2.1.1.72: site-specific DNA-methyltransferase (adenine-specific)
This is an abbreviated version!
For detailed information about site-specific DNA-methyltransferase (adenine-specific), go to the full flat file.
Word Map on EC 2.1.1.72
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2.1.1.72
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mtases
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n6-methyladenosine
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endonuclease
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chromatin
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duplex
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s-adenosyl-l-methionine
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cytosine
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adomet
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bacteriophage
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mismatch
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damid
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unmethylated
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hemimethylated
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restriction-modification
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flip
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protein-dna
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methylation-sensitive
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s-adenosyl-l-homocysteine
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2-aminopurine
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methyltransferase-like
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epitranscriptomic
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writer
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m.hhai
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merip-seq
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mettl3-mediated
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alkbh5
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crescentus
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medicine
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prophage
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m6a-dependent
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adohcy
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m6a-modified
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gatatc
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n6-adenosine
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sinefungin
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n6-methylation
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extrahelical
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methyl-directed
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aquaticus
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analysis
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pharmacology
- 2.1.1.72
- mtases
- n6-methyladenosine
- endonuclease
- chromatin
- duplex
- s-adenosyl-l-methionine
- cytosine
- adomet
- bacteriophage
- mismatch
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damid
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unmethylated
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hemimethylated
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restriction-modification
- flip
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protein-dna
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methylation-sensitive
- s-adenosyl-l-homocysteine
- 2-aminopurine
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methyltransferase-like
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epitranscriptomic
-
writer
- m.hhai
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merip-seq
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mettl3-mediated
- alkbh5
- crescentus
- medicine
- prophage
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m6a-dependent
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adohcy
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m6a-modified
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gatatc
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n6-adenosine
- sinefungin
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n6-methylation
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extrahelical
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methyl-directed
- aquaticus
- analysis
- pharmacology
Reaction
Synonyms
6mA DNA methyltransferases, A1S_0222, AamA, acinetobacter adenine methyltransferase A, adenine methyltransferase, adenine methyltransferase 1, adenine N6-methyltransferase, adenine-(N6)-DNA methyltransferase, adenine-N6 DNA methyltransferase, adenine-N6 MTAse, AhdI methyltransferase, AMT1, ApyPI, AquII, AquIII, AquIV, BamHI MTase, BsbI, C18A3.1, CcrM, CcrM DNA adenine methyltransferase, CcrM methylase, CdpI, cell cycle-regulated DNA methyltransferase, cell cycle-regulated methyltransferase, cell-cycle regulating MTase, CstMI, Dam, Dam DNA-(adenine-N6)-methyltransferase, Dam DNA-(adenine-N6)-MTase, Dam methylase, Dam MTase, DAMT-1, DANN 6mA MTase, DNA 6mA methyltransferase, DNA adenine 5'-GATC-3' methylase, DNA adenine methylase, DNA adenine methyltransferase, DNA adenine methyltransferases, DNA adenine MTase, DNA adenine N6-methyltransferase, DNA adenine-N6 MTase, DNA methyltransferase, DNA MTase, DNA N-6 adenine methyltransferase, DNA N6 adenine methyltransferase 1, DNA N6-adenine methyltransferase, DNA [amino]-methyltransferase, DNA-(adenine N6)-methyltransferase, DNA-(adenine-N6)-methyltransferase, DNA-(adenine-N6-)-methyltransferase, DNA-(N6-adenine)-methyltransferase, DNA-adenine methyltransferase, DNA-[adenine] methyltransferase, DNA-[adenine] MTase, DNA-[N6-adenine] MTase, DNA-[N6-adenine]-methyltransferase, DNA:m6A MTase, DNAm6A MTase, DraRI, DrdIV, EcoDam, EcoDam DNA-[N6-adenine] MTase, EcoKDam, EcoP15I, EcoP15I MTase, EcoRII DNA methyltransferase, EcoRV, EcoVIII, gamma-adenine MTase, Hia5 protein, Hin1523 protein, HP0050 methyltransferase, HP0593 DNA-(N6-adenine)-methyltransferase, HP0593 MTase, HpyAXII, HpyIIIM, isospecific adenine DNA methyltransferase, isospecific DNA MTase, KpnI DNA methyltransferase, KpnI DNA-(N6-adenine)-methyltransferase, KpnI MTase, M-RsrI, M. TthP, M.Aba17978ORF8565P, M.AbaBGORF222P, M.AluBI, M.BseCI, M.BstZ1II, M.Csp231I, M.DpnM, M.EcaI, M.EcoKCcrM, M.EcoP15I, M.EcoRI, M.EcoRII, M.EcoRV, M.EcoVIII, M.EfaBMDam, M.HindIII, M.HpyAXII, M.KpnI, M.LlaCI, M.MboIIA, M.NgoAXP, M.RsrI, M.TaqI, M1.HpyAVI, M1.MboII, M2.BstSEI, m6A methyltransferase, MaqI, MettL3-MettL14 complex, MmeI, modification methylase, More, MTA1, MTA1c, MTase, N-6 adenine-specific DNA methyltransferase 1, N6 adenine methyltransferase, N6 adenine MTase, N6-Ade MTase, N6-adenine DNA -methyltransferase, N6-adenine methyltransferase, N6-adenine MTase, N6AMT1, N6_N4_MTase, NgoAXPMod subunit, NhaXI, NlaCI, Nme1821 protein, NmeAIII, Pho(M98A)Dam, PlaDI, PspOMII, PspPRI, RceI, restriction-modification system, RpaB5I, RsrI N6-adenine DNA methyltransferase, SdeAI, sequence-specific DNA adenine methyltransferase, specific methyltransferase, SpoDI, T4 Dam, T4 Dam (N6-Ade)-MTase, T4 Dam DNA methyltransferase, T4 Dam DNA-(N6-adenine)-methyltransferase, T4 Dam MTase, T4 DNA-adenine methyltransferase, T4Dam, T4Dam DNA-[N6-adenine] MTase, T4DNA-(N6-adenine)-methyltransferase, type IC M.EcoR124I DNA methyltransferase, VspI methyltransferase, Wadmtase, [N6-adenine] MTase
ECTree
2.1.1.72 site-specific DNA-methyltransferase (adenine-specific)Advanced search results
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results (Engineering
Engineering on EC 2.1.1.72 - site-specific DNA-methyltransferase (adenine-specific)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H317A
H336A
N330A
R272A
R302A
R350A
S315A
S315A/H317A/N330A/R350A
the mutant shows about 90% reduced methylation activity on double stranded DNA but no effect on S-adenosyl-L-methionione binding
L72P
site-directed mutagenesis, altered secondary structure, the active site is pushed away from the ligand binding site, especially by altered position of Trp84
S124D
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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
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
H335A
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the mutant is catalytically inactive and binds to DNA more tightly than the wild type enzyme
K139A
K9A
L122A
L122A/P134A
the variant methylates hemimethylated DNA with 80% of wild type activity
L122A/V133L
L122G
the mutant has no preference for hemimethylated substrate and is about 1.5fold more active than the wild type enzyme on the hemimethylated DNA substrate
L122I
the variant methylates hemimethylated DNA with 98% of wild type activity
L122S
the variant is able to sense the methylation status of the 5'-GATC-3' double-stranded target recognition site and methylates only hemimethylated DNA with 35-40% of wild type activity
L122T
the variant methylates hemimethylated DNA with 90% of wild type activity
L122V
the variant methylates hemimethylated DNA with 95% of wild type activity
L175P
slightly lowers the ability of the restriction enzyme to cut DNA
N120A
N120S
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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
N132A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
P134A
P134G
R116A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
R124A
R124S/P134S/K139E/F159L/K241E
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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
R95A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
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
V133A
the mutant shows increased activity with hemimethylated DNA compared to the wild type enzyme (160%)
V133I
the mutant shows decreased activity with hemimethylated DNA compared to the wild type enzyme
V133L
the mutant shows most strongly decreased activity with hemimethylated DNA compared to the wild type enzyme
V133S
the mutant shows strongly decreased activity with hemimethylated DNA compared to the wild type enzyme
Y119A
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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
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
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
Y32L
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the mutant binds to S-adenosyl-L-methionine as efficiently as wild type enzyme but is catalytically inactive
D194A
M98A
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to avoid expression of this truncated protein, a mutant form of the Pyrococcus horikoshii dam gene (M98A) is prepared by site-directed mutagenesis
additional information
H317A
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the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
H317A
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the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
H336A
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the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
H336A
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the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
N330A
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the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
N330A
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the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
R272A
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the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
R272A
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the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
R302A
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the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
R302A
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the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
R350A
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the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
R350A
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the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
S315A
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the mutant shows a severely decreased methylation activity compared to the wild type enzyme (below 10% activity)
S315A
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the mutant shows a severely decreased methylation activity (to less than 10%) compared to the wild type enzyme
K139A
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site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
K139A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
K9A
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the mutant shows strongly reduced methylation activity towards the sequence GATC
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
reduces the size of an aliphatic hydrocarbon side chain, is sufficient to convert EcoDam into a bona fide maintenance MTase with pronounced preference for hemimethylated DNA
L122A
the mutant is almost inactive on unmethylated DNA. The variant is able to sense the methylation status of the 5'-GATC-3' double-stranded target recognition site and methylates only hemimethylated DNA with 35-40% of wild type activity
L122A/V133L
the mutant shows increased activity with hemimethylated DNA compared to the wild type enzyme
L122A/V133L
the variant is able to sense the methylation status of the 5'-GATC-3' double-stranded target recognition site and methylates only hemimethylated DNA
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
loses its p-stacking with Gua1, shows small changes in specificity factor S1
N126A
the mutant displays decreased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
P134A
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site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
P134A
high catalytic activity, exhibits only a small reduction in the amplitude of the fluorescence change, but no detectable changes in the kinetics of base-flipping, induces base-flipping of the substrate with altered sequence at the third base-pair
P134A
the variant methylates hemimethylated DNA with 100% of wild type activity
P134G
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site-directed mutagenesis, 2-3fold reduced DNA binding compared to the wild-type enzyme
P134G
high catalytic activity, exhibits only a small reduction in the amplitude of the fluorescence change, but no detectable changes in the kinetics of base-flipping, induces base-flipping of the substrate with altered sequence at the third base-pair
R124A
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site-directed mutagenesis, over 100fold reduced activity and about 10fold reduced DNA binding compared to the wild-type enzyme
R124A
overall reduction in catalytic activity but methylates the near-cognate substrates GATT and GATG faster than the canonical GATC, no base-flipping signal
R137A
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site-directed mutagenesis, DNA binding is similar to the wild-type enzyme
R137A
the mutant displays increased kcat value compared to the wild type enzyme using the preferred DNA sequence 5'-GCATACCGGATCAAGTAAATG-3'
Y138A
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site-directed mutagenesis, DNA binding is similar to the wild-type enzyme
Y138A
loses its interaction with the O6 atom of Gua1, shows small changes in specificity factor S1
D194A
the Hia5 mutant shows loss of DNA MTase activity
D194A
Haemophilus influenzae biotype aegyptius ATCC 11116
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the Hia5 mutant shows loss of DNA MTase activity
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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
additional information
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strain SSU dam chromosomal deletion mutant, is not viable
additional information
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strain SSU dam chromosomal deletion mutant, is not viable
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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
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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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complementation of the Escherichia coli dam mutant strain GM2163 with the Yersinia enterocolitica dam gene
additional information
EcoDam K9A variant, shows slightly reduced catalytic activity and DNA binding, shows a loss of specificity at the first base-pair, unable to methylate any of the near-cognate sites, base-flipping of substrates carrying a base-pair substitution at the first position of the target site is more efficient than with wild-type
additional information
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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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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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mutational inactivation of the enzyme does not influence the mismatch repair, the adherence of the bacterium to host cells, e.g. HEp-2 cells, or the fitness of the bacterial cell
additional information
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site-directed mutagenesis at the dimer interface drastically affects enzyme activity in addition to the oligomeric status of the enzyme
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
