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

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, dsDNA viruses, no RNA stage

EC NUMBER
COMMENTARY
2.1.1.72
-
RECOMMENDED NAME
GeneOntology No.
site-specific DNA-methyltransferase (adenine-specific)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
-
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
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 + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
reaction scheme and random bi bi kinetic mechanism
-
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
two distinct stages of methylation under single turnover conditions
-
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
ordered bi bi mechanism during progressive methylation process
-
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
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 + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
ordered bi bi mechanism with S-adenosyl-L-methionine binding first, fast methyl transfer, slow product release
-
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
D181 and Y184 are essential for activity
-
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
molecular mechanism, effector action of substrates, progressive methylation of extended DNA containing more than one methylation site
-
S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
active site structure, enzyme-methyl donor product interactions, substrate binding mechanism and conformational changes, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenine methyltransferase
-
-
adenine N6-methyltransferase
-
-
adenine-N6 DNA methyltransferase
-
-
adenine-N6 MTAse
-
-
-
-
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
-
-
CcrM methylase
-
-
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
D5FM16
-
Dam
Edwardsiella tarda TXD1
D5FM16
-
-
Dam
P0AEE9
-
Dam DNA-(adenine-N6)-methyltransferase
-
-
Dam DNA-(adenine-N6)-MTase
-
-
Dam methylase
-
-
Dam methylase
-
-
Dam methylase
-
-
Dam MTase
P04392
-
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
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 MTase
-
-
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-[N6-adenine] MTase
-
-
DNA-[N6-adenine]-methyltransferase
-
-
-
-
DNA:m6A MTase
Q9L8Y0
-
DNAm6A MTase
-
-
DNAm6A MTase
Haemophilus influenzae biotype aegyptius ATCC 11116
G9C944
-
-
DNAm6A MTase
Haemophilus influenzae Rd (FluMu)
-
-
-
DNAm6A MTase
-
-
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
-
-
EcoP15I
-
-
EcoP15I MTase
-
-
EcoRII DNA methyltransferase
-
-
gamma-adenine MTase
-
-
Hia5 protein
Haemophilus influenzae biotype aegyptius ATCC 11116
G9C944
-
-
Hin1523 protein
-
-
Hin1523 protein
Haemophilus influenzae Rd (FluMu)
-
-
-
HP0050 methyltransferase
-
-
HP0050 methyltransferase
-
-
-
HP0593 DNA-(N6-adenine)-methyltransferase
-
-
HP0593 DNA-(N6-adenine)-methyltransferase
-
-
-
HP0593 MTase
-
-
HP0593 MTase
-
-
-
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
-
-
KpnI MTase
-
-
M.BstZ1II
Geobacillus stearothermophilus 14P
Q32WE7
-
-
M.Csp231I
Citrobacter sp.
Q32WH2
-
M.Csp231I
Q32WH2
-
-
M.EcoKCcrM
-
-
M.EcoRI
-
-
M.EcoRII
-
-
M.EcoRV
-
-
M.EfaBMDam
Q9L8Y0
-
M.HpyAXII
-
-
M.HpyAXII
Helicobacter pylori NSH57
-
-
-
M.MboIIA
-
-
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
Q32WH2
-
-
MTase
Geobacillus stearothermophilus 14P
Q32WE7
-
-
N-6 adenine-specific DNA methyltransferase 1
Q9Y5N5
-
N6 adenine methyltransferase
-
-
N6 adenine methyltransferase
-
-
-
N6 adenine MTase
-
-
N6 adenine MTase
-
-
N6 adenine MTase
-
-
-
N6-Ade MTase
-
-
N6-adenine DNA -methyltransferase
-
-
-
-
N6-adenine methyltransferase
Q9L8Y0
-
N6AMT1
Q9Y5N5
-
NgoAXPMod subunit
-
-
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
-
Nme1821 protein
-
-
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
-
-
T4 Dam DNA methyltransferase
-
-
T4 Dam DNA-(N6-adenine)-methyltransferase
-
-
T4 Dam MTase
-
-
T4 DNA-adenine methyltransferase
-
-
T4Dam DNA-[N6-adenine] MTase
-
-
T4DNA-(N6-adenine)-methyltransferase
-
-
type IC M.EcoR124I DNA methyltransferase
P10484
-
VspI methyltransferase
-
-
Wadmtase
-
-
modification methylase
-
-
-
-
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
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
-
CAS REGISTRY NUMBER
COMMENTARY
69553-52-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isolate SSU
-
-
Manually annotated by BRENDA team
strain D and xD
-
-
Manually annotated by BRENDA team
Amoeba proteus D
strain D and xD
-
-
Manually annotated by BRENDA team
strain NEB686
-
-
Manually annotated by BRENDA team
Bacillus sp. NEB686
strain NEB686
-
-
Manually annotated by BRENDA team
Citrobacter sp.
strain RFL231
UniProt
Manually annotated by BRENDA team
strain RFL231
UniProt
Manually annotated by BRENDA team
Corynebacterium striatum M82B
strain M82B
-
-
Manually annotated by BRENDA team
strain NEB479
UniProt
Manually annotated by BRENDA team
Deinococcus radiodurans NEB479
strain NEB479
UniProt
Manually annotated by BRENDA team
Deinococcus radiodurans RI
strain RI
-
-
Manually annotated by BRENDA team
strain TXD1
UniProt
Manually annotated by BRENDA team
Edwardsiella tarda TXD1
strain TXD1
UniProt
Manually annotated by BRENDA team
derivatives of strain AB1157
-
-
Manually annotated by BRENDA team
gene yhdJ or ccrM
-
-
Manually annotated by BRENDA team
M.EcoRV, M.EcoRI, Escherichia coli dam methyltransferase and M.FokI enzyme
-
-
Manually annotated by BRENDA team
strains GHE131, GHE134, GHE135 and GM2163
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus 14P
strain 14P
UniProt
Manually annotated by BRENDA team
Geobacillus stearothermophilus SE-589
strain SE-589
-
-
Manually annotated by BRENDA team
Haemophilus influenzae biotype aegyptius ATCC 11116
Hia5 protein
UniProt
Manually annotated by BRENDA team
Haemophilus influenzae Rd (FluMu)
-
-
-
Manually annotated by BRENDA team
diverse strains, overview
-
-
Manually annotated by BRENDA team
strain NSH57
-
-
Manually annotated by BRENDA team
Helicobacter pylori NSH57
strain NSH57
-
-
Manually annotated by BRENDA team
strain ATCC 10900
-
-
Manually annotated by BRENDA team
strain FA1090
-
-
Manually annotated by BRENDA team
Neisseria gonorrhoeae FA1090
strain FA1090
-
-
Manually annotated by BRENDA team
strain ST640 Sange
-
-
Manually annotated by BRENDA team
Neisseria lactamica ST640 Sange
strain ST640 Sange
-
-
Manually annotated by BRENDA team
strain Z2491
-
-
Manually annotated by BRENDA team
Neisseria meningitidis Z2491 (Pnme1)
-
-
-
Manually annotated by BRENDA team
Peridinium triquetrum
-
-
-
Manually annotated by BRENDA team
strain OM2164
UniProt
Manually annotated by BRENDA team
strain OM2164
UniProt
Manually annotated by BRENDA team
strain PRwf-1
UniProt
Manually annotated by BRENDA team
strain PRwf-1
UniProt
Manually annotated by BRENDA team
strain DSS-3
UniProt
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
serovar Typhimurium, ATCC 14028
-
-
Manually annotated by BRENDA team
Synechococcus sp. PCC 7002 PR-6
strain PR-6
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-
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
-
lack of Dam methylation causes partial attenuation upon intranasal or intraperitoneal inoculation of mice
malfunction
-
mutants lacking Dam methylase are not viable, Dam overproduction does not impair bacterial growth
malfunction
-
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
-
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
-
inactivation of the enzyme results in poor growth
malfunction
-
inactivation of the enzyme results in poor growth
-
malfunction
Helicobacter pylori NSH57
-
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
-
metabolism
Q9Y5N5
the enzyme potentially participates in arsenic metabolism in vivo
physiological function
-
MmeI DNA methylation prevents cleavage by MmeI
physiological function
-
DNA adenine methyltransferase is essential for proper DNA replication timing, gene regulation, and mismatch repair
physiological function
-
transcriptional inhibition by hemimethylation of genes dnaA, ccrM, and ctrA
physiological function
-
synthesis of P pili (pyelonephritis-associated protein) is subjected to phase variation and switching between On and Off states is controlled by Dam methylation, Dam methylation inhibits OxyR binding in the On state, Dam methylation of the upstream GATC site in agn43 increases transcription initiation, which occurs precisely at the G nucleotide of the GATC, finP transcription is activated by Dam methylation, Dam methylation does not regulate tir gene transcription nor tir mRNA stability
physiological function
-
Dam methylation of finP prevents repression by H-NS,methlation of traJ leads to activation of Lrp binding to the traJ UAS by strand-specific hemimethylation
physiological function
-
DNA adenine methylation is involved in Aeromonas hydrophila pathogenesis
physiological function
-
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. Dam methylation plays a role in enterohemorrhagic Escherichia coli by controlling the production of the virulence factor Shiga toxin 2
physiological function
-
Dam methylation may control the expression of virulence genes
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 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
D5FM16, -
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
Q9Y5N5
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
Edwardsiella tarda TXD1
-
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
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
P14751
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
GGGTGATCAGGG, CCCTGATCACCC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
GCGTGATCACGC
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
GGGTGATCAGGG+CCCTGATCACCC, annealed
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
lambda phage DNA
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in cell cycle regulation of Caulobacter crescentus
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
enzyme is a critical regulator of bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
specific target sequence is GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
the enzyme is cell cycle regulated and essential for viability
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
unmethylated or hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
enzyme methylates the first adenine in the sequence ATGCAT
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
methylation of target sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
P04392
specific methylation of target sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
P14751
substrate and product binding site structures
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
P14385
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
P0AEE8
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
P04043
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
C0LTP9, -
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
P23192
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
P10484
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q6NFX9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
A1U7P0
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
A7HWD2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q30TC2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q5LS45
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
Dam methylates a GATC recognition site
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
Dam methylates the adenine residue in GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
recognition sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
the DNA target sequence is GANTC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
the wild type enzyme shows target specificity for GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
129-mer DNA or pUC19 DNA are used as substrates
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
Corynebacterium striatum M82B
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Helicobacter pylori NSH57
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Neisseria meningitidis Z2491 (Pnme1)
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Deinococcus radiodurans RI
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
Neisseria lactamica ST640 Sange
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
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
show the reaction diagram
Bacillus sp. NEB686
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Deinococcus radiodurans NEB479
C0LTP9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Synechococcus sp. PCC 7002 PR-6
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
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
show the reaction diagram
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + oligodeoxynucleotide duplexes
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
substrate contains one single specific recognition site as 5'-GATC/5'-GATC, or modified variants
-
-
?
S-adenosyl-L-methionine + pUC19 DNA adenine
S-adenosyl-L-homocysteine + pUC19 DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
show the reaction diagram
Geobacillus stearothermophilus, Geobacillus stearothermophilus SE-589
-
-
-
-
?
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
?
-
Corynebacterium striatum M82B, Neisseria meningitidis Z2491
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
P14751
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme is involved in cell cycle regulation of Caulobacter crescentus
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
enzyme is a critical regulator of bacterial virulence
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
specific target sequence is GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
the enzyme is cell cycle regulated and essential for viability
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methylaminopurine
show the reaction diagram
-
unmethylated or hemimethylated DNA
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
C0LTP9, -
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q6NFX9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
A1U7P0
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
A7HWD2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q30TC2
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q5LS45
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
Dam methylates a GATC recognition site
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
Dam methylates the adenine residue in GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
-
recognition sequence GATC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
the DNA target sequence is GANTC
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the target sequence is 5'GATC3'
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
the wild type enzyme shows target specificity for GATC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Corynebacterium striatum M82B
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Helicobacter pylori NSH57
-
M.HpyAXII targets GTAC sites
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q134M6
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Deinococcus radiodurans RI
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
Neisseria lactamica ST640 Sange
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
B6IW55
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
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
show the reaction diagram
Bacillus sp. NEB686
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Deinococcus radiodurans NEB479
C0LTP9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Q1QGU9
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
Synechococcus sp. PCC 7002 PR-6
-
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
A5WI42
-
-
-
?
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
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
show the reaction diagram
C0LTP8
-
-
-
?
S-adenosyl-L-methionine + T7 DNA adenine
S-adenosyl-L-homocysteine + T7 DNA 6-methyladenine
show the reaction diagram
Geobacillus stearothermophilus, Geobacillus stearothermophilus SE-589
-
-
-
-
?
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
?
-
Corynebacterium striatum M82B, Neisseria meningitidis Z2491
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
2-3 mM required
Co2+
-
3fold stimulation of activity at 1 mM
Mg2+
-
2-3 mM required
Mg2+
-
no requirement for Mg2+
Mg2+
-
3.5fold stimulation of activity at 1 mM
Mn2+
-
5fold stimulation of activity at 1 mM
additional information
-
Ca2+, Zn2+, and Ni2+ ions do not affect the methylation activity of the enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
20mer fully methylated DNA duplex
-
product inhibition, noncompetitive against both S-adenosyl-L-methionine and 20mer unmethylated DNA duplex
-
5'-S-(2-carboxyethyl)-5'-thioadenosine
-
non-competitive inhibition
diethyl dicarbonate
-
the inactivation of the enzyme by diethyl dicarbonate is specific for histidine residues, pre-incubating the methylase with DNA is able to protect the enzyme from diethyl dicarbonate inactivation, hydroxylamine is unable to reverse the effect caused by diethyl dicarbonate
fully methylated sites 5'-GMTC/5'-GMTC DNA
-
the inhibition potential of fully methylated sites 5'-GMTC/5'-GMTC is much lower for a long DNA molecule compared to short single-site duplxes, enzyme does not dissociate from the DNA but continues one-sited methylation with linear diffusion, after which it rapidly reorientates itself and reconstitutes
-
K+
-
enzyme activity decreases 100fold in the presence of 100 mM K+
methylated DNA
-
competitive
-
methylated DNA
-
mixed-type inhibition against S-adenosyl-L-methionine, uncompetitive against unmethylated DNA
-
methylated duplex DNA
-
partial inhibition at high concentrations, mixed inhibition against un- or hemimethylated DNA, noncompetitive against S-adenosyl-L-methionine
-
Mg2+
-
Mg2+ inhibits methylation activity
Na+
-
enzyme activity decreases 100fold in the presence of 100 mM Na+
S-adenosyl-L-homocysteine
-
competitive
S-adenosyl-L-homocysteine
-
product inhibition
S-adenosyl-L-homocysteine
-
product inhibition, competitive against S-adenosyl-L-methionine, noncompetitive to 20mer unmethylated DNA duplex
S-adenosyl-L-homocysteine
-
competitive inhibition against S-adenosyl-L-methionine, noncompetitive against DNA
S-adenosyl-L-homocysteine
-
competitive against S-adenosyl-L-methionine, uncompetitive against DNA
S-adenosyl-L-homocysteine
-
strong inhibition
S-adenosyl-L-methionine
-
methylation reaction is inhibited above 0.0015 mM of S-adenosyl-L-methionine
Sinefungin
-
i.e. adenosyl ornithine, interaction mechanism with the enzyme, binding site structure, stabilization of the flipped adenine in presence of the inhibitor
Sinefungin
-
binding structure
Sinefungin
-
enzyme-DNA-inhibitor complex formation and structure
Sinefungin
P14385
competetive inhibitor
Mg2+
-
enzyme activity decreases in the presence of Mg2+ concentrations above 2.5 mM
additional information
-
inhibited at ionic strength greater than 0.2 M
-
additional information
-
reduction of methylation rate at high concentrations of the substrate 20-mer DNA duplex
-
additional information
-
enzyme is inhibited at ionic strength greater than 0.2 M
-
additional information
-
-
-
additional information
-
no substrate inhibition even at high concentrations, no formation of dead-end complexes
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
S-adenosyl-L-methionine
-
stimulates at increasing concentrations
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.7e-05
-
DNA
-
pH 8.0, 37C
1e-14
-
DNA adenine
-
His-tagged wild-type
2e-14
-
DNA adenine
-
mutant S124D
3.6e-06
-
DNA adenine
-
-
7e-06
-
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 22C
8e-06
-
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 22C
1e-05
-
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 22C
1.74e-05
-
DNA adenine
-
-
2.27e-05
-
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 22C
2.3e-05
-
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 22C
2.55e-05
-
DNA adenine
-
-
2.7e-05
-
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 22C
3.1e-05
-
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 22C
3.5e-05
-
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 22C
4.4e-05
-
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 22C
7.6e-05
-
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 22C
8.09e-05
-
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 22C
8.1e-05
-
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 22C
8.3e-05
-
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 22C
8.6e-05
-
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 22C
9e-05
-
DNA adenine
-
-
9e-05
-
DNA adenine
P23192
-
9e-05
-
DNA adenine
P04043
-
9.1e-05
-
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 37C
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 22C
0.00027
-
DNA adenine
-
-
0.0003
-
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
-
0.0008
-
DNA adenine
-
-
0.00083
-
DNA adenine
-
-
0.00091
-
DNA adenine
-
-
0.001
-
DNA adenine
-
-
0.00195
-
DNA adenine
-
-
0.00195
-
DNA adenine
P23192
-
0.00195
-
DNA adenine
P04043
-
0.0071
-
DNA adenine
-
-
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 55C
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
-
S-adenosyl-L-methionine
-
-
1.1e-09
-
T4 gt- dam- DNA
-
nonglucosylated unmethylated T4 gt- dam- DNA
-
1.1e-09
-
T4 gt- dam- DNA
-
nonglucosylated unmethylated T4 gt- dam- DNA
-
9.8e-06
-
T7 DNA adenine
-
in 33 mM Tris-acetate, pH 7.9, 10 mM magnesium acetate, 66 mM potassium acetate, 1 mM dithiothreitol, at 55C
-
0.0199
-
DNA adenine
-
in 10 mM Tris/HCl, pH 8.0, 5 mM 2-mercaptoethanol, at 37C
additional information
-
additional information
-
Km-values for oligonucleotide substrates containing the native or modified recognition site: 5.3-12.9 nM
-
additional information
-
additional information
-
turnover numbers for the canonical 14-mer duplex and various substituted duplexes
-
additional information
-
additional information
-
the T4 Dam methylation reaction cannot be explained by a simple Michaelian scheme
-
additional information
-
additional information
-
Km-values fpr 14-mers and various substituted duplexes
-
additional information
-
additional information
-
detailed kinetics, enzyme shows a simple kinetic behaviour towards a 20mer duplex DNA, random bi bi mechanism
-
additional information
-
additional information
-
steady-state and pre-steady-state kinetics, single turnover methylation kinetics
-
additional information
-
additional information
-
detailed steady-state and pre-steady-state kinetics for different methylation sites
-
additional information
-
additional information
-
kinetics, ordered bi bi kinetic mechanism, cooperative binding of 2 molecules of enzyme per DNA is required for activity
-
additional information
-
additional information
-
steady-state kinetics, kinetic mechanism, thermodynamics
-
additional information
-
additional information
-
quantitative stopped-flow kinetics using 2-aminopurine as a probe to detect base flipping, wild-type and mutant enzymes
-
additional information
-
additional information
-
pre-steady-state and steady-state kinetics, reaction kinetics with diverse DNA duplex substrates, role of individual elements of the recognition site, kinetic reaction scheme assuming that the enzyme is isomerized into a catalytically active form, overview
-
additional information
-
additional information
-
detailed kinetics for diverse substrate duplexes and methylation sites
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00033
-
DNA
-
substrate plasmid DNA, recombinant enzyme, pH 8.0, 37C
0.0011
-
DNA
-
substrate unmethylated duplex DNA, recombinant enzyme, pH 8.0, 37C
0.0056
-
DNA
-
substrate hemimethylated duplex DNA, recombinant enzyme, pH 8.0, 37C
0.0155
-
DNA
-
pH 8.0, 37C
9.6e-05
-
DNA adenine
-
-
0.000167
-
DNA adenine
-
mutant S124D
0.00017
-
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 22C
0.00033
-
DNA adenine
-
-
0.00033
-
DNA adenine
P23192
-
0.00033
-
DNA adenine
P04043
-
0.00072
-
DNA adenine
-
-
0.00072
-
DNA adenine
P23192
-
0.00072
-
DNA adenine
P04043
-
0.00082
-
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 22C
0.0009
-
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 22C
0.0015
-
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 22C
0.0022
-
DNA adenine
-
-
0.0022
-
DNA adenine
P23192
-
0.0022
-
DNA adenine
P04043
-
0.0025
-
DNA adenine
-
-
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 22C
0.0035
-
DNA adenine
-
His-tagged wild-type
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 22C
0.0038
-
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 22C
0.0041
-
DNA adenine
-
-
0.0047
-
DNA adenine
-
-
0.0053
-
DNA adenine
-
-
0.0055
-
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 22C
0.0056
-
DNA adenine
P23192
-
0.0056
-
DNA adenine
P04043
-
0.008
-
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 22C
0.0083
-
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 22C
0.013
-
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 22C
0.015
-
DNA adenine
-
20mer duplex, unligated, single-site, pH 8.0, 25C
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 22C
0.015
-
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 22C
0.019
-
DNA adenine
-
-
0.019
-
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 22C
0.02
-
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 22C
0.0208
-
DNA adenine
-
-
0.058
-
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 22C
0.094
-
DNA adenine
-
-
0.105
-
DNA adenine
-
-
0.11
-
DNA adenine
-
-
0.124
-
DNA adenine
-
-
0.14
-
DNA adenine
-
-
0.142
-
DNA adenine
-
-
0.16
-
DNA adenine
-
-
0.167
-
DNA adenine
-
-
0.203
-
DNA adenine
-
-
0.23
-
DNA adenine
-
-
0.25
-
DNA adenine
-
-
0.27
-
DNA adenine
-
-
0.3
-
DNA adenine
-
-
0.316
-
DNA adenine
-
-
0.33
-
DNA adenine
-
-
0.37
-
DNA adenine
-
-
0.447
-
DNA adenine
-
-
0.58
-
DNA adenine
-
-
0.73
-
DNA adenine
P14385
-
0.21
-
oligodeoxynucleotide duplexes 5'-GATC/5'-GATC
-
-
-
0.000118
-
S-adenosyl-L-methionine
-
-
0.00021
-
S-adenosyl-L-methionine
-
-
0.000248
-
S-adenosyl-L-methionine
-
-
0.00028
-
S-adenosyl-L-methionine
-
-
0.00117
-
S-adenosyl-L-methionine
-
-
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 55C
-
0.93
-
DNA adenine
-
-
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
-
turnover-numbers of the canonical 12-mer and 20 mers and for various defective 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
-
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
48.3
-
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 22C
10151
100
-
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 22C
10151
117
-
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 22C
10151
125
-
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 22C
10151
133
-
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 22C
10151
160
-
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 22C
10151
167
-
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 22C
10151
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 22C
10151
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 22C
10151
187
-
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 22C
10151
223
-
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 22C
10151
262
-
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 22C
10151
267
-
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 22C
10151
300
-
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 22C
10151
367
-
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 22C
10151
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.005
-
5'-S-(2-carboxyethyl)-5'-thioadenosine
-
-
0.00062
-
S-adenosyl-L-homocysteine
-
versus S-adenosyl-L-methionine, pH 8.0, 37C
0.0024
-
S-adenosyl-L-homocysteine
-
-
0.0024
-
S-adenosyl-L-homocysteine
-
-
4.6e-09
-
methylated DNA
-
-
-
additional information
-
additional information
-
detailed inhibition kinetics
-
additional information
-
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.005
-
5'-S-(2-carboxyethyl)-5'-thioadenosine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
8
-
-
assay at
8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.8
9
-
pH 2.8: about 65% of maximal activity, pH 9.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
37
-
-
assay at
37
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.8
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q9Y5N5
intercranial artery
Manually annotated by BRENDA team
Q32WE7
growth temperature for strain 14P is 55C
Manually annotated by BRENDA team
Geobacillus stearothermophilus 14P
-
growth temperature for strain 14P is 55C
-
Manually annotated by BRENDA team
Q9Y5N5
lowest expression
Manually annotated by BRENDA team
Q9Y5N5
highest expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Vibrio vulnificus (strain YJ016)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28000
-
-
sucrose density gradient sedimentation
28000
-
-
gel filtration
28400
-
-
gel filtration
30000
-
-
about, recombinant enzyme, gel filtration
30000
-
-
gel filtration, mutant S124D
30690
-
-
gel filtration, glycerol gradient centrifugation
30690
-
-
glycerol density gradient ultracentrifugation analysis
31200
-
-
sequence analysis
72000
-
-
gel filtration, the enzyme occurs as both monomer and dimer in solution
74400
-
-
gel filtration
77500
-
-
calculated from amino acid sequence
90000
-
-
recombinant enzyme, gel filtration
105100
-
-
calculated from amino acid sequence
144000
-
-
gel filtration, the enzyme occurs as both monomer and dimer in solution
additional information
-
-
sequence analysis of the gene for N6-methyladenosine DNA methylase
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 39000, SDS-PAGE
?
-
x * 30400, SDS-PAGE
?
-
1 * 34000, SDS-PAGE, 1 * 32662, sequence analysis
?
-
x * 40000, SDS-PAGE
?
G9C944
x * 34000, SDS-PAGE
?
-
x * 38000, SDS-PAGE
?
-
x * 33600, SDS-PAGE
?
-
1 * 34000, SDS-PAGE, 1 * 32662, sequence analysis
-
?
Haemophilus influenzae biotype aegyptius ATCC 11116
-
x * 34000, SDS-PAGE
-
?
Haemophilus influenzae Rd (FluMu)
-
x * 38000, SDS-PAGE
-
?
Neisseria meningitidis Z2491 (Pnme1)
-
x * 33600, SDS-PAGE
-
dimer
-
2 * 45000, recombinant enzyme, SDS-PAGE
dimer
-
in solution, but dissociate into monomers upon addition of the DNA
dimer
P23192
-
dimer
-
dimerizes at high protein concentrations
dimer
-
gel filtration
dimer
-
Dam dimerizes on short, synthetic DNA, resulting in enhanced catalysis, however, dimerization is not observed on large genomic DNA
homodimer
-
2 * 70600, the enzyme occurs as both monomer and dimer in solution, His-tagged enzyme, MALDI-TOF mass spectrometry
homodimer
-
2 * 70600, the enzyme occurs as both monomer and dimer in solution, His-tagged enzyme, MALDI-TOF mass spectrometry
-
monomer
-
enzyme and S-adenosyl-L-methionine form a catalytically active complex
monomer
-
1 * 32000, His-tagged enzyme, SDS-PAGE
monomer
-
1 * 72000, the enzyme occurs as both monomer and dimer in solution, His-tagged enzyme, gel filtration
monomer
-
1 * 32000, His-tagged enzyme, SDS-PAGE; 1 * 72000, the enzyme occurs as both monomer and dimer in solution, His-tagged enzyme, gel filtration
-
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
-
structure analysis of enzyme in ternary complex with partially and fully specific DNA and a methyl-donor analogue
additional information
-
secondary structure analysis
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
-
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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, 16C, 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 cognate DNA at 1.89 A resolution, in the presence of S-adenosyl-L-homocysteine
-
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
P43423
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 S-adenosyl-L-methionine, S-adenosyl-L-homocysteine and with the inhibitor sinefungin, at a resolution of 2.4 A
P14385
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
fully active
30
-
-
thermally inactivated within 20 min
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
ethanol (0.02% v/v) does not show any effect on enzyme
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by nickel affinity chromatography
-
Ni-NTA agarose column chromatography, gel filtration
-
recombinant enzyme by several chromatographic steps
-
by Ni2+-affinity chromatography and gel filtration
-
heparin-Sepharose column chromatography
-
Ni-NTA agarose column chromatography
-
phosphocellulose column chromatography and Blue Sepharose column chromatography
-
recombinant enzyme from overexpression
-
recombinant His-tagged enzyme from strain XL-2Blue
-
recombinant wild-type and mutant enzymes to over 95% purity
-
ammonium sulfate precipitation, phosphocellulose column chromatography, hydroxyapatite column chromatography, and Sephacryl S-200 gel filtration
-
by Ni-NTA affinity chromatography and gel filtration
P43423
Ni-NTA agarose column chromatography
-
Ni-NTA agarose column chromatography
G9C944
Ni-NTA column chromatography
-
Ni2+-NTA 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
-
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
-
partial purification using phosphocellulose column chromatography, hydroxylapatite column chromatography, CM-Sephadex gel filtration, and heparin agarose column chromatography
-
Ni-NTA agarose column chromatography
-
Ni-NTA agarose column chromatography
-
mutant purified by nickel-ion metal-affinity chromatography, more than 95% pure
-
partially purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene ahdI, genetic organization and regulation, modelling transcription activity of the PahdICR operon from the PahdIMS promoter, 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
-
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
-
expressed in Escherichia coli
-
expressed in Escherichia coli
-
subcloned into pET21b overexpression in Escherichia coli
-
genomic library construction, DNA and amino acid sequence determination and computational analysis, genetic organization, expression in Escherichia coli
Citrobacter sp.
Q32WH2
expressed in Escherichia coli
Q6NFX9
expressed in Escherichia coli
-
expressed in Escherichia coli; expressed in Escherichia coli
C0LTP9, -
expressed in dam-deficient Escherichia coli strain ER2925
D5FM16, -
cloning of T2 dam gene into expression vector pJW2, creation of T2-T4 hybrid genes in expression vector pJW2
-
the enzyme is subcloned into the plasmid expression vector pJW2
-
from transposon Tn1549, into plasmid pEfaORF18Ks, expressed in Escherichia coli GM2163 cells
Q9L8Y0
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli XL2 Blue cells
P0AEE9
expressed in Escherichia coli XL2-Blue cells
-
expressed in Escherichia coli XL2Blue cells
-
expressed in MCF-7 cells and in MCF-10A cells
-
expression of wild-type and mutant enzymes
-
gene yhdJ or ccrM, chromosomally encoded, DNA sequence determination and analysis, overvexpression decreases bacterial growth by altering cell division, cells show aberant morphology
-
His-tagged EcoDam expressed in HMS174(DE3) cells
-
mutant enzymes are expressed in Escherichia coli HMS174(DE3) cells
-
overexpression as His-tagged protein in strain XL-2Blue
-
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
-
expressed in Escherichia coli RRI cells
-
genomic library construction, DNA and amino acid sequence determination and computational analysis, genetic organization, expression in Escherichia coli
Q32WE7
into a pQE60 vector containing a C-terminal 6 x His tag and transformed into Escherichia coli M15 cells
P43423
expressed in Escherichia coli strain ER2566
-
expressed in Escherichia coli strain ER2566
G9C944
expressed in Escherichia coli BL21 (DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli ER2925(DE3) cells
-
gene jhp0085, DNA sequence determination
-
expression in Escherichia coli strain DH10B
-
expressed in Escherichia coli
A1U7P0
expressed in Escherichia coli
-
expressed in Escherichia coli strain ER2683
-
expressed in Escherichia coli ER2566 cells
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expressed in Escherichia coli GM2163 cells
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expressed in Escherichia coli
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expressed in Escherichia coli strain ER2566
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expressed in Escherichia coli
Q1QGU9
expressed in Escherichia coli
A7HWD2
putative Pfa MTase gene, subcloned into different expression vectors under regulatable promoters, these constructs separately transferred into Escherichia coli and yeast cells
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expressed in Escherichia coli
C0LTP8
expressed in Escherichia coli
A5WI42
expression of the apo-enzyme mutant L72P as His-tagged enzyme
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mutant expressed in Escherichia coli BL21(DE3)
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expressed in Escherichia coli
Q134M6
expressed in Escherichia coli
B6IW55
expressed in Escherichia coli
Q5LS45
expressed in Escherichia coli
Q30TC2
expressed in Escherichia coli
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expressed in Nicotiana tabacum
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expressed in Escherichia coli
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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
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Y107G
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inactive
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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Y107G
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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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
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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
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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
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potential targets for both vaccines and antimicrobials
medicine
Q9L8Y0
confers antibiotic resistance in clinical isolates, important determinant of bacterial virulence, may be transmitted by horizontal gene transfer, potential drug target
analysis
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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
P10484
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
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computational analysis of a published Dam knockout microarray alongside other publicly available
medicine
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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
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potential targets for both vaccines and antimicrobials
medicine
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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
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DNA adenine methyltransferase identification is a useful technology to map holocarboxylase synthetase binding sites in human chromatin
analysis
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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
medicine
P14385
potential targets for both vaccines and antimicrobials
analysis
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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
medicine
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Dam is essential for viability and mediates virulenc
medicine
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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; 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
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additional information
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DNA-[adenine] MTase pseudogene, ORF encodes a protein exhibiting a high degree of homology to the putative Saccharomyces cerevisiae MTase
additional information
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potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
medicine
-
potential targets for both vaccines and antimicrobials
additional information
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transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
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potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
pharmacology
-
enzyme is a target for antibiotics and antbiotic development
additional information
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potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
medicine
-
potential targets for both vaccines and antimicrobials
additional information
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potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
medicine
P23192
potential targets for both vaccines and antimicrobials
additional information
Oxytricha fallax, Paramecium aurelia, Peridinium triquetrum
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transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
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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
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potential ORF that appears to code for DNA-[adenine] MTase, seems to be a pseudogene
medicine
-
potential targets for both vaccines and antimicrobials
additional information
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contains complete DNA-[adenine] MTase-like ORF but the DNA-[adenine] MTase like gene is a pseudogene, no evidence of DNA-[adenine] methylation
medicine
P04043
potential targets for both vaccines and antimicrobials
additional information
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transcriptionally active macronuclear DNA contains N6-methyladenine
additional information
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high degree of homology to the prokaryote enzymes