Information on EC 2.1.1.127 - [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.127
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RECOMMENDED NAME
GeneOntology No.
[ribulose-bisphosphate carboxylase]-lysine N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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-
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
139171-98-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-homocysteine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + L-Lys
S-adenosyl-L-homocysteine + methyl-L-Lys
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + methyl-L-Lys
S-adenosyl-L-homocysteine + dimethyl-L-Lys + trimethyl-L-Lys
show the reaction diagram
about 2fold higher activity than with Lys
-
-
?
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
show the reaction diagram
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
show the reaction diagram
S-adenosyl-L-methionine + [fructose-1,6-bisphosphate aldolase]-lysine
S-adenosyl-L-homocysteine + [fructose-1,6-bisphosphate aldolase]-N6-methyl-L-lysine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-lysine
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
show the reaction diagram
-
methylation is required for gamma-tocopherol methyltransferase activity
-
-
?
S-adenosyl-L-methionine + [large subunit of Rubisco]-L-lysine
S-adenosyl-L-homocysteine + [large subunit of Rubisco]-N6-methyl-L-lysine
show the reaction diagram
-
methylation occurs at Lys-394
-
-
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
show the reaction diagram
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
?
show the reaction diagram
-
the enzyme catalyzes the posttranslational methylation of the epsilon-amino group of Lys-14 in the large subunit of Rubisco
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-
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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
show the reaction diagram
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate-carboxylase]-N6-methyl-L-lysine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
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
show the reaction diagram
S-adenosyl-L-methionine + [fructose-1,6-bisphosphate aldolase]-lysine
S-adenosyl-L-homocysteine + [fructose-1,6-bisphosphate aldolase]-N6-methyl-L-lysine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6-methyl-L-lysine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + [large subunit of Rubisco]-L-lysine
S-adenosyl-L-homocysteine + [large subunit of Rubisco]-N6-methyl-L-lysine
show the reaction diagram
-
methylation occurs at Lys-394
-
-
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase]-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase]-N6-methyl-L-lysine
show the reaction diagram
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]-L-lysine
?
show the reaction diagram
-
the enzyme catalyzes the posttranslational methylation of the epsilon-amino group of Lys-14 in the large subunit of Rubisco
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-
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additional information
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methyl-L-Lys
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S-adenosyl-L-homocysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0027 - 0.0083
ribulose-1,5-bisphosphate-carboxylase
0.018
ribulose-bisphosphate-carboxylase from Spinacia sp.
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-
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0.006 - 0.0137
S-adenosyl-L-methionine
0.0129 - 0.0138
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
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0.014 - 0.0148
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
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0.314 - 0.32
[gamma-tocopherol methyltransferase]-L-lysine
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0.0045
[large subunit of Rubisco]-L-lysine
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at pH 7.8 and 30C
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0.0014
[ribulose-1,5-bisphosphate carboxylase]-lysine
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-
additional information
additional information
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substrate binding kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000062
L-Lys
Pisum sativum
Q43088
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0.00025
methyl-L-Lys
Pisum sativum
Q43088
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.05 - 1.32
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 2]-L-lysine
42164
0.57 - 1.05
[chloroplastic fructose 1,6-bisphosphate aldolase isoform 3]-L-lysine
42165
0.033 - 0.05
[gamma-tocopherol methyltransferase]-L-lysine
19660
8.65
[large subunit of Rubisco]-L-lysine
Pisum sativum
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at pH 7.8 and 30C
88160
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
101
methyl-L-Lys
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 10
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
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x * 56000, calculation from nucleotide sequence
60000
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x * 60000, SDS-PAGE
additional information
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the full-length enzyme is processed by removing the N-terminal 36 amino acids when expressed in E. coli cells
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with S-adenosyl-L-methionine, crystal structure analysis
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hanging drop vapour diffusion method, the crystal structure of the large subunit of the enzyme in ternary complex with either Lys or epsilon-N-methyllysine and the product S-adenosylhomocysteine are determined to resolution of 2.65 and 2.55 A, respectively
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, 300 mM KCl, 5 mM DTT, stable for at least 1 month
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-80C, in presence of 2 mg/ml beta-lactoglobulin, indefinitely stable
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4C, stable for up to 30 days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
large scale affinity purification
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native and recombinant enzyme
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nickel-Sepharose column chromatography, Sephadex G-25 gel filtration, and Q-Sepharose column chromatography
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme expression in enzyme-deficient Nicotiana tabacum plants, recombinant substrate identification
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expressed in Escherichia coli Rosetta-2 cells
expression in Escherichia coli
RLSMT, expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y305F
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the SET7/9 Y305F mutant not only has a high efficiency for mono-methylation but also becomes a dimethylase. The Y305F mutation leads to a less tight active site
additional information
Show AA Sequence (115 entries)
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