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Information on EC 2.1.1.113 - site-specific DNA-methyltransferase (cytosine-N4-specific) and Organism(s) Bacillus amyloliquefaciens and UniProt Accession P23941

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Bacillus amyloliquefaciens
UNIPROT: P23941 not found.
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The taxonomic range for the selected organisms is: Bacillus amyloliquefaciens
The enzyme appears in selected viruses and cellular organisms
Synonyms
modification methylase, m.pvuii, m.ngomxv, m.bcnia, m.pspgi, sll0729, m.bcnib, m2.mboii, n4-cytosine methyltransferase, m.smai, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BamHI [cytosine-N4] MTase
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cytosine-N5-methyltransferase
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DNA-(N4-cytosine)-methyltransferase
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DNA[cytosine-N4]methyltransferase
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m4C-forming Mtase
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modification methylase
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N4mC MTase
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restriction-modification system
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N4-methylcytosine
show the reaction diagram
the product inhibition pattern consistent with a steady-state random bi-bi mechanism in which the dominant order of substrate binding and product release: S-adenosyl-L-methionine, methylated DNA, DNAMe, S-adenosyl-L-homocysteine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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CAS REGISTRY NUMBER
COMMENTARY hide
169592-50-1
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90371-46-3
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92228-39-2
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98982-80-0
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99637-25-9
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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]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
show the reaction diagram
target sequences
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?
S-adenosyl-L-methionine + 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5
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show the reaction diagram
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?
S-adenosyl-L-methionine + 5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'
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show the reaction diagram
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?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
show the reaction diagram
additional information
?
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integrity of ATCC sequence is critical
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
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competitive with regard to S-adenosylmethionine and non-competitive with respect to unmethylated 20-mer duplex
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00035
5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5'
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0.000196
5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'
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0.00122 - 0.0016
S-adenosyl-L-methionine
additional information
additional information
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Km-values for several oligonucleotides
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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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?
MTB1_BACAM
423
0
49136
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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enzyme in a free state exists as a dimer. Introduction of substoichiometric amounts of DNA into the reaction mixture results in pronounced multimerization of the enzyme. However, addition of SAM in saturating concentration at an excess of the oligonucleotide duplex over BamHI Mtase converts most of the enzyme into a monomeric state
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Malygin, E.G.; Zinoviev, V.V.; Evdokimov, A.A.; Lindstrom, W.M., Jr.; Reich, N.O.; Hattman, S.
DNA-(cytosine-N4)- and (adenine-N6)-methyltransferases have different kinetic mechanisms but the same reaction route: a comparison of M.BamHI and T4 Dam
J. Biol. Chem.
20
1-31
2003
Bacillus amyloliquefaciens
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Manually annotated by BRENDA team
Zinoviev, V.V.; Evdokimov, A.A.; Malygin, E.G.
DNA-(N4-Cytosine)-methyltransferase from Bacillus amyloliquefaciens: mechanism of action derived from steady-state kinetics
Mol. Biol. (Mosk.)
37
116-124
2003
Bacillus amyloliquefaciens
-
Manually annotated by BRENDA team
Lindstrom, W.M., Jr.; Malygin, E.G.; Ovechkina, L.G.; Zinoviev, V.V.; Reich, N.O.
Functional analysis of BamHI DNA cytosine-N4 methyltransferase
J. Mol. Biol.
325
711-720
2003
Bacillus amyloliquefaciens
Manually annotated by BRENDA team
Bujnicki, J.M.; Radlinska, M.
Molecular evolution of DNA-(cytosine-N4) methyltransferases: evidence for their polyphyletic origin
Nucleic Acids Res.
27
4501-4509
1999
Bacillus amyloliquefaciens (P18051), Bacillus amyloliquefaciens (P23941), Bacillus amyloliquefaciens H (P23941), Bacillus subtilis (O68556), Bacillus subtilis (Q45489), Cenarchaeum symbiosum, Cenarchaeum symbiosum (O74074), Cenarchaeum symbiosum A, Cenarchaeum symbiosum B (O74074), Citrobacter freundii (P14243), Citrobacter freundii (Q04845), Citrobacter freundii 4111 (Q04845), Citrobacter freundii RFL9 (P14243), Curtobacterium albidum (P71101), Geobacillus stearothermophilus (P70986), Geobacillus stearothermophilus JN2091 (P70986), Gordonia rubripertincta (O85488), Halobacterium phage phiH (Q38204), Helicobacter pylori, Helicobacter pylori (Q9ZLF1), Kocuria varians (P14244), Kocuria varians RFL19 (P14244), Lactobacillus phage phig1e, Methanocaldococcus jannaschii, Methanothermobacter thermautotrophicus (P29568), Methanothermobacter thermautotrophicus Z-250 (P29568), Methanothermobacter wolfeii (O59647), Neisseria gonorrhoeae (Q9AKV2), Neisseria gonorrhoeae ME11 (Q9AKV2), Proteus hauseri (P11409), Pseudomonas alcaligenes, Pseudomonas alcaligenes NCIB 986, Pyrococcus horikoshii, Pyrococcus horikoshii OT-3, Pyrococcus sp. (O93645), Saccharopolyspora sp. (O52711), Salmonella enterica subsp. enterica serovar Typhi, Salmonella enterica subsp. enterica serovar Typhi CT18, Serratia marcescens (P14230), Streptomyces caespitosus (O52692), Streptomyces fimbriatus (O52513), Trichormus variabilis (P0A462), Xanthomonas campestris pv. cyanopsidis (P30774), Xanthomonas citri pv. malvacearum
Manually annotated by BRENDA team
Malygin, E.G.; Ovechkina, L.G.; Zinoviev, V.V.; Lindstrem, U.M.; Reich, N.O.
DNA-(N4-cytosine)-methyltransferase from Bacillus amyloliquefaciens: kinetic and substrate-binding properties
Mol. Biol. (Mosk.)
35
35-44
2001
Bacillus amyloliquefaciens
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Manually annotated by BRENDA team
Zinoviev, V.V.; Yakishchik, S.I.; Evdokimov, A.A.; Malygin, E.G.; Hattman, S.
Symmetry elements in DNA structure important for recognition/methylation by DNA [amino]-methyltransferases
Nucleic Acids Res.
32
3930-3934
2004
Bacillus amyloliquefaciens
Manually annotated by BRENDA team