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Information on EC 2.1.1.72 - site-specific DNA-methyltransferase (adenine-specific)
for references in articles please use BRENDA:EC2.1.1.72
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.72 site-specific DNA-methyltransferase (adenine-specific)
IUBMB Comments
This is a large group of enzymes, most of which form so-called ’restriction-modification systems’ with nucleases that possess similar site specificity [the nucleases are listed as either EC 3.1.21.3 (type 1 site-specific deoxyribonuclease), EC 3.1.21.4 (type II site-specific deoxyribonuclease) or EC 3.1.21.5 (type III site-specific deoxyribonuclease)]. A complete listing of all of these enzymes has been produced by R.J. Roberts and is available on-line at http://rebase.neb.com/rebase/rebase.html.
The enzyme appears in viruses and cellular organisms
- 2.1.1.72
- mtases
- n6-methyladenosine
- endonuclease
- chromatin
- duplex
- s-adenosyl-l-methionine
- cytosine
- adomet
- bacteriophage
- mismatch
-
damid
-
unmethylated
-
hemimethylated
-
restriction-modification
- flip
-
protein-dna
-
methylation-sensitive
- s-adenosyl-l-homocysteine
- 2-aminopurine
-
methyltransferase-like
-
epitranscriptomic
-
writer
- m.hhai
-
merip-seq
-
mettl3-mediated
- alkbh5
- crescentus
- medicine
- prophage
-
m6a-dependent
-
adohcy
-
m6a-modified
-
gatatc
-
n6-adenosine
- sinefungin
-
n6-methylation
-
extrahelical
-
methyl-directed
- aquaticus
- analysis
- pharmacology
Reaction Schemes
show+
adenine in DNA
=
+
N6-methyladenine in DNA
Synonyms
dam mtase, dna adenine methyltransferase, m6a methyltransferase, dam methylase, dna adenine methylase, m.taqi, t4 dam, m.ecorv, specific methyltransferase, ecodam, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A1S_0222
AamA
acinetobacter adenine methyltransferase A
adenine methyltransferase 1
adenine methyltransferase A
adenine-(N6)-DNA methyltransferase
adenine-N6 MTAse
-
-
-
-
AMT1
ApyPI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
AquII
AquIII
AquIV
BsbI
CamA
CcrM
CdpI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
cell cycle-regulated methyltransferase
Clostridioides difficile-specific DNA adenine MTase
CstMI
Dam
Dam DNA-(adenine-N6)-methyltransferase
Dam methylase
DNA 6mA methyltransferase
DNA 6mA MTase
DNA adenine methylase
DNA adenine methyltransferase
DNA adenine MTase
DNA adenine N6-methyltransferase
DNA methyltransferase
DNA MTase
DNA N6-adenine methyltransferase
DNA [amino]-methyltransferase
DNA-(adenine N6)-methyltransferase
DNA-(adenine-N6)-methyltransferase
DNA-[adenine] methyltransferase
DNA-[adenine] MTase
DNA-[N6-adenine] MTase
DNA-[N6-adenine]-methyltransferase
-
-
-
-
DNAm6A MTase
DraRI
DrdIV
EcoDam
EcoVIII
Hia5 protein
Hin1523 protein
HpyAXII
isospecific adenine DNA methyltransferase
isospecific DNA MTase
M.AbaBGORF222P
M.AluBI
M.BstZ1II
M.Csp231I
M.EcoVIII
M.HindIII
M.HpyAXII
M.LlaCI
M.NgoAXP
M.PtoI
M.RsrI
M.TaqI
M1.HpyAVI
M2.BstSEI
m6A methyltransferase
MaqI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
MmeI
modification methylase
-
-
-
-
MTA1
MTA1c
MTase
N6 adenine MTase
N6-adenine DNA -methyltransferase
-
-
-
-
N6-adenine methyltransferase
N6-adenine MTase
N6AMT1
NgoAXPMod subunit
NhaXI
NlaCI
Nme1821 protein
NmeAIII
PlaDI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
PspOMII
PspPRI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
RceI
restriction-modification system
-
-
-
-
RpaB5I
RsrI N6-adenine DNA methyltransferase
SdeAI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
specific methyltransferase
SpoDI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
T4 Dam
T4Dam
UP3_c0262
[N6-adenine] MTase
additional information
AquII
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
AquII
Picosynechococcus sp. PCC 7002 PR-6
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
AquIII
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
AquIII
Picosynechococcus sp. PCC 7002 PR-6
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
AquIV
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
AquIV
Picosynechococcus sp. PCC 7002 PR-6
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
BsbI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
BsbI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
CstMI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
CstMI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
Dam
-
-
DNA adenine methyltransferase
-
-
DraRI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
DraRI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
DrdIV
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
DrdIV
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
HpyAXII
-
consists of a restriction endonuclease and a DNA methyltransferase
HpyAXII
-
consists of a restriction endonuclease and a DNA methyltransferase
-
MmeI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
MmeI
has both endonuclease and DNA methyltransferase activities
NhaXI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
NhaXI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
NlaCI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
NlaCI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
NmeAIII
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
NmeAIII
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
PspOMII
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
PspOMII
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
RceI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
RceI
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
RpaB5I
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
RpaB5I
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
additional information
-
this is a large group of enzymes most of which, with enzymes of similar site specificity listed as EC 3.1.21.3, 4 or 5, form so-called "restriction-modification systems". A complete listing of all these enzymes has been produced by R.J. Roberts, this list is updated annually
additional information
the enzyme belongs to the m6N-adenine beta-class MTases
additional information
the enzyme belongs to the m6N-adenine beta-class MTases
-
additional information
the enzyme belongs to the m6N-adenine beta-class MTases
additional information
the enzyme belongs to the m6N-adenine beta-class MTases
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
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
-
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
-
-
-
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
molecular mechanism, effector action of substrates, progressive methylation of extended DNA containing more than one methylation site
-
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
D181 and Y184 are essential for activity
-
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
ordered bi bi mechanism with S-adenosyl-L-methionine binding first, fast methyl transfer, slow product release
-
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
active site structure, enzyme-methyl donor product interactions, substrate binding mechanism and conformational changes, overview
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
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
-
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
ordered bi bi mechanism during progressive methylation process
-
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
two distinct stages of methylation under single turnover conditions
-
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N6-methyladenine in DNA
reaction scheme and random bi bi kinetic mechanism
-
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + (CGG*CCG)73 oligodeoxynucleotide duplexes 5'-GATC/5'-GATC
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + DNA containing N6-methyladenine
-
Substrates: the enzyme specifically binds double-stranded DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
S-adenosyl-L-methionine + adenine in T4 gt- dam- DNA
S-adenosyl-L-homocysteine + N6-methyladenine in T4 gt- dam- DNA
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
S-adenosyl-L-methionine + GGATCC
S-adenosyl-L-homocysteine + GG(6mA)TCC
A0A7R7A6G8
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + Int1 DNA
S-adenosyl-L-homocysteine + Int1 DNA containing N6-methyladenine
S-adenosyl-L-methionine + mRNA
S-adenosyl-L-homocysteine + mRNA containing N6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + oligodeoxynucleotide duplexes
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: substrate contains one single specific recognition site as 5'-GATC/5'-GATC, or modified variants
Products: -
Products: -
?
S-adenosyl-L-methionine + pUC19 DNA adenine
S-adenosyl-L-homocysteine + pUC19 DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + RGATCY
S-adenosyl-L-homocysteine + RG(6mA)TCY
A0A7R7A6G8
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
?
S-adenosyl-L-methionine + single stranded DNA adenine
S-adenosyl-L-homocysteine + single stranded DNA 6-methyladenine
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
Substrates: CamA contains an N-terminal domain for catalyzing methyl transfer, and a C-terminal DNA recognition domain. Major and minor groove DNA contacts in the recognition site involve base-specific hydrogen bonds, van der Waals contacts and the Watson-Crick pairing of a rearranged A:T base pair
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
Substrates: CamA contains an N-terminal domain for catalyzing methyl transfer, and a C-terminal DNA recognition domain. Major and minor groove DNA contacts in the recognition site involve base-specific hydrogen bonds, van der Waals contacts and the Watson-Crick pairing of a rearranged A:T base pair
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
r
S-adenosyl-L-methionine + adenine in T4 gt- dam- DNA
S-adenosyl-L-homocysteine + N6-methyladenine in T4 gt- dam- DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in T4 gt- dam- DNA
S-adenosyl-L-homocysteine + N6-methyladenine in T4 gt- dam- DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the DNA target sequence is GANTC
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the DNA target sequence is GANTC, CcrM is more active on hemimethylated than unmethylated DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the target sequence is 5'GATC3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 129-mer DNA or pUC19 DNA are used as substrates
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: the enzyme methylates the adenine of hemimethylated GANTC after replication
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: DNA adenine methyltransferase methylates the N6 positions of adenines in the sequence 5'-GATC-3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the wild type enzyme shows target specificity for GATC sites
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: Dam methylates a GATC recognition site
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: Dam methylates the adenine residue in GATC sites
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the target sequence is 5'GATC3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the EcoRV DNA methyltransferase methylates the first adenine in the GATATC recognition sequence
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Escherichia coli E1585-68
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Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the Hin1523 protein causes the methylation of 29.6% of the adenines in lambda DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: 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
Haemophilus influenzae biotype aegyptius ATCC 11116
Substrates: 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
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the Hin1523 protein causes the methylation of 29.6% of the adenines in lambda DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: M.HpyAXII targets GTAC sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: duplex 2 DNA, 5'-GCAG-3' is the recognition site for the enzyme
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: HP0050 methyltransferase methylates one adenine at a time in the sequence 5'-GAAG-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the sequences of 5'-GAGG-3', 5'-GGAG-3' or 5'-GAAG-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the sequences of 5'-GAGG-3', 5'-GGAG-3' or 5'-GAAG-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: M.HpyAXII targets GTAC sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme complex is active on single-stranded and unpaired DNA in vitro and methylates GGACT in single-strand DNA and double-strand DNA-containing mismatches
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: 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'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Oxytricha trifallax JRB310
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Substrates: the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Picosynechococcus sp. PCC 7002 PR-6
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: Dam catalyzes postreplicative methylation of adenosine moieties located in 5'-GATC-3' sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the target sequence is 5'GATC3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: recognition sequence GATC
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
-
Substrates: 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
-
Substrates: the target sequence is 5'GATC3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme is involved in cell cycle regulation of Caulobacter crescentus
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: a biotinylated double stranded 23mer oligodeoxynucleotide with one hemimethylated GANTC site is used as substrate
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: substrate and product binding site structures
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: enzyme is a critical regulator of bacterial virulence
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme is cell cycle regulated and essential for viability
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: methylation of target sequence GATC
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: enzyme methylates the first adenine in the sequence ATGCAT
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: -
Products: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme recognizes 5'-GATC-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: nonglucosylated, hydroxymethylcytosine-containing T2gt- virion DNA has a higher level of methylation than T4gt virion DNA does
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: enzyme is not important in mismatch repair and for adherence of the bacterium to host cells, e.g. HEp-2 cells
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: enzyme is a member of a restriction-modification system, R-M system, plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme catalyzes the methylation of adenine at the N-6 position within its DNA recognition sequence GATC. Enzymatic methylation of the hemimethylated GATC site results in destabilisation of the duplex, increasing the proportion of dissociated DNA, and producing an observable increase in fluorescence. By using a suitable oligonucleotide substrate, labeled on adjacent strands with a fluorophore (fluorescein) and quencher (dabcyl), the destabilization of duplex DNA due to adenine methylation can be monitored by fluorescence measurements. The separation of fluorophore and quencher during strand dissociation causes an observable increase in fluorescence, providing a reproducible, direct, and real-time activity assay
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: synthetic oligonucleotide substrates containing the native recognition site GATC or its modified variants
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: interaction with substrates containing defective recognition sites. Deoxyguanosine residues in both strands of the modified GATC are indispensable for complex formation
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: nonglucosylated, hydroxymethylcytosine-containing T2gt- virion DNA has a higher level of methylation than T4gt virion DNA does
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: hemimethylated DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: specific target sequence is GATC
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: methylation of DNA-adenine at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as in bacterial virulence
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: unmethylated or hemimethylated DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: binding site is the GATC sequence, the adenine is located in the palindromic recognition site GATC, substrate binding mechanism
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: specific methylation of target sequence GATC
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: specific methylation of oligonucleotide duplexes containing one or two target sequence GATC sites
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: unmethylated or hemimethylated DNA, 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
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: GGGTGATCAGGG
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: CCCTGATCACCC
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: 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
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: GCGTGATCACGC
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: GGGTGATCAGGG+CCCTGATCACCC, annealed
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: lambda phage DNA
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme is responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: -
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme modifies the third adenine within the recognition sequence 5-ATTAAT-3'
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: the enzyme methylates GATC sequences
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
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Substrates: -
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S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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Substrates: 100% activity
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S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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Escherichia coli E1585-68
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Substrates: 100% activity
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S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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-
Substrates: 100% activity
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S-adenosyl-L-methionine + DNA duplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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Substrates: 100% activity
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S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
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Substrates: -
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S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
Escherichia coli E1585-68
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Substrates: -
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S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
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Substrates: -
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S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
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Substrates: -
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S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
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Substrates: -
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S-adenosyl-L-methionine + double stranded DNA adenine
S-adenosyl-L-homocysteine + double stranded DNA 6-methyladenine
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Substrates: -
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S-adenosyl-L-methionine + Int1 DNA
S-adenosyl-L-homocysteine + Int1 DNA containing N6-methyladenine
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Substrates: adenine methylation occurs at a GAATTC site
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S-adenosyl-L-methionine + Int1 DNA
S-adenosyl-L-homocysteine + Int1 DNA containing N6-methyladenine
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Substrates: adenine methylation occurs at a GAATTC site
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S-adenosyl-L-methionine + lambda phage DNA
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Substrates: the enzyme modifies the adenine residue with formation of 5'-(m6A)GCT-3'
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S-adenosyl-L-methionine + lambda phage DNA
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Substrates: the enzyme modifies the adenine residue with formation of 5'-(m6A)GCT-3'
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S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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Substrates: low activity. Only the DNA strand of the RNA/DNA heteroduplex is methylated
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S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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Escherichia coli E1585-68
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Substrates: low activity. Only the DNA strand of the RNA/DNA heteroduplex is methylated
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S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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Substrates: low activity. Only the DNA strand of the RNA/DNA heteroduplex is methylated
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S-adenosyl-L-methionine + RNA/DNA heteroduplex carrying the 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence
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Substrates: low activity. Only the DNA strand of the RNA/DNA heteroduplex is methylated
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S-adenosyl-L-methionine + single stranded DNA adenine
S-adenosyl-L-homocysteine + single stranded DNA 6-methyladenine
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Substrates: the level of single stranded DNA methylation is 7fold lower than double stranded DNA. However, upon star activity conditions (30% DMSO), the efficiency of single stranded DNA modification is raised by up to 50% of the relative activity
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S-adenosyl-L-methionine + single stranded DNA adenine
S-adenosyl-L-homocysteine + single stranded DNA 6-methyladenine
Escherichia coli E1585-68
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Substrates: the level of single stranded DNA methylation is 7fold lower than double stranded DNA. However, upon star activity conditions (30% DMSO), the efficiency of single stranded DNA modification is raised by up to 50% of the relative activity
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S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
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Substrates: -
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S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
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Substrates: -
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S-adenosyl-L-methionine + T7 phage DNA
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Substrates: the enzyme modifies the adenine residue with formation of 5'-(m6A)GCT-3'
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S-adenosyl-L-methionine + T7 phage DNA
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Substrates: the enzyme modifies the adenine residue with formation of 5'-(m6A)GCT-3'
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additional information
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Substrates: the enzyme is part of the type II restriction-modification system AhdI, overview
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additional information
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Substrates: 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
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: 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
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additional information
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Substrates: the enzyme methylates GANTC sequences but does not specifically bind to DNA containing GANTC sequences
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additional information
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Substrates: the enzyme methylates adenine residues in 5'-GANTC-3' sequences
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additional information
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Substrates: the enzyme does not specifically bind to DNA containing GANTC sequences
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
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Substrates: substrate specificity with different oligonucleotides, substrate binding specificity, overview
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: the wild type Dam shows no detectable activity at GATT sites
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additional information
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Substrates: 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'
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additional information
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Substrates: the wild type enzyme is active on hemimethylated and unmethylated DNA substrates
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additional information
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Substrates: 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)
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additional information
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Substrates: 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)
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additional information
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Substrates: the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3')
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additional information
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Substrates: the DNA substrate preference for M.EcoVIII is: hemimethylated AAGCTT > AAGCTT > GAGCTT >/= CAGCTT > AATCTT > ATGCTT > ACGCTT > TAGCTT > AACCTT = single stranded AAGCTT > AGGCTT = AAACTT
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additional information
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Escherichia coli E1585-68
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Substrates: the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3')
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additional information
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Escherichia coli E1585-68
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Substrates: the DNA substrate preference for M.EcoVIII is: hemimethylated AAGCTT > AAGCTT > GAGCTT >/= CAGCTT > AATCTT > ATGCTT > ACGCTT > TAGCTT > AACCTT = single stranded AAGCTT > AGGCTT = AAACTT
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additional information
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Substrates: the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3') and single stranded DNA adenine
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additional information
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Substrates: the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3') and single stranded DNA adenine
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additional information
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Substrates: 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
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additional information
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Substrates: purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
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additional information
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Substrates: purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
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additional information
?
-
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Substrates: the enzyme complex shows strong activity on single-stranded oligo 6 T (containing GGACT), much reduced activities on 4 T (containing GGAGT) and 4B (AGACT), and no activity on oligos having two substitutions within the recognition, e.g. 6B (AGAGT) or 5 T and 5B (GGATC). Furthermore, the enzyme complex has no activity on an oligo-containing G and C only and no activity on A-containing oligos without matching consensus sequence. The enzyme complex acts on single-stranded DNA (6 T) faster than that on the corresponding single-stranded RNA and is inactive on double-stranded DNA or RNA/DNA hybrid
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additional information
?
-
-
Substrates: the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3') and single stranded DNA adenine
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additional information
?
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Substrates: the enzyme is not able to methylate nucleotide sequence containing two mismatches (5'-CAGCTG-3') and single stranded DNA adenine
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?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
Substrates: MmeI does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
-
Substrates: 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
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?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
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?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
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?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
Picosynechococcus sp. PCC 7002 PR-6
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
additional information
?
-
-
Substrates: Dam-dependent regulation of secretion of pathogenicity island 1 is transmitted via transcriptional regulator HilD
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?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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additional information
?
-
-
Substrates: plastid transcription is largely insensitive to adenine methylation of the plastid DNA
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additional information
?
-
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Substrates: S-adenosyl-L-methionine plays a crucial role in reorientation of the enzyme in DNA with mutationally altered Ade residues to 2-aminopurine, overview
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additional information
?
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-
Substrates: DNA substrate specificities of wild-type and mutant enzymes
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additional information
?
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Substrates: enzyme binds also nonspecific to DNA, linear diffusion along the DNA, overview
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additional information
?
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Substrates: enzyme and S-adenosyl-L-methionine form a catalytically active complex
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additional information
?
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-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + DNA containing N6-methyladenine
-
Substrates: the enzyme specifically binds double-stranded DNA
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?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
S-adenosyl-L-methionine + mRNA
S-adenosyl-L-homocysteine + mRNA containing N6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine in DNA
S-adenosyl-L-homocysteine + N6-methyladenine in DNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
-
Substrates: 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
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the DNA target sequence is GANTC
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
-
Substrates: the target sequence is 5'GATC3'
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: the enzyme methylates the adenine of hemimethylated GANTC after replication
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: 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
Substrates: 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
-
Substrates: 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
Products: -
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
-
Substrates: 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
Substrates: 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
Substrates: 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
Products: -
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
-
Substrates: Dam methylates a GATC recognition site
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Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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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Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: Dam methylates the adenine residue in GATC sites
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Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the target sequence is 5'GATC3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
Products: -
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?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Escherichia coli E1585-68
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: M.HpyAXII targets GTAC sites
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the sequences of 5'-GAGG-3', 5'-GGAG-3' or 5'-GAAG-3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the sequences of 5'-GAGG-3', 5'-GGAG-3' or 5'-GAAG-3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: M.HpyAXII targets GTAC sites
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme recognizes the palindromic specific sequence 5'-AAGCTT-3' and catalyzes formation of N6-methyladenine at the first A-residue. The enzyme prefers DNA containing a hemimethylated target site
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: 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'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Oxytricha trifallax JRB310
-
Substrates: the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Picosynechococcus sp. PCC 7002 PR-6
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: Dam catalyzes postreplicative methylation of adenosine moieties located in 5'-GATC-3' sites
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the target sequence is 5'GATC3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: recognition sequence GATC
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the enzyme consists of two MT-A70 proteins and two homeobox-like DNA-binding proteins and specifically methylates ApT dinucleotides in double stranded DNA. The enzyme activity is 3-3.5fold higher on hemimethylated substrates, relative to unmethylated double stranded DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Substrates: the target sequence is 5'GATC3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme is involved in cell cycle regulation of Caulobacter crescentus
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: enzyme is a critical regulator of bacterial virulence
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme is cell cycle regulated and essential for viability
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme recognizes 5'-GATC-3'
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: enzyme is not important in mismatch repair and for adherence of the bacterium to host cells, e.g. HEp-2 cells
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: enzyme is a member of a restriction-modification system, R-M system, plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: hemimethylated DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: specific target sequence is GATC
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: methylation of DNA-adenine at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as in bacterial virulence
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: unmethylated or hemimethylated DNA
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme is responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: the enzyme methylates GATC sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is part of the type II restriction-modification system AhdI, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme methylates adenine residues in 5'-GANTC-3' sequences
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the wild type Dam shows no detectable activity at GATT sites
Products: -
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?
additional information
?
-
-
Substrates: 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'
Products: -
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?
additional information
?
-
Substrates: the wild type enzyme is active on hemimethylated and unmethylated DNA substrates
Products: -
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?
additional information
?
-
Substrates: purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
Products: -
Products: -
?
additional information
?
-
-
Substrates: purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
Products: -
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?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: MmeI does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Picosynechococcus sp. PCC 7002 PR-6
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
additional information
?
-
-
Substrates: Dam-dependent regulation of secretion of pathogenicity island 1 is transmitted via transcriptional regulator HilD
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
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?
additional information
?
-
-
Substrates: plastid transcription is largely insensitive to adenine methylation of the plastid DNA
Products: -
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?
additional information
?
-
-
Substrates: S-adenosyl-L-methionine plays a crucial role in reorientation of the enzyme in DNA with mutationally altered Ade residues to 2-aminopurine, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not produce any detectable N4-cytosine methylation
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
-
Ca2+, Zn2+, and Ni2+ ions do not affect the methylation activity of the enzyme
Mg2+
-
Mg2+ is necessary for the methylation reaction, concentrations of magnesium over 5-25 mM supported the reaction more or less equivalently
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S,3S,4R,5R)-3,4-dihydroxy-5-(6-[[(3-iodophenyl)methyl]amino]-9H-purin-9-yl)-N-methyloxolane-2-carboxamide
-
-
-
20mer fully methylated DNA duplex
-
product inhibition, noncompetitive against both S-adenosyl-L-methionine and 20mer unmethylated DNA duplex
-
5'-S-[2-[N'-(cyclohexylmethyl)carbamimidamido]ethyl]-N-(3-phenylpropyl)-5'-thioadenosine
-
-
5'-S-[3-[N'-(cyclohexylmethyl)carbamimidamido]propyl]-5'-thioadenosine
-
-
5'-S-[3-[N'-(cyclohexylmethyl)carbamimidamido]propyl]-N-(3-phenylpropyl)-5'-thioadenosine
-
-
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
weak binding of the methyl donor S-adenosyl-L-methionine (SAM) might provide avenues for inhibiting CamA activity using SAM analogs
-
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
-
additional information
-
enzyme is 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
-
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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
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Methyl-accepting RNA in 13762 mammary adenocarcinoma correlated with low adenine methyltransferase levels.
Adenocarcinoma
The m6A Methyltransferase METTL14-Mediated N6-Methyladenosine Modification of PTEN mRNA Inhibits Tumor Growth and Metastasis in Stomach Adenocarcinoma.
Adenocarcinoma of Lung
H3K4 Methylation Status and Lysine Specific Methyltransferase KMT2C Expression Correlate with Prognosis in Lung Adenocarcinoma.
Adenocarcinoma of Lung
m6A RNA Methylation Regulators Act as Potential Prognostic Biomarkers in Lung Adenocarcinoma.
Alzheimer Disease
Altered Expression of the m6A Methyltransferase METTL3 in Alzheimer's Disease.
Bacterial Infections
N6-Adenosine Methylation of Socs1 mRNA Is Required to Sustain the Negative Feedback Control of Macrophage Activation.
Breast Neoplasms
Identification of holocarboxylase synthetase chromatin binding sites in human mammary cell lines using the DNA adenine methyltransferase identification technology.
Breast Neoplasms
Ribosome 18S m6A Methyltransferase METTL5 Promotes Translation Initiation and Breast Cancer Cell Growth.
Breast Neoplasms
The m6A methyltransferase METTL3 controls epithelial-mesenchymal transition, migration and invasion of breast cancer through the MALAT1/miR-26b/HMGA2 axis.
Breast Neoplasms
The m6A methyltransferase METTL3 promotes the stemness and malignant progression of breast cancer by mediating m6A modification on SOX2.
Carcinogenesis
Epitranscriptomics in liver disease: Basic concepts and therapeutic potential.
Carcinogenesis
Methyltransferase-like 3-induced N6-methyladenosine upregulation promotes oral squamous cell carcinoma by through p38.
Carcinogenesis
N6-methyladenosine (m6A) methyltransferase WTAP accelerates the Warburg effect of gastric cancer through regulating HK2 stability.
Carcinoma
The M6A methyltransferase METTL3 promotes the development and progression of prostate carcinoma via mediating MYC methylation.
Carcinoma
The M6A methyltransferase METTL3: acting as a tumor suppressor in renal cell carcinoma.
Carcinoma, Hepatocellular
Circular RNA circDLC1 inhibits MMP1-mediated liver cancer progression via interaction with HuR.
Carcinoma, Non-Small-Cell Lung
The mechanism of m6A methyltransferase METTL3-mediated autophagy in reversing gefitinib resistance in NSCLC cells by ?-elemene.
Carcinoma, Ovarian Epithelial
METTL3 regulates m6A in endometrioid epithelial ovarian cancer independently of METTl14 and WTAP.
Carcinoma, Renal Cell
The M6A methyltransferase METTL3: acting as a tumor suppressor in renal cell carcinoma.
Colonic Neoplasms
m6A methyltransferase METTL3 maintains colon cancer tumorigenicity by suppressing SOCS2 to promote cell proliferation.
Colorectal Neoplasms
m6A methyltransferase METTL3 suppresses colorectal cancer proliferation and migration through p38/ERK pathways.
Colorectal Neoplasms
METTL3/YTHDF2 m6A axis accelerates colorectal carcinogenesis through epigenetically suppressing YPEL5.
Decompression Sickness
Fluorescence Study of DNA Binding and Bending by EcoRI DNA Methyltransferase.
Decompression Sickness
The M.EcoRV DNA-(adenine N6)-methyltransferase uses DNA bending for recognition of an expanded EcoDam recognition site.
Diabetes Mellitus
Transoesophageal echocardiographic findings in patients with ischemic lacunar and nonlacunar stroke.
Glioblastoma
N6-methyladenosine Modulates Nonsense-mediated mRNA Decay in Human Glioblastoma.
Hypertension
The m6A methyltransferase METTL3 promotes hypoxic pulmonary arterial hypertension.
Hypertension
Transoesophageal echocardiographic findings in patients with ischemic lacunar and nonlacunar stroke.
Infections
Characterization of a DNA Adenine Methyltransferase Gene of Borrelia hermsii and Its Dispensability for Murine Infection and Persistence.
Infections
Comparative studies of the phage T2 and T4 DNA (N6-adenine)methyltransferases: amino acid changes that affect catalytic activity.
Infections
DNA adenine methylase overproduction in Yersinia pseudotuberculosis alters YopE expression and secretion and host immune responses to infection.
Infections
Enterotoxigenic Escherichia coli infection promotes enteric defensin expression via FOXO6-METTL3-m6A-GPR161 signalling axis.
Infections
Escherichia coli bacteriophage T1 DNA methyltransferase appears to interact with Escherichia coli enolase.
Infections
In vivo-selected mutations in methyl-directed mismatch repair suppress the virulence attenuation of Salmonella dam mutant strains following intraperitoneal, but not oral, infection of naïve mice.
Infections
N6-methyladenosine RNA modification suppresses antiviral innate sensing pathways via reshaping double-stranded RNA.
Infections
Rate of translocation of bacteriophage T7 DNA across the membranes of Escherichia coli.
Infections
The Helicobacter pylori HpyAXII restriction-modification system limits exogenous DNA uptake by targeting GTAC sites but shows asymmetric conservation of the DNA methyltransferase and restriction endonuclease components.
Infections
Widespread remodeling of the m6A RNA-modification landscape by a viral regulator of RNA processing and export.
Leukemia
Widespread, exceptionally high levels of histone H3 lysine 4 trimethylation largely mediate "privileged" gene expression.
Lung Neoplasms
The m6A methyltransferase METTL3 contributes to Transforming Growth Factor-beta-induced epithelial-mesenchymal transition of lung cancer cells through the regulation of JUNB.
Lung Neoplasms
The mechanism of m6A methyltransferase METTL3-mediated autophagy in reversing gefitinib resistance in NSCLC cells by ?-elemene.
Lymphoma
m6A methyltransferase Wilms' tumor 1-associated protein facilitates cell proliferation and cisplatin resistance in NK/T cell lymphoma by regulating dual-specificity phosphatases 6 expression via m6A RNA methylation.
Melanoma
METTL3 induces PLX4032 resistance in melanoma by promoting m6A-dependent EGFR translation.
Nasopharyngeal Carcinoma
The m6A methyltransferase METTL3 aggravates the progression of nasopharyngeal carcinoma through inducing EMT by m6A-modified Snail mRNA.
Neoplasm Metastasis
Targeting Histone Methyltransferase DOT1L by a Novel Psammaplin A Analog Inhibits Growth and Metastasis of Triple-Negative Breast Cancer.
Neoplasm Metastasis
The m6A Methyltransferase METTL14-Mediated N6-Methyladenosine Modification of PTEN mRNA Inhibits Tumor Growth and Metastasis in Stomach Adenocarcinoma.
Neoplasm Metastasis
The m6A methyltransferase METTL3 controls epithelial-mesenchymal transition, migration and invasion of breast cancer through the MALAT1/miR-26b/HMGA2 axis.
Neoplasms
Associations between arsenic (+3 oxidation state) methyltransferase (AS3MT) and N-6 adenine-specific DNA methyltransferase 1 (N6AMT1) polymorphisms, arsenic metabolism, and cancer risk in a chilean population.
Neoplasms
Connecting METTL3 and intratumoural CD33+ MDSCs in predicting clinical outcome in cervical cancer.
Neoplasms
Methyl-accepting RNA in 13762 mammary adenocarcinoma correlated with low adenine methyltransferase levels.
Neoplasms
METTL3 promotes ovarian carcinoma growth and invasion through the regulation of AXL translation and epithelial to mesenchymal transition.
Neoplasms
Role of m6A methyltransferase component VIRMA in multiple human cancers (Review).
Neoplasms
The loss of RNA N6-adenosine methyltransferase Mettl14 in tumor-associated macrophages promotes CD8+ T cell dysfunction and tumor growth.
Neoplasms
The m6A Methyltransferase METTL14-Mediated N6-Methyladenosine Modification of PTEN mRNA Inhibits Tumor Growth and Metastasis in Stomach Adenocarcinoma.
Neoplasms
The m6A methyltransferase METTL3 controls epithelial-mesenchymal transition, migration and invasion of breast cancer through the MALAT1/miR-26b/HMGA2 axis.
Neoplasms
The M6A methyltransferase METTL3: acting as a tumor suppressor in renal cell carcinoma.
Osteoporosis
Mettl3-mediated m6A RNA methylation regulates the fate of bone marrow mesenchymal stem cells and osteoporosis.
Osteoporosis
Regulatory Role of RNA N6-Methyladenosine Modification in Bone Biology and Osteoporosis.
Osteosarcoma
The m6A methyltransferase METTL3 promotes osteosarcoma progression by regulating the m6A level of LEF1.
Ovarian Neoplasms
A newly defined risk signature, consisting of three m6A RNA methylation regulators, predicts the prognosis of ovarian cancer.
Pancreatic Neoplasms
m6A Methyltransferase METTL14-Mediated Upregulation of Cytidine Deaminase Promoting Gemcitabine Resistance in Pancreatic Cancer.
Prostatic Neoplasms
Genome-wide analysis of ETV1 targets: Insights into the role of ETV1 in tumor progression.
Prostatic Neoplasms
m6A methyltransferase METTL3 promotes the progression of prostate cancer via m6A-modified LEF1.
Prostatic Neoplasms
RNA m6A Methyltransferase METTL3 Promotes The Growth Of Prostate Cancer By Regulating Hedgehog Pathway.
Pulmonary Arterial Hypertension
The m6A methyltransferase METTL3 promotes hypoxic pulmonary arterial hypertension.
Relapsing Fever
Characterization of a DNA Adenine Methyltransferase Gene of Borrelia hermsii and Its Dispensability for Murine Infection and Persistence.
Retinoblastoma
m6A methyltransferase METTL3 promotes retinoblastoma progression via PI3K/AKT/mTOR pathway.
Salmonella Infections
Cross-protective immunity conferred by a DNA adenine methylase deficient Salmonella enterica serovar Typhimurium vaccine in calves challenged with Salmonella serovar Newport.
Salmonella Infections
Development of a Salmonella cross-protective vaccine for food animal production systems.
Seminoma
The m6A methyltransferase METTL3 regulates autophagy and sensitivity to cisplatin by targeting ATG5 in seminoma.
site-specific dna-methyltransferase (adenine-specific) deficiency
A role for the bacterial GATC methylome in antibiotic stress survival.
Stomach Neoplasms
Effect of histone modifications on hMLH1 alternative splicing in gastric cancer.
Stomach Neoplasms
Knockdown of m6A methyltransferase METTL3 in gastric cancer cells results in suppression of cell proliferation.
Stomach Neoplasms
m6A Methyltransferase 3 Promotes the Proliferation and Migration of Gastric Cancer Cells through the m6A Modification of YAP1.
Stomach Neoplasms
METTL16 promotes cell proliferation by up-regulating cyclin D1 expression in gastric cancer.
Stomach Neoplasms
N6-methyladenosine (m6A) methyltransferase WTAP accelerates the Warburg effect of gastric cancer through regulating HK2 stability.
Stomach Neoplasms
The m6A methyltransferase METTL14 inhibits the proliferation, migration, and invasion of gastric cancer by regulating the PI3K/AKT/mTOR signaling pathway.
Stroke, Lacunar
Transoesophageal echocardiographic findings in patients with ischemic lacunar and nonlacunar stroke.
Thyroid Neoplasms
Progression of Thyroid Carcinoma Is Promoted by the m6A Methyltransferase METTL3 Through Regulating m6A Methylation on TCF1.
Tuberculosis
DNA methylation impacts gene expression and ensures hypoxic survival of Mycobacterium tuberculosis.
Typhoid Fever
Cross-protective immunity conferred by a DNA adenine methylase deficient Salmonella enterica serovar Typhimurium vaccine in calves challenged with Salmonella serovar Newport.
Typhoid Fever
Innate interferon response in macrophage and epithelial cells infected with wild-type compared to DNA adenine methylase and flagellin mutant Salmonella enterica serovar Typhimurium.
Typhoid Fever
Salmonella DNA adenine methylase mutants elicit protective immune responses to homologous and heterologous serovars in chickens.
Typhoid Fever
Tissue selectivity of interferon-stimulated gene expression in mice infected with Dam(+) versus Dam(-) Salmonella enterica serovar Typhimurium strains.
Urinary Bladder Neoplasms
The m6A methyltransferase METTL3 promotes bladder cancer progression via AFF4/NF-?B/MYC signaling network.
Vesicular Stomatitis
N6-methyladenosine RNA modification suppresses antiviral innate sensing pathways via reshaping double-stranded RNA.
Wilms Tumor
m6A methyltransferase Wilms' tumor 1-associated protein facilitates cell proliferation and cisplatin resistance in NK/T cell lymphoma by regulating dual-specificity phosphatases 6 expression via m6A RNA methylation.
Wilms Tumor
Mammalian WTAP is a regulatory subunit of the RNA N6-methyladenosine methyltransferase.
Wilms Tumor
miR-550-1 functions as a tumor suppressor in acute myeloid leukemia via the hippo signaling pathway.
Wilms Tumor
N6-methyladenosine (m6A) methyltransferase WTAP accelerates the Warburg effect of gastric cancer through regulating HK2 stability.
Wilms Tumor
Wilms' tumour 1-associating protein inhibits endothelial cell angiogenesis by m6A-dependent epigenetic silencing of desmoplakin in brain arteriovenous malformation.
Wilms Tumor
WTAP promotes myocardial ischemia/reperfusion injury by increasing endoplasmic reticulum stress via regulating m6A modification of ATF4 mRNA.
Wolf-Hirschhorn Syndrome
Wolf-Hirschhorn Syndrome Candidate 1 (whsc1) Functions as a Tumor Suppressor by Governing Cell Differentiation.
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
0.0002576
single stranded DNA adenine
-
with specific sequence AAGCTT, at pH 7.0 and 37°C
-
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
-
0.0000000011
adenine in T4 gt- dam- DNA
-
nonglucosylated unmethylated T4 gt- dam- DNA
-
0.0000000011
adenine in T4 gt- dam- DNA
-
nonglucosylated unmethylated T4 gt- dam- DNA
-
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
0.0000244
double stranded DNA adenine
-
with specific sequence MAGCTT/TTCGAA, at pH 7.0 and 37°C
-
0.0000751
double stranded DNA adenine
-
with specific sequence AAGCTT/TTCGAA, at pH 7.0 and 37°C
-
0.0000782
double stranded DNA adenine
-
with specific sequence CAGCTT/GTCGAA, at pH 7.0 and 37°C
-
0.0000784
double stranded DNA adenine
-
with specific sequence GAGCTT/CTCGAA, at pH 7.0 and 37°C
-
0.0000855
double stranded DNA adenine
-
with specific sequence TAGCTT/ATGCAA, at pH 7.0 and 37°C
-
0.000089
double stranded DNA adenine
-
with specific sequence ACGCTT/TGCGAA, at pH 7.0 and 37°C
-
0.0000912
double stranded DNA adenine
-
with specific sequence AGGCTT/TCCGAA, at pH 7.0 and 37°C
-
0.0000914
double stranded DNA adenine
-
with specific sequence ATGCTT/TACGAA, at pH 7.0 and 37°C
-
0.0001023
double stranded DNA adenine
-
with specific sequence AAACTT/TTTGAA, at pH 7.0 and 37°C
-
0.0001273
double stranded DNA adenine
-
with specific sequence AACCTT/TTGGAA, at pH 7.0 and 37°C
-
0.000143
double stranded DNA adenine
-
with specific sequence AATCTT/TTAGAA, at pH 7.0 and 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
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
-
Km-values fpr 14-mers 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
-
turnover numbers for the canonical 14-mer duplex and various substituted duplexes
-
additional information
additional information
-
detailed kinetics for diverse substrate duplexes and methylation sites
-
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
-
quantitative stopped-flow kinetics using 2-aminopurine as a probe to detect base flipping, wild-type and mutant enzymes
-
additional information
additional information
-
steady-state kinetics, kinetic mechanism, thermodynamics
-
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
-
detailed steady-state and pre-steady-state kinetics for different methylation sites
-
additional information
additional information
-
steady-state and pre-steady-state kinetics, single turnover methylation kinetics
-
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
-
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
0.0005
single stranded DNA adenine
-
with specific sequence AAGCTT, at pH 7.0 and 37°C
-
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
-
0.00033
adenine in DNA
-
substrate plasmid DNA, recombinant enzyme, pH 8.0, 37°C
-
0.0011
adenine in DNA
-
substrate unmethylated duplex DNA, recombinant enzyme, pH 8.0, 37°C
-
0.0056
adenine in 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 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
0.0038
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
0.0055
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
0.008
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
0.0083
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
0.013
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
0.015
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
0.015
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
0.019
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
0.02
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
0.058
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
0.0002
double stranded DNA adenine
-
with specific sequence AGGCTT/TCCGAA, at pH 7.0 and 37°C
-
0.00022
double stranded DNA adenine
-
with specific sequence TAGCTT/ATGCAA, at pH 7.0 and 37°C
-
0.00022
double stranded DNA adenine
-
with specific sequence ACGCTT/TGCGAA, at pH 7.0 and 37°C
-
0.00025
double stranded DNA adenine
-
with specific sequence ATGCTT/TACGAA, at pH 7.0 and 37°C
-
0.00027
double stranded DNA adenine
-
with specific sequence AACCTT/TTGGAA, at pH 7.0 and 37°C
-
0.00033
double stranded DNA adenine
-
with specific sequence CAGCTT/GTCGAA, at pH 7.0 and 37°C
-
0.00033
double stranded DNA adenine
-
with specific sequence GAGCTT/CTCGAA, at pH 7.0 and 37°C
-
0.00033
double stranded DNA adenine
-
with specific sequence AAACTT/TTTGAA, at pH 7.0 and 37°C
-
0.00033
double stranded DNA adenine
-
with specific sequence AATCTT/TTAGAA, at pH 7.0 and 37°C
-
0.0015
double stranded DNA adenine
-
with specific sequence AAGCTT/TTCGAA, at pH 7.0 and 37°C
-
0.0021
double stranded DNA adenine
-
with specific sequence MAGCTT/TTCGAA, at pH 7.0 and 37°C
-
additional information
additional information
-
turnover-numbers of synthetic oligonucleotide substrates containing the native recognition site GATC or its modified variants
-
additional information
additional information
-
turnover numbers for the canonical 14-mer duplex and various substituted duplexes
-
additional information
additional information
-
residues at position 20 and 26 are responsible for the different turnover-number values of the two MTases bor both canonical and noncanonical sites
-
additional information
additional information
-
turnover-numbers of the canonical 12-mer and 20 mers and for various defective duplexes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.9
single stranded DNA adenine
-
with specific sequence AAGCTT, at pH 7.0 and 37°C
-
48.3
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
100
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
117
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
125
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
133
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
160
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
167
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
168
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
187
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
187
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
223
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
262
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
267
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
300
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
367
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
1.7
double stranded DNA adenine
-
with specific sequence AGGCTT/TCCGAA, at pH 7.0 and 37°C
-
1.7
double stranded DNA adenine
-
with specific sequence AAACTT/TTTGAA, at pH 7.0 and 37°C
-
1.9
double stranded DNA adenine
-
with specific sequence AACCTT/TTGGAA, at pH 7.0 and 37°C
-
2.2
double stranded DNA adenine
-
with specific sequence TAGCTT/ATGCAA, at pH 7.0 and 37°C
-
2.6
double stranded DNA adenine
-
with specific sequence ACGCTT/TGCGAA, at pH 7.0 and 37°C
-
2.7
double stranded DNA adenine
-
with specific sequence ATGCTT/TACGAA, at pH 7.0 and 37°C
-
2.9
double stranded DNA adenine
-
with specific sequence AATCTT/TTAGAA, at pH 7.0 and 37°C
-
4.2
double stranded DNA adenine
-
with specific sequence CAGCTT/GTCGAA, at pH 7.0 and 37°C
-
4.3
double stranded DNA adenine
-
with specific sequence GAGCTT/CTCGAA, at pH 7.0 and 37°C
-
19.6
double stranded DNA adenine
-
with specific sequence AAGCTT/TTCGAA, at pH 7.0 and 37°C
-
86.1
double stranded DNA adenine
-
with specific sequence MAGCTT/TTCGAA, at pH 7.0 and 37°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00062
S-adenosyl-L-homocysteine
-
versus S-adenosyl-L-methionine, pH 8.0, 37°C
additional information
additional information
-
detailed inhibition kinetics
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
(2S,3S,4R,5R)-3,4-dihydroxy-5-(6-[[(3-iodophenyl)methyl]amino]-9H-purin-9-yl)-N-methyloxolane-2-carboxamide
Clostridioides difficile
-
pH 7.5, 22°C
-
0.00015
5'-S-[2-[N'-(cyclohexylmethyl)carbamimidamido]ethyl]-N-(3-phenylpropyl)-5'-thioadenosine
Clostridioides difficile
pH 7.5, 22°C
-
0.0015
5'-S-[3-[N'-(cyclohexylmethyl)carbamimidamido]propyl]-5'-thioadenosine
Clostridioides difficile
pH 7.5, 22°C
-
0.00027
5'-S-[3-[N'-(cyclohexylmethyl)carbamimidamido]propyl]-N-(3-phenylpropyl)-5'-thioadenosine
Clostridioides difficile
pH 7.5, 22°C
-
0.00071
N-[2-[1-(tert-butoxycarbonyl)piperidin-4-yl]ethyl]adenosine
Clostridioides difficile
-
pH 7.5, 22°C
-
0.00039
N-[3-[1-(tert-butoxycarbonyl)piperidin-4-yl]propyl]adenosine
Clostridioides difficile
-
pH 7.5, 22°C
-
0.002
N-[[1-(tert-butoxycarbonyl)piperidin-4-yl]methyl]adenosine
Clostridioides difficile
-
pH 7.5, 22°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme catalyzes the methylation of adenine at the N-6 position within its DNA recognition sequence GATC. Enzymatic methylation of the hemimethylated GATC site results in destabilisation of the duplex, increasing the proportion of dissociated DNA, and producing an observable increase in fluorescence. By using a suitable oligonucleotide substrate, labeled on adjacent strands with a fluorophore (fluorescein) and quencher (dabcyl), the destabilization of duplex DNA due to adenine methylation can be monitored by fluorescence measurements. The separation of fluorophore and quencher during strand dissociation causes an observable increase in fluorescence, providing a reproducible, direct, and real-time activity assay
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
M.PtoI is able to methylate lambda DNA (producing m6A) at pH ranging from 4 to 7, with optimum activity being detected at pH 5
7.5
7.5 - 8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.8 - 9
-
pH 2.8: about 65% of maximal activity, pH 9.0: about 45% of maximal activity
4 - 7
-
M.PtoI is able to methylate lambda DNA (producing m6A) at pH ranging from 4 to 7, with optimum activity being detected at pH 5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
M.EcoRV, M.EcoRI, Escherichia coli dam methyltransferase and M.FokI enzyme
-
-
brenda
-
485566, 485567, 485568, 485569, 485570, 485573, 485574, 485576, 485577, 658407, 659268, 659301, 659905
-
-
brenda
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
-
-
brenda
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
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
growth temperature for strain 14P is 55°C
brenda
-
growth temperature for strain 14P is 55°C
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
physiological function
drug target
-
koenimbine, a natural bioactive chemical compound of Murraya koenigii and mahanine may be potential antibiotics for inhibiting Dam-containing bacterial pathogens
drug target
decreased N6amt1 caused by NR2F6 is required for neuropathic pain, likely through its regulation of m6A-controlled KCNJ16 in dorsal horn neurons, suggesting that DNA m6A modification may be a potential target for analgesic and treatment strategies
drug target
antivirulence drug development targeting CamA. Three S-adenosyl-L-homocysteine analogs (SGC0946, SGC8158 and JNJ-64619178) are identified which are already in (pre)clinical studies as inhibitors of human epigenetic enzymes, and show that they can also inhibit CamA enzymatic activity in vitro at low micromolar concentrations
drug target
-
antivirulence drug development targeting CamA. Three S-adenosyl-L-homocysteine analogs (SGC0946, SGC8158 and JNJ-64619178) are identified which are already in (pre)clinical studies as inhibitors of human epigenetic enzymes, and show that they can also inhibit CamA enzymatic activity in vitro at low micromolar concentrations
-
malfunction
-
lack of Dam methylation causes partial attenuation upon intranasal or intraperitoneal inoculation of mice
malfunction
-
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
-
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
-
mutants lacking Dam methylase are not viable, Dam overproduction does not impair bacterial growth
malfunction
-
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
-
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
-
enzyme gene disruption mutants fail to complete the sexual cycle when induced to mate and display complete lethality
malfunction
-
enzyme gene disruption mutants fail to complete the sexual cycle when induced to mate and display complete lethality
malfunction
-
enzyme loss-of-function leads to severe defects in growth and development
malfunction
-
enzyme deletion suppresses the trans-generational phenotypes of spr-5 mutant worms
malfunction
-
deletion and overexpression of Dam has a similar effect on inducing the macrophage death and secretion of inflammatory cytokines. Both C50336DELTAdam and C50336::dam are defective in inhibiting the expression of several anti-inflammasome factors (such as Braf, Cul1, Xiap, Pten, and Sirt1) compared to wild-type. In addition, both the absence and overexpression of Dam blocks the activation of c-Jun N-terminal kinase pathway during Salmonella enteritidis infection
malfunction
-
deficiency in Dam leads to a differential expression of over 1000 genes in RM13514. Dam regulated genes are involved in diverse functions. Dam regulates a large number of genes located on prophages, pathogenicity islands, and plasmids, including Shiga toxin genes, type III secretion system (TTSS) genes, and enterohemolysin genes. Production of Stx2 in dam mutant is significantly higher than in RM13514, supporting a role of Dam in maintaining lysogeny of Stx2-prophage
malfunction
downregulation of dorsal horn N6amt1 contributes to the development and maintenance of nerve injury-induced nociceptive hypersensitivity by upregulating expression of the inwardly rectifying potassium channel Kir5.1 (encoded by the Kcnj16 gene) through DNA m6A methylation in the Kcnj16 promoter
malfunction
-
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
-
enzyme gene disruption mutants fail to complete the sexual cycle when induced to mate and display complete lethality
-
malfunction
-
enzyme loss-of-function leads to severe defects in growth and development
-
malfunction
Oxytricha trifallax JRB310
-
enzyme gene disruption mutants fail to complete the sexual cycle when induced to mate and display complete lethality
-
malfunction
-
deletion and overexpression of Dam has a similar effect on inducing the macrophage death and secretion of inflammatory cytokines. Both C50336DELTAdam and C50336::dam are defective in inhibiting the expression of several anti-inflammasome factors (such as Braf, Cul1, Xiap, Pten, and Sirt1) compared to wild-type. In addition, both the absence and overexpression of Dam blocks the activation of c-Jun N-terminal kinase pathway during Salmonella enteritidis infection
-
malfunction
Escherichia coli RM13514
-
deficiency in Dam leads to a differential expression of over 1000 genes in RM13514. Dam regulated genes are involved in diverse functions. Dam regulates a large number of genes located on prophages, pathogenicity islands, and plasmids, including Shiga toxin genes, type III secretion system (TTSS) genes, and enterohemolysin genes. Production of Stx2 in dam mutant is significantly higher than in RM13514, supporting a role of Dam in maintaining lysogeny of Stx2-prophage
-
metabolism
the enzyme potentially participates in arsenic metabolism in vivo
metabolism
the enzyme, in addition to being responsible for GATC methylation, can also function as a methylation-independent transcriptional repressor
metabolism
-
the enzyme plays a critical role in the regulation of cellular processes within many bacterial species, including mismatch repair and the timing of DNA replication
physiological function
-
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
-
CcrM regulates the genes dnaA, ctrA, and ccrM at transcriptional level
physiological function
-
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
-
Dam methylation may control the expression of virulence genes
physiological function
-
DNA adenine methylation is involved in Aeromonas hydrophila pathogenesis
physiological function
-
DNA adenine methylation is involved in Aeromonas hydrophila pathogenesis
physiological function
-
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
-
transcriptional regulation of std expression by Dam methylation
physiological function
-
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
-
DNA adenine methyltransferase is essential for proper DNA replication timing, gene regulation, and mismatch repair
physiological function
MmeI DNA methylation prevents cleavage by MmeI
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
-
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
-
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
-
transcriptional inhibition by hemimethylation of genes dnaA, ccrM, and ctrA
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
-
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
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
the enzyme is essential for cell viability and confers potent cross-protective efficacy as well as decreased virulence and spontaneous mutation frequency
physiological function
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
physiological function
-
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
-
the enzyme is required for the bulk of 6-methyladenine and all symmetric methylation at the ApT dinucleotides
physiological function
-
the enzyme plays a major role during Photorhabdus luminescens insect infection. Enzyme overexpression increases the biofilm formation ability
physiological function
A0A7R7A6G8
restriction endonuclease R.Nph3I constitutes an active restriction-modification system with the adjacent methyltransferase NRS3_07 and is sensitive to 6-methyl-adenosine DNA methylation
physiological function
CamA is needed for efficient sporulation and alters persistence in the colon
physiological function
-
DNA adenine methylase (Dam) is essential for modulating inflammasome activation during Salmonella enteritidis infection. There are complex and dynamic interplays between Dam and the inflammasome under different conditions
physiological function
-
UP3_c0262 is a m6A methyltransferase containing a methylated A residue in both DNA strands of the GTNAC motif. Whole genome methylation analysis of SV3F4 shows that 99.9% of the GTNAC motif is m6A modified. The UP3_c0261 (endonuclease) and UP3_c0262 genes may act as a type II restriction-modification system in the Ureaplasma SV3F4 strain
physiological function
-
DNA adenine methylase, not the PstI restriction-modification system, regulates virulence gene expression in Shiga toxin-producing Escherichia coli
physiological function
-
DNA adenine methylase M.PtoI that is part of a type I restriction-modification system
physiological function
-
the enzyme is required for normal sporulation and persistence
physiological function
CamA-mediated methylation at CAAAAA is required for normal sporulation, biofilm formation, and intestinal colonization by Clostridioides difficile
physiological function
peripheral nerve injury significantly alters the global DNA m6A level and decreased N6amt1 expression in dorsal horn neurons
physiological function
-
CamA is needed for efficient sporulation and alters persistence in the colon
-
physiological function
-
CamA-mediated methylation at CAAAAA is required for normal sporulation, biofilm formation, and intestinal colonization by Clostridioides difficile
-
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 is involved in life cycle regulation and also plays a role in DNA mismatch repair
-
physiological function
-
the enzyme plays a major role during Photorhabdus luminescens insect infection. Enzyme overexpression increases the biofilm formation ability
-
physiological function
Picrophilus oshimae DSM 9790
-
DNA adenine methylase M.PtoI that is part of a type I restriction-modification system
-
physiological function
-
the enzyme is required for the bulk of 6-methyladenine and all symmetric methylation at the ApT dinucleotides
-
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
-
physiological function
-
the enzyme is involved in life cycle regulation and also plays a role in DNA mismatch repair
-
physiological function
-
DNA adenine methylase (Dam) is essential for modulating inflammasome activation during Salmonella enteritidis infection. There are complex and dynamic interplays between Dam and the inflammasome under different conditions
-
physiological function
Ureaplasma parvum SV3F4
-
UP3_c0262 is a m6A methyltransferase containing a methylated A residue in both DNA strands of the GTNAC motif. Whole genome methylation analysis of SV3F4 shows that 99.9% of the GTNAC motif is m6A modified. The UP3_c0261 (endonuclease) and UP3_c0262 genes may act as a type II restriction-modification system in the Ureaplasma SV3F4 strain
-
physiological function
Escherichia coli RM13514
-
DNA adenine methylase, not the PstI restriction-modification system, regulates virulence gene expression in Shiga toxin-producing Escherichia coli
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
144000
-
gel filtration, the enzyme occurs as both monomer and dimer in solution
28000
30000
30690
34000
39000
70600
-
2 * 70600, the enzyme occurs as both monomer and dimer in solution, His-tagged enzyme, MALDI-TOF mass spectrometry
72000
-
gel filtration, the enzyme occurs as both monomer and dimer in solution
additional information
-
sequence analysis of the gene for N6-methyladenosine DNA methylase
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
-
2 * 70600, the enzyme occurs as both monomer and dimer in solution, His-tagged enzyme, MALDI-TOF mass spectrometry
monomer
additional information
dimer
-
in solution, but dissociate into monomers upon addition of the DNA
dimer
-
Dam dimerizes on short, synthetic DNA, resulting in enhanced catalysis, however, dimerization is not observed on large genomic DNA
monomer
-
1 * 72000, the enzyme occurs as both monomer and dimer in solution, His-tagged enzyme, gel filtration
monomer
-
enzyme and S-adenosyl-L-methionine form a catalytically active complex
additional information
-
structure analysis of enzyme in ternary complex with partially and fully specific DNA and a methyl-donor analogue
additional information
-
enzyme is predominantly a monomer in solution, mechanism of DNA-induced dimerization upon binding to DNA substrate and complex formation, structure and interaction analysis of the enzyme complexed with a 12mer DNA duplex and S-adenosyl-L-homocysteine in a enzyme/duplex ratio of 2, no flipping of adenine out of the DNA duplex
additional information
-
structure analysis of enzyme in ternary complex with partially and fully specific DNA and S-adenosyl-L-homocysteine, S-adenosyl-L-methionine, or inhibitor adenosyl ornithine, i.e. sinefungin
additional information
the enzyme contains 2 domains: a seven-stranded catalytic domain harboring the binding sites for S-adenosyl-L-homocysteine, and a DNA binding domain of a five-helix bundle and a beta-hairpin
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with double-stranded DNA containing the recognition sequence GANTC, sitting drop vapor diffusion method, using 0.1 M HEPES pH 7.8, with 10% (w/v) polyethylene glycol 8000 and 3% (w/v) polyethylene glycol 6000
enzyme complexed with substrate S-adenosyl-L-methionine, product S-adenosyl-L-homocysteine, or inhibitor sinefungin, and L72P mutant apo-enzyme, 2.0 mg/ml protein in crystallization buffer containing 100 mM HEPES, pH 7.4, 1.5 M LiSO4, and 1-20 mM of the ligand compounds, X-ray diffraction structure determination and analysis at 2.3 A resolution
in complex with cognate DNA at 1.89 A resolution, in the presence of S-adenosyl-L-homocysteine
in complex with duplex DNA and AMP, hanging drop vapor diffusion method, using 10% (w/v) PEG 5000 monomethyl ether, 0.1 M HEPES pH 7.5, 0.2M potassium acetate and 15 mM MnCl2 at 20°C
-
in complex with non-cognate DNA, lacking any GATC sequences, hanging drop vapor diffusion method, using 5-40% (w/v) PEG 200 from and 100 mM MES or HEPES (pH 6.4-7.0)
in complex with its cognate DNA, by the hanging-drop vapour-diffusion method, to a resolution of 2.5 A, crystals belong to the hexagonal space group P6
apoenzyme, hanging drop vapor diffusion method, using 1.0 M Bis-Tris, pH 9.0, 1.4 M ammonium tartrate. Enzyme in complex with S-adenosyl-L-methionine, hanging drop vapor diffusion method, using 1.0 M Bis-Tris pH 6.0, 14% (w/v) PEG 2000, 0.2 M lithium sulfate
-
purified recombinant enzyme in binary complex with S-adenosyl-L-homocysteine or in ternary complex with a synthetic 12 bp DNA duplex and S-adenosyl-L-homocysteine, hanging drop vapour diffusion method, 16°C, reservoir solution contains 2.4 M ammonium sulfate and 100 mM MES, pH 6.0, for the binary complex, and contains 20-25% w/v PEG 8000, 100 mM HEPES, pH 7.5, and 10 mM ammonium sulfate for the ternary complex, X-ray diffraction structure determination and analysis at 2.3-3.5 A resolution, modeling
in complex with S-adenosyl-L-methionine, S-adenosyl-L-homocysteine and with the inhibitor sinefungin, at a resolution of 2.4 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H317A
H336A
N330A
R272A
R302A
R350A
S315A
S315A/H317A/N330A/R350A
the mutant shows about 90% reduced methylation activity on double stranded DNA but no effect on S-adenosyl-L-methionione binding
L72P
site-directed mutagenesis, altered secondary structure, the active site is pushed away from the ligand binding site, especially by altered position of Trp84
S124D
-
reduced solubility of the protein relative to that of the wild-type enzyme, fails to crystallize under the same conditions used to crystallize wild-type enzyme, is active and shows a non-linear dependence of activity on enzyme concentration similar as wild-type
D181A
-
site-directed mutagenesis, inactive mutant, mutation abolishes base flipping, D181 seems to contact and stabilize the flipped base, i.e. the intermediate state of the base flipping process
H335A
-
the mutant is catalytically inactive and binds to DNA more tightly than the wild type enzyme
K139A
K9A
L122A
L122A/P134A
the variant methylates hemimethylated DNA with 80% of wild type activity
L122A/V133L
L122G
the mutant has no preference for hemimethylated substrate and is about 1.5fold more active than the wild type enzyme on the hemimethylated DNA substrate
L122I
the variant methylates hemimethylated DNA with 98% of wild type activity
L122S
the variant is able to sense the methylation status of the 5'-GATC-3' double-stranded target recognition site and methylates only hemimethylated DNA with 35-40% of wild type activity
L122T
the variant methylates hemimethylated DNA with 90% of wild type activity
L122V
the variant methylates hemimethylated DNA with 95% of wild type activity
L175P
slightly lowers the ability of the restriction enzyme to cut DNA
N120A
N120S
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme
N126A
N132A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
P134A
P134G
R116A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
R124A
R124S/P134S/K139E/F159L/K241E
-
the mutant shows a more than 20fold preference for methylation at GATT, overall corresponding to a 1600fold change in specificity, the mutant is virtually inactive at GATC sites
R137A
R95A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
S188A
-
site-directed mutagenesis, exchange in the loop next to the active site, 7-8fold reduction of kcat, mutant shows 92% of wild-type enzyme activity
T190A
-
site-directed mutagenesis, mutant shows 75% of wild-type enzyme activity
V133A
the mutant shows increased activity with hemimethylated DNA compared to the wild type enzyme (160%)
V133I
the mutant shows decreased activity with hemimethylated DNA compared to the wild type enzyme
V133L
the mutant shows most strongly decreased activity with hemimethylated DNA compared to the wild type enzyme
V133S
the mutant shows strongly decreased activity with hemimethylated DNA compared to the wild type enzyme
Y119A
-
site-directed mutagenesis, over 100fold reduced activity compared to the wild-type enzyme, 2-3fold reduced DNA binding compared to the wild-type enzyme
Y138A
Y138R
-
the mutant which carries both base Gua1 recognition elements (K9 from EcoDam) is fully active and specific, about 2fold more active than the wild type enzyme
Y184A
-
site-directed mutagenesis, mutant shows 1.7% of wild-type enzyme activity
D194A
F195S
-
the mutant is not able to bind to the S-adenosyl-L-methionine as effectively as the wild type enzyme and is catalytically inactive
Y32L
-
the mutant binds to S-adenosyl-L-methionine as efficiently as wild type enzyme but is catalytically inactive
D194A
M98A
-
to avoid expression of this truncated protein, a mutant form of the Pyrococcus horikoshii dam gene (M98A) is prepared by site-directed mutagenesis
additional information
H317A
-
the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
H317A
-
the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
H336A
-
the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
H336A
-
the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
N330A
-
the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
N330A
-
the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
R272A
-
the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
R272A
-
the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
R302A
-
the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
R302A
-
the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
R350A
-
the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
R350A
-
the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
S315A
-
the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
S315A
-
the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
K139A
-
site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
K139A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
K9A
-
the mutant shows strongly reduced methylation activity towards the sequence GATC
L122A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme
L122A
reduces the size of an aliphatic hydrocarbon side chain, is sufficient to convert EcoDam into a bona fide maintenance MTase with pronounced preference for hemimethylated DNA
L122A
the mutant is almost inactive on unmethylated DNA. The variant is able to sense the methylation status of the 5'-GATC-3' double-stranded target recognition site and methylates only hemimethylated DNA with 35-40% of wild type activity
L122A/V133L
the variant is able to sense the methylation status of the 5'-GATC-3' double-stranded target recognition site and methylates only hemimethylated DNA
L122A/V133L
the mutant shows increased activity with hemimethylated DNA compared to the wild type enzyme
N120A
-
site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme
N120A
loses its p-stacking with Gua1, shows small changes in specificity factor S1
N126A
the mutant displays decreased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
P134A
-
site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
P134A
high catalytic activity, exhibits only a small reduction in the amplitude of the fluorescence change, but no detectable changes in the kinetics of base-flipping, induces base-flipping of the substrate with altered sequence at the third base-pair
P134A
the variant methylates hemimethylated DNA with 100% of wild type activity
P134G
-
site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
P134G
high catalytic activity, exhibits only a small reduction in the amplitude of the fluorescence change, but no detectable changes in the kinetics of base-flipping, induces base-flipping of the substrate with altered sequence at the third base-pair
R124A
-
site-directed mutagenesis, over 100fold reduced activity and about 10fold reduced DNA binding compared to the wild-type enzyme
R124A
overall reduction in catalytic activity but methylates the near-cognate substrates GATT and GATG faster than the canonical GATC, no base-flipping signal
R137A
-
site-directed mutagenesis, DNA binding is similar to the wild-type enzyme
R137A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
Y138A
-
site-directed mutagenesis, DNA binding is similar to the wild-type enzyme
Y138A
loses its interaction with the O6 atom of Gua1, shows small changes in specificity factor S1
D194A
the Hia5 mutant shows loss of DNA MTase activity
D194A
Haemophilus influenzae biotype aegyptius ATCC 11116
-
the Hia5 mutant shows loss of DNA MTase activity
-
additional information
-
mutated dam gene, in which either the aspartic acid or the tyrosine residue was changed to alanine, do not possess MTase activity in the DPPY motif, resistant to DpnI digestion and sensitive to DpnII restriction endonuclease cutting, overproduction in Aeromonas hydrophila results in bacterial motility, hemolytic and cytotoxic activities associated with the cytotoxic enterotoxin, and protease activity similar to that of the wild-type
additional information
-
strain SSU dam chromosomal deletion mutant, is not viable
additional information
-
mutated dam gene, in which either the aspartic acid or the tyrosine residue was changed to alanine, do not possess MTase activity in the DPPY motif, resistant to DpnI digestion and sensitive to DpnII restriction endonuclease cutting, overproduction in Aeromonas hydrophila results in bacterial motility, hemolytic and cytotoxic activities associated with the cytotoxic enterotoxin, and protease activity similar to that of the wild-type
-
additional information
-
strain SSU dam chromosomal deletion mutant, is not viable
-
additional information
-
no methylation of the TGATCprox site after mutation of the site, and subsequently no PapI-dependent binding of Lrp to binding sites 1-3
additional information
EcoDam K9A variant, shows slightly reduced catalytic activity and DNA binding, shows a loss of specificity at the first base-pair, unable to methylate any of the near-cognate sites, base-flipping of substrates carrying a base-pair substitution at the first position of the target site is more efficient than with wild-type
additional information
-
EcoDam K9A variant, shows slightly reduced catalytic activity and DNA binding, shows a loss of specificity at the first base-pair, unable to methylate any of the near-cognate sites, base-flipping of substrates carrying a base-pair substitution at the first position of the target site is more efficient than with wild-type
additional information
-
complementation of the Escherichia coli dam mutant strain GM2163 with the Yersinia enterocolitica dam gene
additional information
-
mutant strains dam, dam mutS, and mutS, deficient in dam and/or mismatch repair, mutS strain does not display many differences from the wild-type at the transcriptional level, both dam and dam mutS strains show differential expression of 206 and 114 genes and expression at higher levels as wild-type, dam mutS strain shows higher variability among some of these induced genes than the dam strain, dam strain has a significantly higher level of basal double-strand breaks than the dam mutS strain
additional information
-
mutational inactivation of the enzyme does not influence the mismatch repair, the adherence of the bacterium to host cells, e.g. HEp-2 cells, or the fitness of the bacterial cell
additional information
-
site-directed mutagenesis at the dimer interface drastically affects enzyme activity in addition to the oligomeric status of the enzyme
additional information
-
deletion of the ORF does not affect cell viability
additional information
-
dam mutant, a CamS SmR SpR exconjugant can not be obtained
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, purified recombinant enzyme, 10 mM Tris-HCl, pH 7.4, 0.1 mM EDTA, 100 mM KCl, 7 mM 2-mercaptoethanol, and 10% glycerol, stable for at least 3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phosphocellulose column chromatography, hydroxyapatite column chromatography, and Sephacryl S-200 gel filtration
-
ceramic hydroxylapatite column chromatography and cation exchange column chromatography
-
GST affinity column chromatography and HiTrap column chromatography
-
heparin Hyper D column chromatography, Source 15Q column chromatography, heparin TSK column chromatography, Source 15 S column chromatography, Superdex 75 gel filtration, and ceramic HTP column chromatography
HiTrap Q column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration
mutant purified by nickel-ion metal-affinity chromatography, more than 95% pure
-
Ni-NTA affinity column chromatography, Mono S column chromatography, and Superdex 200 gel filtration
-
Ni-NTA agarose column chromatography
Ni-NTA column chromatography
Ni2+ affinity column chromatography, UnoS column chromatography, and S75 Sepharose column chromatography
P-11 phosphocellulose column chromatography, heparin-Sepharose column chromatography, Sephacryl S-200 gel filtration, and hydroxyapatite column chromatography
-
partial purification using phosphocellulose column chromatography, hydroxylapatite column chromatography, CM-Sephadex gel filtration, and heparin agarose column chromatography
-
phosphocellulose column chromatography and Blue Sepharose column chromatography
recombinant enzyme from Escherichia coli strain DH10B to homogeneity by ultracentrifugation, treatment by 1% v/v polyethyleneimine with 250 mM KCl, ammonium sulfate fractionation, several steps of dialysis, phosphocellulose resin chromatography, and affinity chromatography
-
HiTrap Q column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration
-
HiTrap Q column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration
-
phosphocellulose column chromatography and Blue Sepharose column chromatography
-
phosphocellulose column chromatography and Blue Sepharose column chromatography
phosphocellulose column chromatography and Blue Sepharose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of T2 dam gene into expression vector pJW2, creation of T2-T4 hybrid genes in expression vector pJW2
-
expressed as glutathione S-transferase fusion protein in Escherichia coli BL21 (DE3) pLysS cells
-
expressed in Escherichia coli
expressed in Escherichia coli strain ER2566
expressed in Escherichia coli XL2-Blue cells
expression in Escherichia coli
from transposon Tn1549, into plasmid pEfaORF18Ks, expressed in Escherichia coli GM2163 cells
gene ahdI, genetic organization and regulation, modelling transcription activity of the PahdICR operon from the PahdIMS promoter, expression in Escherichia coli
-
gene yhdJ or ccrM, chromosomally encoded, DNA sequence determination and analysis, overvexpression decreases bacterial growth by altering cell division, cells show aberant morphology
-
genomic library construction, DNA and amino acid sequence determination and computational analysis, genetic organization, expression in Escherichia coli
in a T7 promoter-based vector system using Escherichia coli ER2566 as a host strain, which can alter the virulence potential
-
into a pQE60 vector containing a C-terminal 6 x His tag and transformed into Escherichia coli M15 cells
ligated into KpnI/XbaI-digested pBluescriptIIKS+, Dam overproduction in Yersinia enterocolitica, which results in an increased frequency of spontaneous mutation and marginally resistance to 2-aminopurine, subcloned into pVLT33 under the control of an inducible Ptac promoter and introduced into the dam mutant strain Escherichia coli GM2163, can complement it, overproduction in CHO cells, lleads to increased invasion of Yersinia enterocolitica
-
native or mutated dam gene overexpressed from the pBAD/damAhSSU pBAD/damD/A, or pBAD/damY/A plasmid under the control of an araBAD promoter, transformed to Escherichia coli GM33
-
overproduction in Yersinia enterocolitica, increased spontaneous resistance to chloramphenicol 21.2fold and to streptomycin 39.4fold, decrease in resistance to 2-aminopurine, expression in Yersinia enterocolitica mutant strain GHY121, can complement it
-
putative Pfa MTase gene, subcloned into different expression vectors under regulatable promoters, these constructs separately transferred into Escherichia coli and yeast cells
-
genomic library construction, DNA and amino acid sequence determination and computational analysis, genetic organization, expression in Escherichia coli
genomic library construction, DNA and amino acid sequence determination and computational analysis, genetic organization, expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
peripheral nerve injury significantly decreased the level of m6A-specific DNA methyltransferase 1 (N6amt1) in dorsal horn neurons
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
medicine
additional information
analysis
-
Dam alters the Ca2+ regulation of Yop secretion but does not affect the temperature regulation of Yop/Ysc expression, in Dam-overproducing strains transcription of the lcrGV and yopN-tyeA operons is slightly upregulated, but LcrG is absent from lysates, while the amounts of YopN and TyeA are not changed, clpXP expression increases after Dam overproduction and the ClpP protease then degrades LcrG, thereby releasing a block in type III secretion
analysis
the first Gua is recognized by K9, removal of which abrogates the first base-pair recognition, the flipped target Ade binds to the surface of EcoDam in the absence of S-adenosyl-L-methionine, which illustrates a possible intermediate in the base-flipping pathway, the orphaned Thy residue displays structural flexibility by adopting an extrahelical or intrahelical position where it is in contact to N120
analysis
structural model of the type IC M.EcoR124I DNA methyltransferase, comprising the HsdS subunit, two HsdM subunits, the cofactor S-adenosyl-L-methionine and the substrate DNA molecule
analysis
-
computational analysis of a published Dam knockout microarray alongside other publicly available
analysis
-
the dimer stabilizes and enhances site-specific DNA-binding by the MTase, because the DNA-binding site may require an interfacial structure formed by both monomers, role of Type II MTases as defense systems against phage
analysis
A0A7R7A6G8
sequential 1-day and one-pot workflow covering in vitro protein synthesis and enzymatic assays to confirm the exact function of putative restriction-modification systems. Fluorogenic molecular beacon probes containing all the probable recognition sequences, are designed and used for the fluorogenicenzyme assay
medicine
potential targets for both vaccines and antimicrobials
medicine
-
methyltransferase activity associated with Dam is essential for attenuation of Aeromonas hydrophila virulence, immunization of mice with a native-Dam-overproducing strain at the same 50% lethal dose does not result in any lethality and provides protection to animals after subsequent challenge with a lethal dose of the control strain
medicine
-
essential for the viability of the bacterium, overproduction of Dam in Aeromonas hydrophila SSU reduces the virulence of the pathogen, decreases the motility and T3SS-associated cytotoxicity, but increases both the cytotoxicity and hemolysis associated with Act, mice infected with the Dam-overproducing strain do not die over a tested period of 3 weeks, indicating bacterial attenuation as a result of Dam overproduction
medicine
-
epigenetic effects, in addition to genotoxic effects, need to be considered in chemical carcinogenesis initiated by r7,t8-dihydroxy-t9,10-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene, since the inhibition of methylation may allow the expression of genes that promote tumor development
medicine
confers antibiotic resistance in clinical isolates, important determinant of bacterial virulence, may be transmitted by horizontal gene transfer, potential drug target
medicine
-
upregulation of recombinational repair in dam mutants allows for the efficient repair of double-strand breaks whose formation is dependent on functional mismatch repair
medicine
potential targets for both vaccines and antimicrobials
medicine
-
DNA adenine methyltransferase identification is a useful technology to map holocarboxylase synthetase binding sites in human chromatin
medicine
-
methyltransferase activity associated with Dam is essential for attenuation of Aeromonas hydrophila virulence, immunization of mice with a native-Dam-overproducing strain at the same 50% lethal dose does not result in any lethality and provides protection to animals after subsequent challenge with a lethal dose of the control strain
-
medicine
-
essential for the viability of the bacterium, overproduction of Dam in Aeromonas hydrophila SSU reduces the virulence of the pathogen, decreases the motility and T3SS-associated cytotoxicity, but increases both the cytotoxicity and hemolysis associated with Act, mice infected with the Dam-overproducing strain do not die over a tested period of 3 weeks, indicating bacterial attenuation as a result of Dam overproduction
-
additional information
-
high degree of homology to the prokaryote enzymes
additional information
-
transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
-
transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
-
transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
-
transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
-
transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
Peridinium triquetrum
-
transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
-
contains complete DNA-[adenine] MTase-like ORF but the DNA-[adenine] MTase like gene is a pseudogene, no evidence of DNA-[adenine] methylation
additional information
-
contains complete DNA-[adenine] MTase-like ORF but the DNA-[adenine] MTase like gene is a pseudogene, no evidence of DNA-[adenine] methylation
additional information
-
DNA-[adenine] MTase like gene is a pseudogene, no evidence of DNA-[adenine] methylation, DNA methylation may occur in a cell-cycle regulated manner, or as a developmental stage-specific event that does not include the red cell stage
additional information
-
potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
additional information
-
potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
additional information
-
potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
additional information
-
potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
additional information
-
potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
additional information
-
potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
additional information
-
potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
additional information
-
DNA-[adenine] MTase pseudogene, ORF encodes a protein exhibiting a high degree of homology to the putative Saccharomyces cerevisiae MTase
EXTERNAL LINKS (specific for EC-Number 2.1.1.72)
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Release 2026.1 (March 2026)
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