Information on EC 2.1.1.72 - site-specific DNA-methyltransferase (adenine-specific)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.72
-
RECOMMENDED NAME
GeneOntology No.
site-specific DNA-methyltransferase (adenine-specific)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
69553-52-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SSU
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain D and xD
-
-
Manually annotated by BRENDA team
strain D and xD
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain NEB686
-
-
Manually annotated by BRENDA team
Bacillus sp. NEB686
strain NEB686
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Citrobacter sp.
strain RFL231
UniProt
Manually annotated by BRENDA team
strain RFL231
UniProt
Manually annotated by BRENDA team
strain M82B
-
-
Manually annotated by BRENDA team
strain M82B
-
-
Manually annotated by BRENDA team
strain NEB479
UniProt
Manually annotated by BRENDA team
strain RI
-
-
Manually annotated by BRENDA team
strain TXD1
UniProt
Manually annotated by BRENDA team
strain TXD1
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain 14P
UniProt
Manually annotated by BRENDA team
strain SE-589
-
-
Manually annotated by BRENDA team
Hia5 protein
UniProt
Manually annotated by BRENDA team
Haemophilus influenzae Rd (FluMu)
-
-
-
Manually annotated by BRENDA team
strain NSH57
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain FA1090
-
-
Manually annotated by BRENDA team
strain FA1090
-
-
Manually annotated by BRENDA team
strain ST640 Sange
-
-
Manually annotated by BRENDA team
Neisseria lactamica ST640 Sange
strain ST640 Sange
-
-
Manually annotated by BRENDA team
strain Z2491
-
-
Manually annotated by BRENDA team
Neisseria meningitidis Z2491 (Pnme1)
-
-
-
Manually annotated by BRENDA team
strain X14
UniProt
Manually annotated by BRENDA team
strain X14
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Peridinium triquetrum
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain OM2164
UniProt
Manually annotated by BRENDA team
strain OM2164
UniProt
Manually annotated by BRENDA team
strain PRwf-1
UniProt
Manually annotated by BRENDA team
strain PRwf-1
UniProt
Manually annotated by BRENDA team
strain BisB5
UniProt
Manually annotated by BRENDA team
strain BisB5
UniProt
Manually annotated by BRENDA team
strain SW
UniProt
Manually annotated by BRENDA team
strain SW
UniProt
Manually annotated by BRENDA team
strain DSS-3
UniProt
Manually annotated by BRENDA team
strain PR-6
-
-
Manually annotated by BRENDA team
Synechococcus sp. PCC 7002 PR-6
strain PR-6
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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 + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
S-adenosyl-L-methionine + oligodeoxynucleotide duplexes
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
substrate contains one single specific recognition site as 5'-GATC/5'-GATC, or modified variants
-
-
?
S-adenosyl-L-methionine + pUC19 DNA adenine
S-adenosyl-L-homocysteine + pUC19 DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
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-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
2-3 mM required
Co2+
-
3fold stimulation of activity at 1 mM
Mn2+
-
5fold stimulation of activity at 1 mM
additional information
-
Ca2+, Zn2+, and Ni2+ ions do not affect the methylation activity of the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20mer fully methylated DNA duplex
-
product inhibition, noncompetitive against both S-adenosyl-L-methionine and 20mer unmethylated DNA duplex
-
5'-S-(2-carboxyethyl)-5'-thioadenosine
-
non-competitive inhibition
diethyl dicarbonate
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the inactivation of the enzyme by diethyl dicarbonate is specific for histidine residues, pre-incubating the methylase with DNA is able to protect the enzyme from diethyl dicarbonate inactivation, hydroxylamine is unable to reverse the effect caused by diethyl dicarbonate
fully methylated sites 5'-GMTC/5'-GMTC DNA
-
the inhibition potential of fully methylated sites 5'-GMTC/5'-GMTC is much lower for a long DNA molecule compared to short single-site duplxes, enzyme does not dissociate from the DNA but continues one-sited methylation with linear diffusion, after which it rapidly reorientates itself and reconstitutes
-
K+
-
enzyme activity decreases 100fold in the presence of 100 mM K+
methylated DNA
methylated duplex DNA
-
partial inhibition at high concentrations, mixed inhibition against un- or hemimethylated DNA, noncompetitive against S-adenosyl-L-methionine
-
Na+
-
enzyme activity decreases 100fold in the presence of 100 mM Na+
S-adenosyl-L-homocysteine
S-adenosyl-L-methionine
-
methylation reaction is inhibited above 0.0015 mM of S-adenosyl-L-methionine
sinefungin
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-S-(propionic acid)5'-deoxy-9-(1'-beta-D-ribofuranosyl)1,3-dideazaadenine
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more than 200% activity in the presence of 0.015 mM 5'-S-(propionic acid)5'-deoxy-9-(1'-beta-D-ribofuranosyl)1,3-dideazaadenine
S-adenosyl-L-methionine
-
stimulates at increasing concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000017
DNA
-
pH 8.0, 37C
0.00000000000001 - 0.0199
DNA adenine
0.0001 - 0.0122
S-adenosyl-L-methionine
0.0000000011
T4 gt- dam- DNA
0.0000098
T7 DNA adenine
-
in 33 mM Tris-acetate, pH 7.9, 10 mM magnesium acetate, 66 mM potassium acetate, 1 mM dithiothreitol, at 55C
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00033 - 0.0155
DNA
0.000096 - 0.93
DNA adenine
0.21
oligodeoxynucleotide duplexes 5'-GATC/5'-GATC
Enterobacteria phage T4
-
-
-
0.000118 - 0.00117
S-adenosyl-L-methionine
0.037
T7 DNA adenine
Geobacillus stearothermophilus
-
in 33 mM Tris-acetate, pH 7.9, 10 mM magnesium acetate, 66 mM potassium acetate, 1 mM dithiothreitol, at 55C
-
additional information
additional information