Information on EC 2.1.1.259 - [fructose-bisphosphate aldolase]-lysine N-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.259
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RECOMMENDED NAME
GeneOntology No.
[fructose-bisphosphate aldolase]-lysine N-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine = 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[fructose-bisphosphate aldolase]-lysine N6-methyltransferase
The enzyme methylates a conserved lysine in the C-terminal part of higher plant fructose-bisphosphate aldolase (EC 4.1.2.13). The enzyme from pea (Pisum sativum) also methylates Lys-14 in the large subunits of hexadecameric higher plant ribulose-bisphosphate-carboxylase (EC 4.1.1.39) [2], but that from Arabidopsis thaliana does not.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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knockdown of the LSMT homologue in transgenic tobacco plants results in a 2fold decrease of alpha-tocopherol
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 + [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-L-lysine
S-adenosyl-L-homocysteine + [large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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mutagenesis of lysine residues 8, 18 and 28 to either Arg or Ala does not affect methylation of Lys-14 by the enzyme, whereas mutagenesis of the Lys-14 methylation site abolishes methylation
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?
S-adenosyl-L-methionine + [acyl carrier protein I precursor]-L-lysine
S-adenosyl-L-homocysteine + [acyl carrier protein I precursor]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine
S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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the substrate is trimethylated at a conserved lysyl residue located close to the C terminus
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?
S-adenosyl-L-methionine + [gamma-tocopherol methyltransferase]-L-lysine
S-adenosyl-L-homocysteine + [gamma-tocopherol methyltransferase]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [granule-bound starch synthase I precursor]-L-lysine
S-adenosyl-L-homocysteine + [granule-bound starch synthase I precursor]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [NAD(P)H-quinone oxidoreductase chain 5]-L-lysine
S-adenosyl-L-homocysteine + [NAD(P)H-quinone oxidoreductase chain 5]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-L-lysine
S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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no natural substrate. The enzyme is able to interact with unmethylated Rubisco, but the complex is catalytically unproductive
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?
S-adenosyl-L-methionine + [Rubisco large subunit]-L-lysine
S-adenosyl-L-homocysteine + [Rubisco large subunit]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
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-
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-
?
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-methionine + [fructose 1,6-bisphosphate aldolase]-L-lysine
S-adenosyl-L-homocysteine + [fructose 1,6-bisphosphate aldolase]-N6,N6,N6-trimethyl-L-lysine
show the reaction diagram
-
the substrate is trimethylated at a conserved lysyl residue located close to the C terminus
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01923
S-adenosyl-L-methionine
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in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30C
1.2
[large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-L-lysine
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in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
S-adenosyl-L-methionine
Pisum sativum
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in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30C
0.011
[large subunit of spinach Rubisco-human carbonic anhydrase II fusion protein]-L-lysine
Pisum sativum
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in 100 mM Bicine, 20 mM MgCl2 pH 8.0, at 30C
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51700
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x * 51700, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 51700, calculated from amino acid sequence