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adenine methyltransferase
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-
adenine N6-methyltransferase
-
-
adenine-N6 DNA methyltransferase
-
-
AhdI methyltransferase
-
-
ApyPI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
AquII
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
AquII
Synechococcus 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
Synechococcus 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
Synechococcus 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
Bacillus sp. NEB686
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
CcrM DNA adenine methyltransferase
-
-
CdpI
Q6NFX9
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
cell cycle-regulated methyltransferase
-
-
cell-cycle regulating MTase
-
-
CstMI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
CstMI
Corynebacterium striatum M82B
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
Dam
Edwardsiella tarda TXD1
D5FM16
-
-
Dam
-
-
659920,
671878,
674250,
675380,
675828,
676746,
702334,
702628,
703200,
703347,
704168,
704430,
705127,
705175,
713742,
720029
Dam DNA-(adenine-N6)-methyltransferase
-
-
Dam DNA-(adenine-N6)-MTase
-
-
DNA adenine 5'-GATC-3' methylase
-
-
DNA adenine methylase
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
-
;
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
Amoeba proteus D
-
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
D5FM16
-
DNA adenine methyltransferase
Edwardsiella tarda TXD1
D5FM16
-
-
DNA adenine methyltransferase
P04392
-
DNA adenine methyltransferase
-
-
659040,
659422,
674250,
675380,
675828,
676746,
702115,
702334,
703347,
703765,
704168,
704430,
705127,
713742,
720029
DNA adenine methyltransferase
P0AEE9
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
G9C944
-
DNA adenine methyltransferase
Haemophilus influenzae biotype aegyptius ATCC 11116
G9C944
-
-
DNA adenine methyltransferase
Haemophilus influenzae Rd (FluMu)
-
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
Neisseria meningitidis Z2491 (Pnme1)
-
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferase
-
-
DNA adenine methyltransferases
-
-
DNA adenine N6-methyltransferases
-
-
DNA adenine N6-methyltransferases
G9C944
-
DNA adenine N6-methyltransferases
Haemophilus influenzae biotype aegyptius ATCC 11116
G9C944
-
-
DNA adenine N6-methyltransferases
Haemophilus influenzae Rd (FluMu)
-
-
-
DNA adenine N6-methyltransferases
-
-
DNA adenine N6-methyltransferases
Neisseria meningitidis Z2491 (Pnme1)
-
-
-
DNA methyltransferase
-
-
DNA methyltransferase
P43423
-
DNA methyltransferase
Geobacillus stearothermophilus SE-589
-
-
-
DNA methyltransferase
-
-
DNA methyltransferase
Neisseria gonorrhoeae FA1090
-
-
-
DNA [amino]-methyltransferase
-
-
DNA-(adenine N6)-methyltransferase
-
-
DNA-(adenine-N6)-methyltransferase
-
-
DNA-(adenine-N6)-methyltransferase
-
-
DNA-(adenine-N6-)-methyltransferase
-
-
DNA-(N6-adenine)-methyltransferase
-
-
DNA-adenine methyltransferase
-
-
DNA-[adenine] methyltransferase
Anopheles gambiae,
Arabidopsis thaliana,
Caenorhabditis elegans,
Chlamydomonas reinhardtii,
Chlorella sp.,
Drosophila melanogaster,
Homo sapiens,
Leishmania major,
Oxytricha fallax,
Paramecium aurelia, Peridinium triquetrum,
Plasmodium falciparum,
Plasmodium knowlesi,
Plasmodium yoelii,
Saccharomyces cerevisiae,
Schizosaccharomyces pombe,
Stylonychia mytilus,
Tetrahymena thermophila -
-
DNA-[adenine] MTase
Anopheles gambiae,
Arabidopsis thaliana,
Caenorhabditis elegans,
Chlamydomonas reinhardtii,
Chlorella sp.,
Drosophila melanogaster,
Homo sapiens,
Leishmania major,
Oxytricha fallax,
Paramecium aurelia, Peridinium triquetrum,
Plasmodium falciparum,
Plasmodium knowlesi,
Plasmodium yoelii,
Saccharomyces cerevisiae,
Schizosaccharomyces pombe,
Stylonychia mytilus,
Tetrahymena thermophila -
-
DNA-[N6-adenine] MTase
-
-
DNA-[N6-adenine]-methyltransferase
-
-
-
-
DNAm6A MTase
Haemophilus influenzae biotype aegyptius ATCC 11116
G9C944
-
-
DNAm6A MTase
Haemophilus influenzae Rd (FluMu)
-
-
-
DNAm6A MTase
Neisseria meningitidis Z2491 (Pnme1)
-
-
-
DraRI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
DraRI
Deinococcus radiodurans RI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
DrdIV
C0LTP9
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
DrdIV
Deinococcus radiodurans NEB479
C0LTP9
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
EcoDam DNA-[N6-adenine] MTase
-
-
EcoRII DNA methyltransferase
-
-
Hia5 protein
Haemophilus influenzae biotype aegyptius ATCC 11116
G9C944
-
-
Hin1523 protein
Haemophilus influenzae Rd (FluMu)
-
-
-
HP0050 methyltransferase
-
-
HP0050 methyltransferase
-
-
-
HP0593 DNA-(N6-adenine)-methyltransferase
-
-
HP0593 DNA-(N6-adenine)-methyltransferase
-
-
-
HpyAXII
-
consists of a restriction endonuclease and a DNA methyltransferase
HpyAXII
Helicobacter pylori NSH57
-
consists of a restriction endonuclease and a DNA methyltransferase
-
KpnI DNA methyltransferase
-
-
KpnI DNA-(N6-adenine)-methyltransferase
-
-
M.BstZ1II
Geobacillus stearothermophilus 14P
Q32WE7
-
-
M.Csp231I
Citrobacter sp.
Q32WH2
-
M.HpyAXII
Helicobacter pylori NSH57
-
-
-
M.NgoAXP
Neisseria gonorrhoeae FA1090
-
-
-
M1.MboII
-
a type IIS methyltransferase
M2.BstSEI
Geobacillus stearothermophilus SE-589
-
-
-
m6A methyltransferase
Q9L8Y0
-
MaqI
A1U7P0
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
MmeI
B2MU09
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
MmeI
B2MU09
has both endonuclease and DNA methyltransferase activities
MTase
Citrobacter sp.
Q32WH2
-
MTase
Geobacillus stearothermophilus 14P
Q32WE7
-
-
N-6 adenine-specific DNA methyltransferase 1
Q9Y5N5
-
N6 adenine methyltransferase
-
-
N6 adenine methyltransferase
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-
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N6-adenine DNA -methyltransferase
-
-
-
-
N6-adenine methyltransferase
Q9L8Y0
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NgoAXPMod subunit
Neisseria gonorrhoeae FA1090
-
-
-
NhaXI
Q1QGU9
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
NhaXI
Q1QGU9
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
NlaCI
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
NlaCI
Neisseria lactamica ST640 Sange
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
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Nme1821 protein
Neisseria meningitidis Z2491 (Pnme1)
-
-
-
NmeAIII
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
NmeAIII
-
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
PlaDI
A7HWD2
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
PspOMII
C0LTP8
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
PspOMII
C0LTP8
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
PspPRI
A5WI42
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
PspPRI
A5WI42
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
RceI
B6IW55
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
RceI
B6IW55
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
restriction-modification system
-
-
-
-
RpaB5I
Q134M6
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
RpaB5I
Q134M6
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
-
RsrI N6-adenine DNA methyltransferase
-
-
SdeAI
Q30TC2
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
specific methyltransferase
Citrobacter sp.
Q32WH2
-
specific methyltransferase
Q32WH2
-
-
specific methyltransferase
Q32WE7
-
specific methyltransferase
Geobacillus stearothermophilus 14P
Q32WE7
-
-
SpoDI
Q5LS45
a type II restriction endonuclease that combines endonuclease and methyltransferase activities
T4 Dam (N6-Ade)-MTase
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T4 Dam DNA methyltransferase
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T4 Dam DNA-(N6-adenine)-methyltransferase
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T4 DNA-adenine methyltransferase
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T4Dam DNA-[N6-adenine] MTase
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T4DNA-(N6-adenine)-methyltransferase
-
-
type IC M.EcoR124I DNA methyltransferase
P10484
-
VspI methyltransferase
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modification methylase
-
-
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-
additional information
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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
Citrobacter sp.
Q32WH2
the enzyme belongs to the m6N-adenine beta-class MTases
additional information
Q32WH2
the enzyme belongs to the m6N-adenine beta-class MTases
-
additional information
-
enzyme belongs to the Dam MTase family
additional information
Q32WE7
the enzyme belongs to the m6N-adenine beta-class MTases
additional information
Geobacillus stearothermophilus 14P
Q32WE7
the enzyme belongs to the m6N-adenine beta-class MTases
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S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
P14751
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme mediates methyl group transfer reaction from S-adenosyl-L-methionine to adenine in the palindromic recognition sequence, GATC, of a 20-mer oligonucleotide duplex
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GGGTGATCAGGG, CCCTGATCACCC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme modifies the third adenine within the recognition sequence 5-ATTAAT-3'
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
canonical 14mers and various substituted duplexes. Non-selfcomplementary tetradecamer duplex d[GCCGGATCTAGACG]*d[CGTCTAGATCCGGC] containing the hemimethylated GATC target sequence on one or the other strand and modifications in the GATC target sequence of the complementary strands. Large differences in DNA methylation of duplexes containing single dI or dG substitutions of the Dam recognition site are observed compared with the canonical substrate, if the substitution involves the top strand, on the G-C rich side. Substitution in either strand by uracil or 5-ethyluracil result in small perturbation of the methylation patterns. When 2,6-diamino-purine replaces the adenine to be methylated, small but significant methylation is observed
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
in unmethylated target (2A/A duplex), the enzyme alone randomly binds to the asymetric 2A/A duplex, S-adenosyl-L-methionine induces an allosteric T4 conformational change that promotes reorientation of the enzyme to the strand containing the native base. S-Adenosyl-L-methionine increases enzyme binding-specificity, in addition to serving as the methyl donor, the enzyme recognizes the palindromic sequence GATC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
various synthetic oligonucleotide substrates. Upon collision of an enzyme monomer with an oligonucleotide duplex, an asymmetrical complex forms in which the enzyme (randomly oriented relative to one of the strands of the specific recognition site) catalyzes a fast transfer of the methyl group from S-adenmosylmethionine to the adenosine residue. Simultaneously, a second T4MTAse subunit is added to the complex, providing for the continuation of the reaction
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme catalyzes methyl group transfer from S-adenosyl-L-methionine to the N6-position of adenine in the palindromic sequence GATC. The rate-limiting step is release of product methylated DNA from the enzyme
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
oligonucleotide substrates containing the native or modified recognition site. The enzyme recognizes the palindromic sequence GATC and catalyzes transfer of the methyl group from S-adenosyl-L-methionine to the N6-position of adenine. The release of product is the rate-limiting step in the reaction
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme preferentially binds DNA before S-adenosylmethionine. S-Adenosylhomocysteine is preferentially released from the enzyme before fully methylated DNA. Binding of both substrates and methylation occurs first in a rapid step followed by regeneration of enzyme in a second rate-limiting step
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme de novo methylates the first adenine residue in the TGATCA sequence in the single-stranded or double-stranded DNA substrate, but it prefers single-stranded structures
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
canonical 12-mer and 20-mers various defective duplexes containing some defect in the DNA-target site, e.g. the absence of an internucleotide phosphate or a nucleotide within the recognition site, or a single-stranded region
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
non-self-complementary tetradecanucleotide duplexes that contain the GATC target sequence. The enzyme is rather tolerant to base modification, binding of the enzyme is inversely proportional to the thermodynamic stability of the duplex in the ternary complex
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GCGTGATCACGC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
nonglucosylated unmethylated T4 gt- dam- DNA. The enzyme methylates the palindromic tetranucleotide, GATC, designated the canonical sequence. At high Mtase:DNA ratios, T4 Dam can methylate some noncanonical sequences belonging to GAY, where Y represents cytosine or thymine
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
GGGTGATCAGGG+CCCTGATCACCC, annealed
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
synthetic oligonucleotide substrates containing the native recognition site GATC or its modified variants
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
interaction with substrates containing defective recognition sites. Deoxyguanosine residues in both strands of the modified GATC are indispensable for complex formation
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
nonglucosylated, hydroxymethylcytosine-containing T2gt- virion DNA has a higher level of methylation than T4gt virion DNA does
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
lambda phage DNA
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of DNA in a sequence specific manner, low substrate specificity with respect to the target base. Cytosine residues can be methylated if they are located in a C:T mismatch base pair at the target position of the enzyme, modification of cytosine residues at position N4
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is involved in cell cycle regulation of Caulobacter crescentus
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a critical regulator of bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a member of a restriction-modification system, R-M system, plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is not important in mismatch repair and for adherence of the bacterium to host cells, e.g. HEp-2 cells
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
P04392
methylation of DNA-adenine at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as in bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of the site GATCprox proximal to the promotor is required for transition to the phase On state by specifically blocking PapI-dependent binding of Lrp to promotor proximal sites 4-6, expression of pyelonephritis-associated pili, i.e. Pap, in uropathogenic Escherichia coli is epigenetically controlled by a reversible OFF to ON switch, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific target sequence is GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is cell cycle regulated and essential for viability
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
unmethylated or hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
binding site is the GATC sequence, the adenine is located in the palindromic recognition site GATC, substrate binding mechanism
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
DNA substrate from calf thymus, methylation of adjacent GATC sites is distributive with DNA derived from a genetic element that controls the transcription of the adjacent genes, the first methylation event is followed by enzyme release
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme methylates the first adenine in the sequence ATGCAT
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme recognizes the sequence 5'-GGTACC-3', methylation at position N6, enzyme utilizes plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of target sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
required substrate recognition target sequence is GATC, occuring base flipping in absence of S-adenosyl-L-methionine is a biphasic process and very fast, but binding of the flipped base into the active site pocket requiring S-adenosyl-L-methionine is slow, active site contains the conserved DPPY motif, whose tyrosine184 residue stacks to the flipped target base
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific for methylation site sequence GATC and structure, an intact GA sequence is essential for activity, altered structural symmetry of the DNA substrate decreases kcat sharply, the best contact between enzyme and DNA is a palindromic interaction site covering the 5'-symmetric residues, which is located in the major groove, and another one in the 3'-half covering the 3'-symmetric residues is located in the minor groove, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific for methylation site sequence GATC and structure, an intact GAT sequence is essential for activity, altered structural symmetry of the DNA substrate decreases kcat sharply, the best contact between enzyme and DNA is a palindromic interaction site covering the 5'-symmetric residues, which is located in the major groove, and another one in the 3'-half covering the 3'-symmetric residues is located in the minor groove, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific methylation of oligonucleotide duplexes containing one or two target sequence GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
P04392
specific methylation of target sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific target sequence is GATC, transition of enzyme-DNA interaction from nonspecific to specific interaction utilizing different substrates, identification of discriminatory contacts stabilizing the transition state, and antidiscriminatory contacts not affecting the methylation of the cognate site but disfavor activity at noncognate sites, involved residues are M114, R116, P126, G128, R130, F111, S112, D171, K11, and Y174, overview, flipping of target adenine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
P14751
substrate and product binding site structures
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
transition of enzyme-DNA interaction from nonspecific to specific interaction utilizing different substrates, identification of discriminatory contacts stabilizing the transition state, and antidiscriminatory contacts not affecting the methylation of the cognate site but disfavor activity at noncognate sites, involved are Y119, N120, L122, R124, and P134, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
unmethylated or hemimethylated DNA, two distinct stages of methylation under single turnover conditions
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
P14385
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
P0AEE8
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
P04043
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP9, -
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
P23192
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
P10484
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q6NFX9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A1U7P0
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A7HWD2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q30TC2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q5LS45
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam belongs to the alpha-class of adenine methyltransferases and transfers a methyl group to the N-6 position of the adenine in the DNA sequence 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam catalyzes postreplicative methylation of adenosine moieties located in 5'-GATC-3' sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
D5FM16, -
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates a GATC recognition site
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates the adenine residue in GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
P0AEE9
Dam methylates the N-6 position of adenine in the DNA sequence 5'-GATC-3' and is highly processive, catalyzing multiple methyltransfers prior to dissociating from the DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates the N-6 position of the adenine in the sequence 5'-GATC-3', Dam shows a dramatic preference for the in vitro methylation of certain GATC sequences in plasmids and PCR-derived DNAfragments
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
DNA adenine methyltransferase methylates the N6 positions of adenines in the sequence 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
EcoP15I MTase adds a methyl group to the second adenine in the recognition sequence 5'-CAGCAG-3' in the presence of S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B2MU09
MmeI modifies only the adenine in the top strand, 5-TCCRAC-3, MmeI endonuclease activity is blocked by this top strand adenine methylation and is unaffected by methylation of the adenine in the complementary strand, 5-GTYGGA-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
recognition sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GANTC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GANTC, CcrM is more active on hemimethylated than unmethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the wild type enzyme shows target specificity for GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
129-mer DNA or pUC19 DNA are used as substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
duplex 2 DNA, 5'-GCAG-3' is the recognition site for the enzyme
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
HP0050 methyltransferase methylates one adenine at a time in the sequence 5'-GAAG-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the EcoRV DNA methyltransferase methylates the first adenine in the GATATC recognition sequence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the enzyme methylates adenines at the N6 position of palindromic 5-GATC-3 sites. The enzyme ethylates both strands of the same site prior to fully dissociating from the DNA, a process referred to as intrasite processivity. Intrasite processivity is disrupted when the DNA flanking a single GATC site is longer than 400 bp on either side. The introduction of a second GATC site within this flanking DNA reinstates intrasite methylation of both sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
G9C944
the Hia5 protein causes the methylation of 61% of the adenines in lambda DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the Hin1523 protein causes the methylation of 29.6% of the adenines in lambda DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Corynebacterium striatum M82B
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Helicobacter pylori NSH57
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Neisseria meningitidis Z2491 (Pnme1)
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Deinococcus radiodurans RI
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Haemophilus influenzae Rd (FluMu)
-
the Hin1523 protein causes the methylation of 29.6% of the adenines in lambda DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Amoeba proteus D
-
the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Edwardsiella tarda TXD1
D5FM16
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Neisseria lactamica ST640 Sange
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Neisseria gonorrhoeae FA1090
-
the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Bacillus sp. NEB686
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Deinococcus radiodurans NEB479
C0LTP9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
HP0050 methyltransferase methylates one adenine at a time in the sequence 5'-GAAG-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
duplex 2 DNA, 5'-GCAG-3' is the recognition site for the enzyme
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Haemophilus influenzae biotype aegyptius ATCC 11116
G9C944
the Hia5 protein causes the methylation of 61% of the adenines in lambda DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Synechococcus sp. PCC 7002 PR-6
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Geobacillus stearothermophilus SE-589
-
the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + oligodeoxynucleotide duplexes
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
substrate contains one single specific recognition site as 5'-GATC/5'-GATC, or modified variants
-
-
?
S-adenosyl-L-methionine + pUC19 DNA adenine
S-adenosyl-L-homocysteine + pUC19 DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
-
-
-
?
additional information
?
-
-
S-adenosyl-L-methionine plays a crucial role in reorientation of the enzyme in DNA with mutationally altered Ade residues to 2-aminopurine, overview
-
-
-
additional information
?
-
-
DNA substrate specificities of wild-type and mutant enzymes
-
-
-
additional information
?
-
-
enzyme and S-adenosyl-L-methionine form a catalytically active complex
-
-
-
additional information
?
-
P04392
enzyme binds also nonspecific to DNA, linear diffusion along the DNA, overview
-
-
-
additional information
?
-
-
substrate specificity with different oligonucleotides, substrate binding specificity, overview
-
-
-
additional information
?
-
-
the common methyl transfer from S-adenosyl-L-methionine to an exocyclic amino group, catalyzed by many enzymes, does not dictate a common kinetic scheme for MTases, comparison to T4Dam MTase from bacteriophage T4
-
-
-
additional information
?
-
-
catalyzes the transfer of a methyl group to the C5 position of the 3'-side cytosine of each strand of the recognition sequence, M.EcoRII binding is diminished by factors of 5-30 but the catalytic activity is either abolished or reduced 4-80fold when trans-anti-B[a]P-N2-dG lesions are introduced into the EcoRII recognition sequence, methylation rates are also diminished and in some cases entirely abolished, depending on the position of the lesion within the recognition sequence
-
-
?
additional information
?
-
-
DNA methylation by DAM may not globally affect gene transcription by physically blocking access of transcription factors to binding sites, Dam is down regulated in the stationary phase, which correlates with the enrichment of GATC in binding sites for CRP and Sigma 38
-
-
-
additional information
?
-
-
the enzyme is part of the type II restriction-modification system AhdI, overview
-
-
-
additional information
?
-
-
Dam-dependent regulation of secretion of pathogenicity island 1 is transmitted via transcriptional regulator HilD
-
-
?
additional information
?
-
B2MU09
MmeI does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
no detectable activity on the single-stranded form of the phage PhiX174 DNA is observed with M1.MboII, double-stranded DNA is less efficiently methylated than pUC18 DNA
-
-
-
additional information
?
-
-
plastid transcription is largely insensitive to adenine methylation of the plastid DNA
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP9, -
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q6NFX9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A1U7P0
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q1QGU9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A7HWD2
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP8
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A5WI42
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
B6IW55
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q134M6
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q30TC2
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q5LS45
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the preferred substrate consists of the annealed product of oligonucleotides 5'-CATTTACTTGATCCGGTATGC-3' and 5'-GCATACCGGATCAAGTAAATG-3', while the nonpreferred substrate consists of the annealed product of oligonucleotides 5'-CATTTAGACGATCTTTTATGC-3' and 5'-GCATAAAAGATCGTCTAAATG-3'
-
-
-
additional information
?
-
-
the wild type Dam shows no detectable activity at GATT sites
-
-
-
additional information
?
-
Q9Y5N5
purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
-
-
-
additional information
?
-
-
the enzyme has a high specificity for GANTC sites, with only minor preferences at the central position. It slightly (1.5fold) prefers hemimethylated DNA over methylated DNA
-
-
-
additional information
?
-
-
the enzyme recognizes and methylates GAGG (100% activity, Km 0.00522 mM), GGAG (about 48% activity, Km 0.017 mM) and GAAG (about 30% activity, Km 0.013 mM), but does not methylate GTGG, GmAmAG or GAGA
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q134M6
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Deinococcus radiodurans RI, Neisseria lactamica ST640 Sange
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
B6IW55
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Bacillus sp. NEB686
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Deinococcus radiodurans NEB479
C0LTP9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme recognizes and methylates GAGG (100% activity, Km 0.00522 mM), GGAG (about 48% activity, Km 0.017 mM) and GAAG (about 30% activity, Km 0.013 mM), but does not methylate GTGG, GmAmAG or GAGA
-
-
-
additional information
?
-
Q1QGU9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Synechococcus sp. PCC 7002 PR-6
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A5WI42
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP8
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
P14751
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is involved in cell cycle regulation of Caulobacter crescentus
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a critical regulator of bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is a member of a restriction-modification system, R-M system, plasmid DNA, and hemi- or unmethylated duplex DNA, preference for hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
enzyme is not important in mismatch repair and for adherence of the bacterium to host cells, e.g. HEp-2 cells
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
P04392
methylation of DNA-adenine at certain GATC sites plays a pivotal role in bacterial and phage gene expression as well as in bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
methylation of the site GATCprox proximal to the promotor is required for transition to the phase On state by specifically blocking PapI-dependent binding of Lrp to promotor proximal sites 4-6, expression of pyelonephritis-associated pili, i.e. Pap, in uropathogenic Escherichia coli is epigenetically controlled by a reversible OFF to ON switch, overview
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
specific target sequence is GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
the enzyme is cell cycle regulated and essential for viability
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-
unmethylated or hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP9, -
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q6NFX9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A1U7P0
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A7HWD2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q30TC2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q5LS45
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam belongs to the alpha-class of adenine methyltransferases and transfers a methyl group to the N-6 position of the adenine in the DNA sequence 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam catalyzes postreplicative methylation of adenosine moieties located in 5'-GATC-3' sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
D5FM16, -
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates a GATC recognition site
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates the adenine residue in GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
P0AEE9
Dam methylates the N-6 position of adenine in the DNA sequence 5'-GATC-3' and is highly processive, catalyzing multiple methyltransfers prior to dissociating from the DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
Dam methylates the N-6 position of the adenine in the sequence 5'-GATC-3', Dam shows a dramatic preference for the in vitro methylation of certain GATC sequences in plasmids and PCR-derived DNAfragments
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
DNA adenine methyltransferase methylates the N6 positions of adenines in the sequence 5'-GATC-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
EcoP15I MTase adds a methyl group to the second adenine in the recognition sequence 5'-CAGCAG-3' in the presence of S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
M1.MboII modifies the last adenine in the recognition sequence 5'-GAAGA-3' to N6-methyladenine
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B2MU09
MmeI modifies only the adenine in the top strand, 5-TCCRAC-3, MmeI endonuclease activity is blocked by this top strand adenine methylation and is unaffected by methylation of the adenine in the complementary strand, 5-GTYGGA-3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
recognition sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GANTC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GANTC, CcrM is more active on hemimethylated than unmethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the DNA target sequence is GATC, the natural substrate for the enzyme is hemimethylated DNA, where one strand is methylated and the other is not
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
the wild type enzyme shows target specificity for GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Corynebacterium striatum M82B
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Helicobacter pylori NSH57
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Deinococcus radiodurans RI
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Amoeba proteus D
-
the sams1 gene is methylated at an internal adenine residue of GATC site in symbiont-bearing amoebae but not in symbiont-free amoebae, suggesting that the modification may have caused the inactivation of sams1 at the transcriptional level
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Edwardsiella tarda TXD1
D5FM16
Dam catalyzes the methylation of N-6 of the adenine residue in GATC sequences
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Neisseria lactamica ST640 Sange
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Neisseria gonorrhoeae FA1090
-
the specific sequence recognized by M.NgoAXP is 5'-CCACC-3', in which the adenine residue is methylated
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Bacillus sp. NEB686
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Deinococcus radiodurans NEB479
C0LTP9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Synechococcus sp. PCC 7002 PR-6
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
Geobacillus stearothermophilus SE-589
-
the enzyme modifies adenine in the nickase recognition site 5'-GAGTC-3' and is specific for 5'-GASTC-3' substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
-
-
-
-
?
additional information
?
-
-
S-adenosyl-L-methionine plays a crucial role in reorientation of the enzyme in DNA with mutationally altered Ade residues to 2-aminopurine, overview
-
-
-
additional information
?
-
-
the enzyme is part of the type II restriction-modification system AhdI, overview
-
-
-
additional information
?
-
-
Dam-dependent regulation of secretion of pathogenicity island 1 is transmitted via transcriptional regulator HilD
-
-
?
additional information
?
-
B2MU09
MmeI does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
no detectable activity on the single-stranded form of the phage PhiX174 DNA is observed with M1.MboII, double-stranded DNA is less efficiently methylated than pUC18 DNA
-
-
-
additional information
?
-
-
plastid transcription is largely insensitive to adenine methylation of the plastid DNA
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP9, -
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q6NFX9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A1U7P0
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q1QGU9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A7HWD2
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP8
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A5WI42
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
B6IW55
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q134M6
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q30TC2
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q5LS45
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
-
the preferred substrate consists of the annealed product of oligonucleotides 5'-CATTTACTTGATCCGGTATGC-3' and 5'-GCATACCGGATCAAGTAAATG-3', while the nonpreferred substrate consists of the annealed product of oligonucleotides 5'-CATTTAGACGATCTTTTATGC-3' and 5'-GCATAAAAGATCGTCTAAATG-3'
-
-
-
additional information
?
-
-
the wild type Dam shows no detectable activity at GATT sites
-
-
-
additional information
?
-
Q9Y5N5
purified recombinant enzyme, in the presence of S-adenosyl-L-methionine and other cofactors, is unable to methylate trivalent inorganic arsenic or monomethylarsonous acid
-
-
-
additional information
?
-
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q134M6
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Deinococcus radiodurans RI, Neisseria lactamica ST640 Sange
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
B6IW55
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Bacillus sp. NEB686
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Deinococcus radiodurans NEB479
C0LTP9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Q1QGU9
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
Synechococcus sp. PCC 7002 PR-6
-
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
A5WI42
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
additional information
?
-
C0LTP8
the enzyme does not produce any detectable N4-cytosine methylation
-
-
-
0.000017
-
DNA
-
pH 8.0, 37°C
0.00000000000001
-
DNA adenine
-
His-tagged wild-type
0.00000000000002
-
DNA adenine
-
mutant S124D
0.0000036
-
DNA adenine
-
-
0.000007
-
DNA adenine
P0AEE9
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
P0AEE9
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
P0AEE9
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
0.0000174
-
DNA adenine
-
-
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
P0AEE9
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
0.0000255
-
DNA adenine
-
-
0.000027
-
DNA adenine
P0AEE9
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
P0AEE9
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
P0AEE9
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
P0AEE9
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
P0AEE9
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
P0AEE9
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
P0AEE9
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
P0AEE9
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
0.00009
-
DNA adenine
-
-
0.00009
-
DNA adenine
P23192
-
0.00009
-
DNA adenine
P04043
-
0.000091
-
DNA adenine
-
-
0.000122
-
DNA adenine
-
-
0.00015
-
DNA adenine
-
-
0.00015
-
DNA adenine
P23192
-
0.00015
-
DNA adenine
P04043
-
0.00015
-
DNA adenine
-
at pH 5.5 and 37°C
0.000182
-
DNA adenine
-
-
0.00022
-
DNA adenine
P0AEE9
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
0.00027
-
DNA adenine
-
-
0.0003
-
DNA adenine
-
in 50 mM NaCl, 50 mM HEPES, 1 mM EDTA, pH 7.5, temperature not specified in the publication
0.0006
-
DNA adenine
P14385
-
0.00083
-
DNA adenine
-
-
0.00091
-
DNA adenine
-
-
0.00195
-
DNA adenine
-
-
0.00195
-
DNA adenine
P23192
-
0.00195
-
DNA adenine
P04043
-
0.0001
-
S-adenosyl-L-methionine
-
-
0.0001
-
S-adenosyl-L-methionine
-
-
0.00086
-
S-adenosyl-L-methionine
-
mutant S124D
0.0018
-
S-adenosyl-L-methionine
-
-
0.0027
-
S-adenosyl-L-methionine
-
His-tagged wild-type
0.0037
-
S-adenosyl-L-methionine
P14385
-
0.0056
-
S-adenosyl-L-methionine
-
-
0.0058
-
S-adenosyl-L-methionine
-
in 33 mM Tris-acetate, pH 7.9, 10 mM magnesium acetate, 66 mM potassium acetate, 1 mM dithiothreitol, at 55°C
0.012
-
S-adenosyl-L-methionine
-
in 50 mM NaCl, 50 mM HEPES, 1 mM EDTA, pH 7.5, temperature not specified in the publication
0.0122
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S-adenosyl-L-methionine
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0.0000000011
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T4 gt- dam- DNA
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nonglucosylated unmethylated T4 gt- dam- DNA
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0.0000000011
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T4 gt- dam- DNA
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nonglucosylated unmethylated T4 gt- dam- DNA
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0.0000098
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T7 DNA adenine
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in 33 mM Tris-acetate, pH 7.9, 10 mM magnesium acetate, 66 mM potassium acetate, 1 mM dithiothreitol, at 55°C
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0.0199
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DNA adenine
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in 10 mM Tris/HCl, pH 8.0, 5 mM 2-mercaptoethanol, at 37°C
additional information
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additional information
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Km-values for oligonucleotide substrates containing the native or modified recognition site: 5.3-12.9 nM
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additional information
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additional information
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turnover numbers for the canonical 14-mer duplex and various substituted duplexes
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additional information
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additional information
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the T4 Dam methylation reaction cannot be explained by a simple Michaelian scheme
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additional information
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additional information
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Km-values fpr 14-mers and various substituted duplexes
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additional information
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additional information
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detailed kinetics, enzyme shows a simple kinetic behaviour towards a 20mer duplex DNA, random bi bi mechanism
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additional information
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additional information
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steady-state and pre-steady-state kinetics, single turnover methylation kinetics
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additional information
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additional information
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detailed steady-state and pre-steady-state kinetics for different methylation sites
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additional information
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additional information
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kinetics, ordered bi bi kinetic mechanism, cooperative binding of 2 molecules of enzyme per DNA is required for activity
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additional information
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additional information
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steady-state kinetics, kinetic mechanism, thermodynamics
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additional information
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additional information
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quantitative stopped-flow kinetics using 2-aminopurine as a probe to detect base flipping, wild-type and mutant enzymes
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additional information
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additional information
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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
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additional information
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additional information
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detailed kinetics for diverse substrate duplexes and methylation sites
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D71A
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phenotype of native Dam
D71A
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phenotype of native Dam
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D181A
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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
E200G
P10484
produces wild-type phenotype
H171A
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the mutant is almost as active as the wild type enzyme
H335A
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the mutant is catalytically inactive and binds to DNA more tightly than the wild type enzyme
K139A
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site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
K139A
P0AEE9
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
K184N
P10484
restriction-deficiency
K9A
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the mutant shows low activity and loss of recognition of Gua1; the mutant shows strongly reduced methylation activity towards the sequence GATC
K9A/Y138R
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the double mutant is highly active and specific
L122A
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site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme
L122A
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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
N120A
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site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme
N120A
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loses its p-stacking with Gua1, shows small changes in specificity factor S1
N120S
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site-directed mutagenesis, slightly reduced activity compared to the wild-type enzyme, DNA binding is similar to the wild-type enzyme
N126A
P0AEE9
the mutant displays decreased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
N126A
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the mutant shows large reduction in methylation activity
N132A
P0AEE9
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
P134A
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site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
P134A
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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
P134G
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site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
P134G
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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
P218S
P10484
loss of ability to bind DNA
R116A
P0AEE9
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
R124A
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site-directed mutagenesis, over 100fold reduced activity and about 10fold reduced DNA binding compared to the wild-type enzyme
R124A
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overall reduction in catalytic activity but methylates the near-cognate substrates GATT and GATG faster than the canonical GATC, no base-flipping signal
R124R/P134A
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the mutant shows an increase of enzyme activity at GAAC sites
R124S/P134A
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the mutant shows an increase of enzyme activity at GATG sites
R124S/P134S
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the mutant shows an increase of enzyme activity at GATT sites
R124S/P134S/K139E/F159L/K241E
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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
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site-directed mutagenesis, DNA binding is similar to the wild-type enzyme
R137A
P0AEE9
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
R163Q
P10484
produces wild-type phenotype
R95A
P0AEE9
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
S154P
P10484
produces wild-type phenotype
S188A
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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
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site-directed mutagenesis, mutant shows 75% of wild-type enzyme activity
Y119A
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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
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site-directed mutagenesis, DNA binding is similar to the wild-type enzyme
Y138A
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loses its interaction with the O6 atom of Gua1, shows small changes in specificity factor S1
Y138R
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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
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site-directed mutagenesis, mutant shows 1.7% of wild-type enzyme activity
D194A
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the Hia5 mutant shows loss of DNA MTase activity
D194A
G9C944
the Hia5 mutant shows loss of DNA MTase activity
D194A
Haemophilus influenzae biotype aegyptius ATCC 11116, Haemophilus influenzae Rd (FluMu)
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the Hia5 mutant shows loss of DNA MTase activity
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C54G
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the mutant has wild type activity
Y32L
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the mutant binds to S-adenosyl-L-methionine as efficiently as wild type enzyme but is catalytically inactive
C54G
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the mutant has wild type activity
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F195S
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the mutant is not able to bind to the S-adenosyl-L-methionine as effectively as the wild type enzyme and is catalytically inactive
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D194A
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the Hia5 mutant shows loss of DNA MTase activity
D194A
Neisseria meningitidis Z2491 (Pnme1)
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the Hia5 mutant shows loss of DNA MTase activity
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L72P
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site-directed mutagenesis, altered secondary structure, the active site is pushed away from the ligand binding site, especially by altered position of Trp84
E76A
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phenotype of native Dam
additional information
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strain SSU dam chromosomal deletion mutant, is not viable
additional information
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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
E76A
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phenotype of native Dam
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additional information
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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; strain SSU dam chromosomal deletion mutant, is not viable
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L175P
P10484
slightly lowers the ability of the restriction enzyme to cut DNA
additional information
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construction of a ccrM null mutant
additional information
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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
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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
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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
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complementation of the Escherichia coli dam mutant strain GM2163 with the Yersinia enterocolitica dam gene
additional information
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Dam mutant, no global changes in transcription
F195S
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the mutant is not able to bind to the S-adenosyl-L-methionine as effectively as the wild type enzyme and is catalytically inactive
additional information
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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
Y32L
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the mutant binds to S-adenosyl-L-methionine as efficiently as wild type enzyme but is catalytically inactive
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additional information
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site-directed mutagenesis at the dimer interface drastically affects enzyme activity in addition to the oligomeric status of the enzyme
S124D
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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
additional information
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deletion of the ORF does not affect cell viability
additional information
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dam mutant, a CamS SmR SpR exconjugant can not be obtained
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History
Enzyme Nomenclature
----S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
-485572, 485578, 658407, 659422, 659715, 659920, 660031, 664054, 671878, 676746, 702115, 702334, 702628, 703200, 703347, 703765, 704168, 705127, 705175, 713742, 719096, 720029--
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