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Information on EC 2.1.1.72 - site-specific DNA-methyltransferase (adenine-specific) and Organism(s) Cereibacter sphaeroides and UniProt Accession P14751

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Cereibacter sphaeroides
UNIPROT: P14751 not found.
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Word Map
The taxonomic range for the selected organisms is: Cereibacter sphaeroides
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
dam mtase, dna adenine methyltransferase, m6a methyltransferase, dam methylase, dna adenine methylase, m.taqi, t4 dam, specific methyltransferase, m.ecorv, ecodam, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DNA adenine MTase
-
RsrI N6-adenine DNA methyltransferase
-
adenine-N6 MTAse
-
-
-
-
DNA-[N6-adenine]-methyltransferase
-
-
-
-
modification methylase
-
-
-
-
N6-adenine DNA -methyltransferase
-
-
-
-
restriction-modification system
-
-
-
-
RsrI N6-adenine DNA methyltransferase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
69553-52-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-methylaminopurine
show the reaction diagram
S-adenosyl-L-methionine + DNA adenine
S-adenosyl-L-homocysteine + DNA 6-methyladenine
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sinefungin
binding structure
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000000000001 - 0.00000000000002
DNA adenine
0.00086 - 0.0027
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
DNA adenine
-
0.000167 - 0.0035
DNA adenine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MTR1_CERSP
319
0
35655
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
-
gel filtration, mutant S124D
74400
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
dimerizes at high protein concentrations
dimer
-
gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L72P
site-directed mutagenesis, altered secondary structure, the active site is pushed away from the ligand binding site, especially by altered position of Trp84
S124D
-
reduced solubility of the protein relative to that of the wild-type enzyme, fails to crystallize under the same conditions used to crystallize wild-type enzyme, is active and shows a non-linear dependence of activity on enzyme concentration similar as wild-type
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant purified by nickel-ion metal-affinity chromatography, more than 95% pure
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the apo-enzyme mutant L72P as His-tagged enzyme
mutant expressed in Escherichia coli BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
potential targets for both vaccines and antimicrobials
analysis
-
the dimer stabilizes and enhances site-specific DNA-binding by the MTase, because the DNA-binding site may require an interfacial structure formed by both monomers, role of Type II MTases as defense systems against phage
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thomas, C.B.; Scavetta, R.D.; Gumport, R.I.; Churchill, M.E.
Structures of liganded and unliganded RsrI N6-adenine DNA methyltransferase: a distinct orientation for active cofactor binding
J. Biol. Chem.
278
26094-26101
2003
Cereibacter sphaeroides (P14751)
Manually annotated by BRENDA team
Bheemanaik, S.; Reddy, Y.V.; Rao, D.N.
Structure, function and mechanism of exocyclic DNA methyltransferases
Biochem. J.
399
177-190
2006
Enterobacter cloacae, Caulobacter vibrioides, Escherichia coli, Klebsiella pneumoniae, Streptococcus pneumoniae (P04043), Tequatrovirus T4 (P04392), Thermus aquaticus (P14385), Cereibacter sphaeroides (P14751), Moraxella bovis (P23192)
Manually annotated by BRENDA team
Thomas, C.B.; Gumport, R.I.
Dimerization of the bacterial RsrI N6-adenine DNA methyltransferase
Nucleic Acids Res.
34
806-815
2006
Cereibacter sphaeroides
Manually annotated by BRENDA team