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Enzyme Nomenclature
Information on EC 2.1.1.72 - site-specific DNA-methyltransferase (adenine-specific)
Word Map on EC 2.1.1.72
- 2.1.1.72
- mtases
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endonuclease
-
duplex
- s-adenosyl-l-methionine
- adomet
- bacteriophage
- cytosine
-
mismatch
-
hemimethylated
-
unmethylated
-
flip
-
damid
-
restriction-modification
- s-adenosyl-l-homocysteine
-
protein-dna
- 2-aminopurine
- medicine
- m.hhai
-
adohcy
- n6-methyladenine
-
methylation-sensitive
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cross-protective
-
extrahelical
- aquaticus
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leucine-responsive
- sinefungin
-
gatatc
-
methyl-directed
- analysis
- pharmacology
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.1.1.72
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RECOMMENDED NAME
GeneOntology No.
site-specific DNA-methyltransferase (adenine-specific)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
steady-state-ordered bi-bi mechanism in which the order of substrate binding and product release is S-adenosyl-L-methionine, DNA, DNAMe, S-adenosyl-L-homocysteine
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
reaction scheme and random bi bi kinetic mechanism
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
two distinct stages of methylation under single turnover conditions
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
ordered bi bi mechanism during progressive methylation process
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
ordered bi bi mechanism with S-adenosyl-L-homocysteine leaving at last, cooperative binding of 2 molecules of enzyme per DNA is required for activity
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
ordered bi bi mechanism with S-adenosyl-L-methionine binding first, fast methyl transfer, slow product release
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
D181 and Y184 are essential for activity
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
molecular mechanism, effector action of substrates, progressive methylation of extended DNA containing more than one methylation site
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S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
active site structure, enzyme-methyl donor product interactions, substrate binding mechanism and conformational changes, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
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CAS REGISTRY NUMBER
COMMENTARY
69553-52-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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485566, 485567, 485568, 485569, 485570, 485573, 485574, 485576, 485577, 658407, 659268, 659301, 659905, 660031
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485572, 485578, 658407, 659422, 659715, 659920, 660031, 664054, 671878, 676746, 702115, 702334, 702628, 703200, 703347, 703765, 704168, 705127, 705175, 713742, 719096, 720029, 720604, 733356
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M.EcoRV, M.EcoRI, Escherichia coli dam methyltransferase and M.FokI enzyme
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strains GHY15, GHY121, GHY125, GHY128, GHY129, GHY130, GHY137, GHY138, GHY139, GHY140, GHY141, GHY142, GHY143, GHY144, GHY145, GHY146, GHY147, GHY148, GHY150, GHY151, GHY157, GHY158 and GHY226
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strains GHY178, GHY179, GHY180, GHY238, GHY239, GHY240, GHY243, GHY244, GHY245, GHY246, GHY247, GHY248, GHY249, GHY250, GHY251, GHY256, GHY257, GHY258, GHY266, GHY267, GHY268, GHY274, GHY275, GHY276 and GHY347
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
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deletion of the methyltransferase M.HpyAXII is lethal when associated with an active endonuclease, M.HpyAXII MTase activity is not required for establishing infection in mice
malfunction
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knockout of a putative DNA methyltransferase gene in Campylobacter jejuni causes reduced motility, aberrant flagellar appearance, and hyperadherence to epithelial cells, accompanied by reduced invasion
malfunction
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lack of Dam methylation causes partial attenuation upon intranasal or intraperitoneal inoculation of mice
malfunction
-
mutants lacking Dam methylase are not viable, Dam overproduction does not impair bacterial growth
malfunction
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a relevant defect of Yersinia enterocolitica Dam overproducers is enhanced invasion capacity, probably associated with transcriptional alterations in invasin genes inv and ail, and with changes in the composition of lipopolysaccharide O-antigen
malfunction
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Dam negative mutants contain lowered levels of the secretion of pathogenicity island 1 transcriptional regulators HilA, HilC, HilD, and InvF. Dam negative mutants with the intestinal epithelium have been tentatively correlated with reduced secretion of pathogenicity island 1
malfunction
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deletion of the methyltransferase M.HpyAXII is lethal when associated with an active endonuclease, M.HpyAXII MTase activity is not required for establishing infection in mice
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metabolism
the enzyme potentially participates in arsenic metabolism in vivo
metabolism
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the enzyme, in addition to being responsible for GATC methylation, can also function as a methylation-independent transcriptional repressor
physiological function
-
MmeI DNA methylation prevents cleavage by MmeI
physiological function
-
DNA adenine methyltransferase is essential for proper DNA replication timing, gene regulation, and mismatch repair
physiological function
-
transcriptional inhibition by hemimethylation of genes dnaA, ccrM, and ctrA
physiological function
-
synthesis of P pili (pyelonephritis-associated protein) is subjected to phase variation and switching between On and Off states is controlled by Dam methylation, Dam methylation inhibits OxyR binding in the On state, Dam methylation of the upstream GATC site in agn43 increases transcription initiation, which occurs precisely at the G nucleotide of the GATC, finP transcription is activated by Dam methylation, Dam methylation does not regulate tir gene transcription nor tir mRNA stability
physiological function
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Dam methylation of finP prevents repression by H-NS,methlation of traJ leads to activation of Lrp binding to the traJ UAS by strand-specific hemimethylation
physiological function
-
DNA adenine methylation is involved in Aeromonas hydrophila pathogenesis
physiological function
-
DNA adenine methylation is involved in Aeromonas hydrophila pathogenesis
physiological function
-
CcrM regulates the genes dnaA, ctrA, and ccrM at transcriptional level
physiological function
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the formation of 6-methyladenine reduces the thermodynamic stability of DNA and changes DNA curvature, as a consequence, the methylation state of specific adenosine moieties can affect DNA-protein interactions. Dam methylation regulates virulence genes at the posttranscriptional level. Dam methylation plays a role in enterohemorrhagic Escherichia coli by controlling the production of the virulence factor Shiga toxin 2
physiological function
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Dam methylation may control the expression of virulence genes
physiological function
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the formation of 6-methyladenine reduces the thermodynamic stability of DNA and changes DNA curvature, as a consequence, the methylation state of specific adenosine moieties can affect DNA-protein interactions. Dam methylation regulates virulence genes at the posttranscriptional level
physiological function
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Dam methylation 1 may control transcription of a postranscriptional regulator of hilD expression, Dam methylation regulates the level and the stability of hilD mRNA
physiological function
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transcriptional regulation of std expression by Dam methylation
physiological function
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Dam is a key regulator of the pap operon which codes for the pilus proteins necessary for uropathogenic Escherichia coli cellular adhesion. Lrp, in the presence and in the absence of PapI and nonspecific DNA, specifically protects pap regulatory GATC sites from Dam methylation when allowed to compete with Dam for assembly on unmethylated and hemimethylated pap DNA. Only at low Lrp concentrations will Dam compete effectively for binding and methylation of the proximal GATC site, leading to a phase switch resulting in the expression of pili
physiological function
Dam is a virulence determinant and plays a role in the pathogenesis of Edwardiella tarda strain TXD1, temporal expression of dam is essential for optimal bacterial infection
physiological function
the enzyme plays a significant role in determining susceptibility to arsenic toxicity and carcinogenicity. Overexpression of the enzyme in UROtsa cells increases resistance to arsenic treatment
physiological function
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DNA adenine methyltransferase controls the expression of the cytotoxic enterotoxin (act) gene of Aeromonas hydrophila via tRNA modifying enzyme-glucose-inhibited division protein. Overproduction of DNA adenine methyltransferase leads to a concomitant increase in Act-associated biological activities of a diarrheal isolate SSU of Aeromonas hydrophila
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair; the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
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the enzyme methylates the rha antirepressor gene thereby activating it. The enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
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the enzyme is essential for cell viability and confers potent cross-protective efficacy as well as decreased virulence and spontaneous mutation frequency
physiological function
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the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
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the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
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Dam is a virulence determinant and plays a role in the pathogenesis of Edwardiella tarda strain TXD1, temporal expression of dam is essential for optimal bacterial infection
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physiological function
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the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
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the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
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the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
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the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
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the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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physiological function
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the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
S-adenosyl-L-methionine + oligodeoxynucleotide duplexes
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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substrate contains one single specific recognition site as 5'-GATC/5'-GATC, or modified variants
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?
S-adenosyl-L-methionine + pUC19 DNA adenine
S-adenosyl-L-homocysteine + pUC19 DNA 6-methyladenine
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-
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?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Bacillus sp. NEB686
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GANTC
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the DNA target sequence is GANTC, CcrM is more active on hemimethylated than unmethylated DNA
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the target sequence is 5'GATC3'
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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129-mer DNA or pUC19 DNA are used as substrates
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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-
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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Dam belongs to the alpha-class of adenine methyltransferases and transfers a methyl group to the N-6 position of the adenine in the DNA sequence 5'-GATC-3'
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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Dam methylates a GATC recognition site
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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Dam methylates the adenine residue in GATC sites
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Dam methylates the N-6 position of adenine in the DNA sequence 5'-GATC-3' and is highly processive, catalyzing multiple methyltransfers prior to dissociating from the DNA
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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Dam methylates the N-6 position of the adenine in the sequence 5'-GATC-3', Dam shows a dramatic preference for the in vitro methylation of certain GATC sequences in plasmids and PCR-derived DNAfragments
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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DNA adenine methyltransferase methylates the N6 positions of adenines in the sequence 5'-GATC-3'
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-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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EcoP15I MTase adds a methyl group to the second adenine in the recognition sequence 5'-CAGCAG-3' in the presence of S-adenosyl-L-methionine
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-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
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-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
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the wild type enzyme shows target specificity for GATC sites
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-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the EcoRV DNA methyltransferase methylates the first adenine in the GATATC recognition sequence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the enzyme methylates adenines at the N6 position of palindromic 5’-GATC-3’ sites. The enzyme ethylates both strands of the same site prior to fully dissociating from the DNA, a process referred to as intrasite processivity. Intrasite processivity is disrupted when the DNA flanking a single GATC site is longer than 400 bp on either side. The introduction of a second GATC site within this flanking DNA reinstates intrasite methylation of both sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the Hin1523 protein causes the methylation of 29.6% of the adenines in lambda DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
the Hia5 protein causes the methylation of 61% of the adenines in lambda DNA
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-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
the Hia5 protein causes the methylation of 61% of the adenines in lambda DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the Hin1523 protein causes the methylation of 29.6% of the adenines in lambda DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
duplex 2 DNA, 5'-GCAG-3' is the recognition site for the enzyme
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
HP0050 methyltransferase methylates one adenine at a time in the sequence 5'-GAAG-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
HP0050 methyltransferase methylates one adenine at a time in the sequence 5'-GAAG-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
duplex 2 DNA, 5'-GCAG-3' is the recognition site for the enzyme
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
MmeI modifies only the adenine in the top strand, 5’-TCCRAC-3’, MmeI endonuclease activity is blocked by this top strand adenine methylation and is unaffected by methylation of the adenine in the complementary strand, 5’-GTYGGA-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam catalyzes postreplicative methylation of adenosine moieties located in 5'-GATC-3' sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Synechococcus sp. PCC 7002 PR-6
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
recognition sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme preferentially binds DNA before S-adenosylmethionine. S-Adenosylhomocysteine is preferentially released from the enzyme before fully methylated DNA. Binding of both substrates and methylation occurs first in a rapid step followed by regeneration of enzyme in a second rate-limiting step
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is involved in cell cycle regulation of Caulobacter crescentus
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
a biotinylated double stranded 23mer oligodeoxynucleotide with one hemimethylated GANTC site is used as substrate
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
nonglucosylated, hydroxymethylcytosine-containing T2gt- virion DNA has a higher level of methylation than T4gt virion DNA does
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme mediates methyl group transfer reaction from S-adenosyl-L-methionine to adenine in the palindromic recognition sequence, GATC, of a 20-mer oligonucleotide duplex
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
in unmethylated target (2A/A duplex), the enzyme alone randomly binds to the asymetric 2A/A duplex, S-adenosyl-L-methionine induces an allosteric T4 conformational change that promotes reorientation of the enzyme to the strand containing the native base. S-Adenosyl-L-methionine increases enzyme binding-specificity, in addition to serving as the methyl donor, the enzyme recognizes the palindromic sequence GATC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
various synthetic oligonucleotide substrates. Upon collision of an enzyme monomer with an oligonucleotide duplex, an asymmetrical complex forms in which the enzyme (randomly oriented relative to one of the strands of the specific recognition site) catalyzes a fast transfer of the methyl group from S-adenmosylmethionine to the adenosine residue. Simultaneously, a second T4MTAse subunit is added to the complex, providing for the continuation of the reaction
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme catalyzes methyl group transfer from S-adenosyl-L-methionine to the N6-position of adenine in the palindromic sequence GATC. The rate-limiting step is release of product methylated DNA from the enzyme
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
oligonucleotide substrates containing the native or modified recognition site. The enzyme recognizes the palindromic sequence GATC and catalyzes transfer of the methyl group from S-adenosyl-L-methionine to the N6-position of adenine. The release of product is the rate-limiting step in the reaction
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
canonical 12-mer and 20-mers various defective duplexes containing some defect in the DNA-target site, e.g. the absence of an internucleotide phosphate or a nucleotide within the recognition site, or a single-stranded region
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
nonglucosylated unmethylated T4 gt- dam- DNA. The enzyme methylates the palindromic tetranucleotide, GATC, designated the canonical sequence. At high Mtase:DNA ratios, T4 Dam can methylate some noncanonical sequences belonging to GAY, where Y represents cytosine or thymine
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
synthetic oligonucleotide substrates containing the native recognition site GATC or its modified variants
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
interaction with substrates containing defective recognition sites. Deoxyguanosine residues in both strands of the modified GATC are indispensable for complex formation
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
nonglucosylated, hydroxymethylcytosine-containing T2gt- virion DNA has a higher level of methylation than T4gt virion DNA does
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
methylation of DNA-adenine at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as in bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific target sequence is GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
unmethylated or hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
binding site is the GATC sequence, the adenine is located in the palindromic recognition site GATC, substrate binding mechanism
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific for methylation site sequence GATC and structure, an intact GAT sequence is essential for activity, altered structural symmetry of the DNA substrate decreases kcat sharply, the best contact between enzyme and DNA is a palindromic interaction site covering the 5'-symmetric residues, which is located in the major groove, and another one in the 3'-half covering the 3'-symmetric residues is located in the minor groove, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific methylation of oligonucleotide duplexes containing one or two target sequence GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
specific methylation of target sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific target sequence is GATC, transition of enzyme-DNA interaction from nonspecific to specific interaction utilizing different substrates, identification of discriminatory contacts stabilizing the transition state, and antidiscriminatory contacts not affecting the methylation of the cognate site but disfavor activity at noncognate sites, involved residues are M114, R116, P126, G128, R130, F111, S112, D171, K11, and Y174, overview, flipping of target adenine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
unmethylated or hemimethylated DNA, two distinct stages of methylation under single turnover conditions
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
canonical 14mers and various substituted duplexes. Non-selfcomplementary tetradecamer duplex d[GCCGGATCTAGACG]*d[CGTCTAGATCCGGC] containing the hemimethylated GATC target sequence on one or the other strand and modifications in the GATC target sequence of the complementary strands. Large differences in DNA methylation of duplexes containing single dI or dG substitutions of the Dam recognition site are observed compared with the canonical substrate, if the substitution involves the top strand, on the G-C rich side. Substitution in either strand by uracil or 5-ethyluracil result in small perturbation of the methylation patterns. When 2,6-diamino-purine replaces the adenine to be methylated, small but significant methylation is observed
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
non-self-complementary tetradecanucleotide duplexes that contain the GATC target sequence. The enzyme is rather tolerant to base modification, binding of the enzyme is inversely proportional to the thermodynamic stability of the duplex in the ternary complex
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of DNA in a sequence specific manner, low substrate specificity with respect to the target base. Cytosine residues can be methylated if they are located in a C:T mismatch base pair at the target position of the enzyme, modification of cytosine residues at position N4
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a critical regulator of bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of the site GATCprox proximal to the promotor is required for transition to the phase On state by specifically blocking PapI-dependent binding of Lrp to promotor proximal sites 4-6, expression of pyelonephritis-associated pili, i.e. Pap, in uropathogenic Escherichia coli is epigenetically controlled by a reversible OFF to ON switch, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is cell cycle regulated and essential for viability
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
DNA substrate from calf thymus, methylation of adjacent GATC sites is distributive with DNA derived from a genetic element that controls the transcription of the adjacent genes, the first methylation event is followed by enzyme release
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme methylates the first adenine in the sequence ATGCAT
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of target sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
required substrate recognition target sequence is GATC, occuring base flipping in absence of S-adenosyl-L-methionine is a biphasic process and very fast, but binding of the flipped base into the active site pocket requiring S-adenosyl-L-methionine is slow, active site contains the conserved DPPY motif, whose tyrosine184 residue stacks to the flipped target base
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific for methylation site sequence GATC and structure, an intact GA sequence is essential for activity, altered structural symmetry of the DNA substrate decreases kcat sharply, the best contact between enzyme and DNA is a palindromic interaction site covering the 5'-symmetric residues, which is located in the major groove, and another one in the 3'-half covering the 3'-symmetric residues is located in the minor groove, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
transition of enzyme-DNA interaction from nonspecific to specific interaction utilizing different substrates, identification of discriminatory contacts stabilizing the transition state, and antidiscriminatory contacts not affecting the methylation of the cognate site but disfavor activity at noncognate sites, involved are Y119, N120, L122, R124, and P134, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme recognizes 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is not important in mismatch repair and for adherence of the bacterium to host cells, e.g. HEp-2 cells
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a member of a restriction-modification system, R-M system, plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme recognizes the sequence 5'-GGTACC-3', methylation at position N6, enzyme utilizes plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
substrate and product binding site structures
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GGGTGATCAGGG
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
CCCTGATCACCC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme de novo methylates the first adenine residue in the TGATCA sequence in the single-stranded or double-stranded DNA substrate, but it prefers single-stranded structures
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GCGTGATCACGC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GGGTGATCAGGG+CCCTGATCACCC, annealed
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
lambda phage DNA
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme modifies the third adenine within the recognition sequence 5-ATTAAT-3'
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
-
-
-
?
additional information
?
-
-
the enzyme is part of the type II restriction-modification system AhdI, overview
-
-
-
additional information
?
-
-
the common methyl transfer from S-adenosyl-L-methionine to an exocyclic amino group, catalyzed by many enzymes, does not dictate a common kinetic scheme for MTases, comparison to T4Dam MTase from bacteriophage T4
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Bacillus sp. NEB686
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme has a high specificity for GANTC sites, with only minor preferences at the central position. It slightly (1.5fold) prefers hemimethylated DNA over methylated DNA
-
-
-
additional information
?
-
-
the enzyme methylates GANTC sequences but does not specifically bind to DNA containing GANTC sequences
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
S-adenosyl-L-methionine plays a crucial role in reorientation of the enzyme in DNA with mutationally altered Ade residues to 2-aminopurine, overview
-
-
-
additional information
?
-
-
DNA substrate specificities of wild-type and mutant enzymes
-
-
-
additional information
?
-
-
enzyme and S-adenosyl-L-methionine form a catalytically active complex
-
-
-
additional information
?
-
enzyme binds also nonspecific to DNA, linear diffusion along the DNA, overview
-
-
-
additional information
?
-
-
substrate specificity with different oligonucleotides, substrate binding specificity, overview
-
-
-
additional information
?
-
-
catalyzes the transfer of a methyl group to the C5 position of the 3'-side cytosine of each strand of the recognition sequence, M.EcoRII binding is diminished by factors of 5-30 but the catalytic activity is either abolished or reduced 4-80fold when trans-anti-B[a]P-N2-dG lesions are introduced into the EcoRII recognition sequence, methylation rates are also diminished and in some cases entirely abolished, depending on the position of the lesion within the recognition sequence
-
-
?
additional information
?
-
-
DNA methylation by DAM may not globally affect gene transcription by physically blocking access of transcription factors to binding sites, Dam is down regulated in the stationary phase, which correlates with the enrichment of GATC in binding sites for CRP and Sigma 38
-
-
-
additional information
?
-
-
the preferred substrate consists of the annealed product of oligonucleotides 5'-CATTTACTTGATCCGGTATGC-3' and 5'-GCATACCGGATCAAGTAAATG-3', while the nonpreferred substrate consists of the annealed product of oligonucleotides 5'-CATTTAGACGATCTTTTATGC-3' and 5'-GCATAAAAGATCGTCTAAATG-3'
-
-
-
additional information
?
-
-
the wild type Dam shows no detectable activity at GATT sites
-
-
-
additional information
?
-
-
the wild type enzyme is active on hemimethylated and unmethylated DNA substrates
-
-
-
additional information
?
-
-
relative to GATC, three near-cognate substrates that carry a base-pair substitution at the first position are still methylated by the enzyme, although at rates reduced by 100fold (AATC) or 1000fold (CATC)
-
-
-
additional information
?
-
-
the enzyme recognizes and methylates GAGG (100% activity, Km 0.00522 mM), GGAG (about 48% activity, Km 0.017 mM) and GAAG (about 30% activity, Km 0.013 mM), but does not methylate GTGG, GmAmAG or GAGA
-
-
-
additional information
?
-
-
the enzyme recognizes and methylates GAGG (100% activity, Km 0.00522 mM), GGAG (about 48% activity, Km 0.017 mM) and GAAG (about 30% activity, Km 0.013 mM), but does not methylate GTGG, GmAmAG or GAGA
-
-
-
additional information
?
-
purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
MmeI does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
no detectable activity on the single-stranded form of the phage PhiX174 DNA is observed with M1.MboII, double-stranded DNA is less efficiently methylated than pUC18 DNA
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
Dam-dependent regulation of secretion of pathogenicity island 1 is transmitted via transcriptional regulator HilD
-
-
?
additional information
?
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Synechococcus sp. PCC 7002 PR-6
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
plastid transcription is largely insensitive to adenine methylation of the plastid DNA
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Bacillus sp. NEB686
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GANTC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GANTC, CcrM is more active on hemimethylated than unmethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q6NFX9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
D5FM16
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
D5FM16
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam belongs to the alpha-class of adenine methyltransferases and transfers a methyl group to the N-6 position of the adenine in the DNA sequence 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates a GATC recognition site
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates the adenine residue in GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
P0AEE9
Dam methylates the N-6 position of adenine in the DNA sequence 5'-GATC-3' and is highly processive, catalyzing multiple methyltransfers prior to dissociating from the DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates the N-6 position of the adenine in the sequence 5'-GATC-3', Dam shows a dramatic preference for the in vitro methylation of certain GATC sequences in plasmids and PCR-derived DNAfragments
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
DNA adenine methyltransferase methylates the N6 positions of adenines in the sequence 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
EcoP15I MTase adds a methyl group to the second adenine in the recognition sequence 5'-CAGCAG-3' in the presence of S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the wild type enzyme shows target specificity for GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A1U7P0
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B2MU09
MmeI modifies only the adenine in the top strand, 5’-TCCRAC-3’, MmeI endonuclease activity is blocked by this top strand adenine methylation and is unaffected by methylation of the adenine in the complementary strand, 5’-GTYGGA-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A7HWD2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q5LS45
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam catalyzes postreplicative methylation of adenosine moieties located in 5'-GATC-3' sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q30TC2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Synechococcus sp. PCC 7002 PR-6
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
recognition sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is involved in cell cycle regulation of Caulobacter crescentus
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
P04392
methylation of DNA-adenine at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as in bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific target sequence is GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
unmethylated or hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a critical regulator of bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of the site GATCprox proximal to the promotor is required for transition to the phase On state by specifically blocking PapI-dependent binding of Lrp to promotor proximal sites 4-6, expression of pyelonephritis-associated pili, i.e. Pap, in uropathogenic Escherichia coli is epigenetically controlled by a reversible OFF to ON switch, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is cell cycle regulated and essential for viability
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme recognizes 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is not important in mismatch repair and for adherence of the bacterium to host cells, e.g. HEp-2 cells
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a member of a restriction-modification system, R-M system, plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
E4T573
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
E4T573
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
P14751
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
A5F520
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
A5F520
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme methylates GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
-
-
-
?
additional information
?
-
-
the enzyme is part of the type II restriction-modification system AhdI, overview
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Bacillus sp. NEB686
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q6NFX9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
S-adenosyl-L-methionine plays a crucial role in reorientation of the enzyme in DNA with mutationally altered Ade residues to 2-aminopurine, overview
-
-
-
additional information
?
-
-
the preferred substrate consists of the annealed product of oligonucleotides 5'-CATTTACTTGATCCGGTATGC-3' and 5'-GCATACCGGATCAAGTAAATG-3', while the nonpreferred substrate consists of the annealed product of oligonucleotides 5'-CATTTAGACGATCTTTTATGC-3' and 5'-GCATAAAAGATCGTCTAAATG-3'
-
-
-
additional information
?
-
-
the wild type Dam shows no detectable activity at GATT sites
-
-
-
additional information
?
-
-
the wild type enzyme is active on hemimethylated and unmethylated DNA substrates
-
-
-
additional information
?
-
Q9Y5N5
purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
-
-
-
additional information
?
-
A1U7P0
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
B2MU09
MmeI does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
no detectable activity on the single-stranded form of the phage PhiX174 DNA is observed with M1.MboII, double-stranded DNA is less efficiently methylated than pUC18 DNA
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q1QGU9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q1QGU9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A7HWD2
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP8
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP8
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A5WI42
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A5WI42
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q134M6
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q134M6
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
B6IW55
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
B6IW55
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q5LS45
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
Dam-dependent regulation of secretion of pathogenicity island 1 is transmitted via transcriptional regulator HilD
-
-
?
additional information
?
-
Q30TC2
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Synechococcus sp. PCC 7002 PR-6
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
plastid transcription is largely insensitive to adenine methylation of the plastid DNA
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
-
Ca2+, Zn2+, and Ni2+ ions do not affect the methylation activity of the enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20mer fully methylated DNA duplex
-
product inhibition, noncompetitive against both S-adenosyl-L-methionine and 20mer unmethylated DNA duplex
-
diethyl dicarbonate
-
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 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-methionine
-
methylation reaction is inhibited above 0.0015 mM of S-adenosyl-L-methionine
methylated DNA
-
mixed-type inhibition against S-adenosyl-L-methionine, uncompetitive against unmethylated DNA
-
Mg2+
-
enzyme activity decreases in the presence of Mg2+ concentrations above 2.5 mM
S-adenosyl-L-homocysteine
-
product inhibition, competitive against S-adenosyl-L-methionine, noncompetitive to 20mer unmethylated DNA duplex
S-adenosyl-L-homocysteine
-
competitive against S-adenosyl-L-methionine, uncompetitive against DNA
S-adenosyl-L-homocysteine
-
competitive inhibition against S-adenosyl-L-methionine, noncompetitive against DNA
sinefungin
-
i.e. adenosyl ornithine, interaction mechanism with the enzyme, binding site structure, stabilization of the flipped adenine in presence of the inhibitor
additional information
-
no substrate inhibition even at high concentrations, no formation of dead-end complexes
-
additional information
-
enzyme is inhibited at ionic strength greater than 0.2 M
-
additional information
-
inhibited at ionic strength greater than 0.2 M
-
additional information
-
reduction of methylation rate at high concentrations of the substrate 20-mer DNA duplex
-
additional information
-
imidazole (5 mM) and ethanol (0.02% v/v) do not show any effect on enzyme
-
additional information
-
5'-allylthio-5'-deoxy-9-(1'-beta-D-ribofuranosyl)6-nitrodideazaadenine, 5'-chloro-5'-deoxyadenosine, 9-(1'-beta-D-ribofuranosyl)6-nitro-1,3-dideazaadenine, 5'-S-(propionamide)5'-deoxy-9-(1'-beta-D-ribofuranosyl)-adenine, 5'-S-(ethylpropionate)5'-deoxy-9-(1'-beta-D-ribofuranosyl)adenine, 5'-S-5'-methylthio deoxyadenosine, 5'-S-propargylthio adenosine, 5'-S-allenylthio adenosine, and 5'-S-propynylthioadenosine have no effect on M.EcoP15I activity
-
additional information
-
leucine-responsive regulatory protein specifically inhibits Dam methylation of GATC proximal to the pilus genes when pre-assembled onto a pap half-site substrate and when competing kinetically with Dam for access to this site, leucine-responsive regulatory protein does not efficiently inhibit Dam methylation of non-regulatory GATC sites in plasmid DNA, leucine-responsive regulatory protein inhibits Dam methylation of GATC proximal to the pilus genes in a pap substrate where GATC distal to the pilus genes is hemimethylated
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-S-(propionic acid)5'-deoxy-9-(1'-beta-D-ribofuranosyl)1,3-dideazaadenine
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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 55°C
-
0.000007
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', mutant enzyme R116A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000008
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', mutant enzyme R95A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.00001
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', mutant enzyme N132A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.0000227
DNA adenine
-
using the DNA sequence 5'-GCATACCCGATCAAGTAAATG-3', wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000023
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000027
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', mutant enzyme K139A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000031
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', mutant enzyme N126A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000035
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', mutant enzyme R116A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000044
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', mutant enzyme K139A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000076
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', mutant enzyme N132A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.0000809
DNA adenine
-
using the DNA sequence 5'-GCATAAAAGATCGTCTAAATG-3', wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000081
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000083
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', mutant enzyme R137A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.000086
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', mutant enzyme R95A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.00022
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', mutant enzyme R137A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.0003
DNA adenine
-
in 50 mM NaCl, 50 mM HEPES, 1 mM EDTA, pH 7.5, temperature not specified in the publication
0.0199
DNA adenine
-
in 10 mM Tris/HCl, pH 8.0, 5 mM 2-mercaptoethanol, at 37°C
0.0058
S-adenosyl-L-methionine
-
in 33 mM Tris-acetate, pH 7.9, 10 mM magnesium acetate, 66 mM potassium acetate, 1 mM dithiothreitol, at 55°C
0.012
S-adenosyl-L-methionine
-
in 50 mM NaCl, 50 mM HEPES, 1 mM EDTA, pH 7.5, temperature not specified in the publication
0.0000000011
T4 gt- dam- DNA
-
nonglucosylated unmethylated T4 gt- dam- DNA
-
0.0000000011
T4 gt- dam- DNA
-
nonglucosylated unmethylated T4 gt- dam- DNA
-
0.0000000011
T4 gt- dam- DNA
-
nonglucosylated unmethylated T4 gt- dam- DNA
-
additional information
additional information
-
Km-values for oligonucleotide substrates containing the native or modified recognition site: 5.3-12.9 nM
-
additional information
additional information
-
turnover numbers for the canonical 14-mer duplex and various substituted duplexes
-
additional information
additional information
-
the T4 Dam methylation reaction cannot be explained by a simple Michaelian scheme
-
additional information
additional information
-
Km-values fpr 14-mers and various substituted duplexes
-
additional information
additional information
-
detailed kinetics, enzyme shows a simple kinetic behaviour towards a 20mer duplex DNA, random bi bi mechanism
-
additional information
additional information
-
steady-state and pre-steady-state kinetics, single turnover methylation kinetics
-
additional information
additional information
-
detailed steady-state and pre-steady-state kinetics for different methylation sites
-
additional information
additional information
-
kinetics, ordered bi bi kinetic mechanism, cooperative binding of 2 molecules of enzyme per DNA is required for activity
-
additional information
additional information
-
steady-state kinetics, kinetic mechanism, thermodynamics
-
additional information
additional information
-
quantitative stopped-flow kinetics using 2-aminopurine as a probe to detect base flipping, wild-type and mutant enzymes
-
additional information
additional information
-
pre-steady-state and steady-state kinetics, reaction kinetics with diverse DNA duplex substrates, role of individual elements of the recognition site, kinetic reaction scheme assuming that the enzyme is isomerized into a catalytically active form, overview
-
additional information
additional information
-
detailed kinetics for diverse substrate duplexes and methylation sites
-
additional information
additional information
-
detailed kinetics for diverse substrate duplexes and methylation sites
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
T7 DNA adenine
-
in 33 mM Tris-acetate, pH 7.9, 10 mM magnesium acetate, 66 mM potassium acetate, 1 mM dithiothreitol, at 55°C
-
0.0011
DNA
-
substrate unmethylated duplex DNA, recombinant enzyme, pH 8.0, 37°C
0.0056
DNA
-
substrate hemimethylated duplex DNA, recombinant enzyme, pH 8.0, 37°C
0.00017
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', mutant enzyme N132A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.00082
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', mutant enzyme R95A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.0009
DNA adenine
using the non-preferred sequence 5'-GCATAAAAGATCGTCTAAATG-3', mutant enzyme R116A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.0015
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', mutant enzyme N126A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.003
DNA adenine
-
in 100 mM Tris (pH 8.0), 1 mM EDTA, 1 mM dithiothreitol, and 0.2 mg/ml bovine serum albumin, at 22°C
0.0038
DNA adenine
-
using the DNA sequence 5'-GCATACCCGATCAAGTAAATG-3', wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C
0.0038
DNA adenine
using the preferred sequence 5'-GCATACCGGATCAAGTAAATG-3', wild type enzyme, in 20 mM potas