion (Reliability: 3)
B9SGF2_RICCO
456
0
51585
TrEMBL
Mitochondrion (Reliability: 2)
A0A2G9G314_9LAMI
501
0
56328
TrEMBL
Mitochondrion (Reliability: 3)
M2X4A7_GALSU
546
0
64376
TrEMBL
Mitochondrion (Reliability: 5)
A0A0B2S6P3_GLYSO
409
0
46672
TrEMBL
other Location (Reliability: 2)
A0A2G9FWU3_9LAMI
488
0
55969
TrEMBL
Chloroplast (Reliability: 4)
A0A2G9H4N2_9LAMI
465
0
52411
TrEMBL
Mitochondrion (Reliability: 4)
A0A7C9CPX2_OPUST
500
0
56892
TrEMBL
Chloroplast (Reliability: 4)
A0A2I0AB43_9ASPA
557
0
62657
TrEMBL
other Location (Reliability: 5)
A0A2G9GDV1_9LAMI
498
0
56701
TrEMBL
Chloroplast (Reliability: 5)
A0A1Z5J8P5_FISSO
466
0
52513
TrEMBL
other Location (Reliability: 5)