Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.21.3 - type I site-specific deoxyribonuclease and Organism(s) Escherichia coli and UniProt Accession Q07736

for references in articles please use BRENDA:EC3.1.21.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: Q07736 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolysed
Synonyms
restriction-modification system, ecoki, rease, ecor124i, type i restriction-modification system, atp-dependent dnase, exodeoxyribonuclease, type ii restriction-modification system, ecor124, ecoai, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
type IB restriction enzyme
-
adenosine triphosphate-dependent deoxyribonuclease
-
-
-
-
ATP-dependent deoxyribonuclease
-
-
-
-
ATP-dependent DNase
-
-
-
-
deoxyribonuclease (ATP- and S-adenosyl-L-methionine dependent)
-
-
-
-
deoxyribonuclease (ATP-dependent)
-
-
-
-
DNase
-
-
-
-
EC 3.1.23
-
-
-
-
EC 3.1.24
-
-
-
-
Eco777I
-
-
EcoA0ORF42P
-
-
EcoB
-
-
-
-
EcoEI
EcoKI type I DNA restriction enzyme
-
-
EcoR124
-
-
EcoR124/3I
-
-
EcoR124I
EcoR124II
-
-
EcoRII modification enzyme
-
-
EcoRII RM gene complex
-
-
EcoRII system
-
-
endodeoxyribonuclease
-
-
-
-
exodeoxyribonuclease
-
-
-
-
H91_orf206
-
-
-
-
H91_orf376
-
-
-
-
MpnORFDAP
-
-
-
-
MpnORFDBP
-
-
-
-
nuclease, deoxyribo-
-
-
-
-
nuclease, deoxyribo-, ATP-dependent
-
-
-
-
R.EcoAI
-
-
-
-
R.EcoEI
-
-
-
-
R.EcoKI
-
-
-
-
R.EcoR124I restriction endonuclease
-
-
-
-
R.EcoR124II
-
-
-
-
R.EcoR124INT
-
-
restriction-modification system
-
-
-
-
type I R-M enzyme
-
-
type I R-M system
-
-
type I restriction enzyme
type I restriction modification enzyme
-
-
type I restriction-modification enzyme
type I restriction-modification system
-
-
type I restriction-modification system EcoR124I
-
type IB restriction enzyme
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolysed
show the reaction diagram
kinetic model for DNA-translocation and DNA cleavage
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37263-09-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
duplex DNA + ATP
double-stranded DNA fragments with terminal 5'-phosphate + ADP + inorganic phosphate
show the reaction diagram
-
-
-
?
DNA + H2O
?
show the reaction diagram
duplex DNA + ATP
double-stranded DNA fragments with terminal 5'-phosphate + ADP + inorganic phosphate
show the reaction diagram
linear plasmid DNA pDRM-2R + ATP
?
show the reaction diagram
-
-
-
?
plasmid DNA + H2O
?
show the reaction diagram
-
EcoKI prefers to have a partially filled DNA-binding site rather than one fully occupied by non-specific DNA. Dimerization of EcoKI does not occur before DNA binding and takes place on specific sites before any looping. Dimerization occurs before the two specific sites are bought together. Looping initially occurs between a target site and a non-specific region of DNA
-
-
?
plasmid pTK-neo + ATP
?
show the reaction diagram
-
the enzyme recognises the symmetrical sequence GAAN7TTC at position 2535 bp
-
-
?
plasmid pUC19 + ATP
?
show the reaction diagram
-
the enzyme recognises the symmetrical sequence GAAN7TTC at positions 1126 bp and 2294 bp
-
-
?
supercoiled plasmid DNA pRK + ATP
?
show the reaction diagram
-
-
-
?
synthetic oligonucleotide + ATP
?
show the reaction diagram
additional information
?
-
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
duplex DNA + ATP
double-stranded DNA fragments with terminal 5'-phosphate + ADP + inorganic phosphate
show the reaction diagram
-
type I enzymes recognize bipartite DNA sequences comprising two half-sequences separated by a gap, for example, AACNNNNNNGTGC (AAC N6 GTGC) where N=any base
-
-
?
linear plasmid DNA pDRM-2R + ATP
?
show the reaction diagram
-
-
-
?
supercoiled plasmid DNA pRK + ATP
?
show the reaction diagram
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ArdA
-
antirestriction protein of InvB plasmid R16, selective
-
ArdA protein
-
-
-
ArdB protein
-
-
-
DNA
-
cleavage of DNA is inhibited by an increased degree of negative supercoiling
Ocr protein
-
-
-
S-adenosyl homocysteine
-
competitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl methionine
-
stimulates DNA cleavage activity
S-adenosyl-L-methionine
additional information
-
REcBCD displaces EcoR124I from the cleaved DNA, allowing it to regain catalytic function and cleave the second aliquot of DNA. RecBCD is able to reactivate cleavage-inactivated EcoR124I holoenzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
167
ATP
-
at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
EcoB, methylase activity
8
-
nuclease reaction
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
individual subunits HsdR and HsdM are soluble cytoplasmic proteins
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
EcoprrI is an apoptosis enzyme
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
T1RA_ECOLX
810
0
92071
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
116000
-
x * 116000, HsdR, x * 55000, HsdM, x * 43000, HsdS
130000
1 * 94000, dynamic light scattering, 1 * 130000, analytical ultracentrifugation, subunit HsdR, subunit is globular and fairly compact
135000
290000 - 315000
-
pentameric enzyme form R2M2S1, gel filtration
312000
-
gel filtration
400000
-
EcoK, sucrose density gradient sedimentation
43000
-
x * 116000, HsdR, x * 55000, HsdM, x * 43000, HsdS
431000
-
x * 431000, calculated from amino acid sequence
52000
-
alpha2,beta2,gamma1, 2 * 135000 + 2 * 62000 + 1 * 52000, EcoK, SDS-PAGE
55000
60000
-
alpha2,beta4,gamma2, 2 * 135000 + 4 * 60000 + 2 * 55000, EcoB, SDS-PAGE
62000
-
alpha2,beta2,gamma1, 2 * 135000 + 2 * 62000 + 1 * 52000, EcoK, SDS-PAGE
94000
1 * 94000, dynamic light scattering, 1 * 130000, analytical ultracentrifugation, subunit HsdR, subunit is globular and fairly compact
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 94000, dynamic light scattering, 1 * 130000, analytical ultracentrifugation, subunit HsdR, subunit is globular and fairly compact
octamer
-
alpha2,beta4,gamma2, 2 * 135000 + 4 * 60000 + 2 * 55000, EcoB, SDS-PAGE
pentamer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
HsdR subunit of isoform EcoKI is phosphorylated on Thr. Phosphorylation in vitro is strictly dependent on the addition of a catalytic amount of cytoplasmic fraction isolated from Escherichia coli. Phosphorylation in vivo only occurs when subunit HsdR is coproduced with subunits HsdM and HsdS
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
database information: http://rebase.neb.com
-
model of subunit HsdR using protein fold-recognition and homology modeling. Subunit shows an ellipsoidal shape of the enzymatic core comprising the N-terminal and central domains. Conformational heterogenity of the C-terminal region implicated in binding of HsdR to the HsdS-HsdM complex
motor subunit HsdR of pR124 plasmid-borne type I restriction-modification enzyme EcoR124I, solved in complex with Mg2+-ATP at 2.6 A resolution. HsdR presents four globular domains in a square-planar arrangement, generating prominent grooves between adjacent domain pairs. Lys220 on alpha8 is 3.1 A from N3 on the exposed edge of ATP bound at the helicase domains, potentially coupling endonuclease and helicase function. A uniformly positive surface groove with a clear match to the size and shape of duplex DNA proceeds from a canonical helicase cleft in a continuous path down the front of the motor subunit between the helical and endonuclease domains, where the cleavage site is recessed slightly from the surface
recombinant motor subunit HsdR of isoform EcoR124I in presence and absence of ATP, at 2.6 A resolution
-
sitting-drop vapor diffusion, crystal structures of three mutants of EcoR124I HsdR are designed to probe this mechanism. The results indicate that interdomain engagement via ATP is responsible for signal transmission between the endonuclease and helicase domains of the motor subunit
sitting-drop vapour-diffusion technique, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I. The shortest of the three encompassed HsdR residues 887-1038 and yielded crystals that belonged to the orthorhombic space group C2221, with unit-cell parameters a = 83.42, b = 176.58, c = 126.03 A, alpha = beta = gamma = 90.0 and two molecules in the asymmetric unit. X-ray diffraction data are collected to a resolution of 2.45 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K220A
the mutant enzyme shows a 5fold reduction in restriction activity. The mutant motor subunit is not defective in interacting with the methyltransferase to form the endonuclease complex
K220Q
the mutant enzyme shows a 400fold reduction in restriction activity. The mutant motor subunit is not defective in interacting with the methyltransferase to form the endonuclease complex
K220R
the mutant motor subunit is not defective in interacting with the methyltransferase to form the endonuclease complex
L80P
-
L80P mutation in the modification enzyme of the EcoRII gene complex confers thermosensitivity of cell growth (shows activity at 30°C but not at 37°C). Under a condition of inhibited protein synthesis, the activity of the mutant is completely lost at a high temperature. In parallel, the L80P mutant protein disappears more rapidly than the wild-type protein
R182A
inactive
T239C
-
shows decreased DNA methyltransferase activity at a higher temperature in vivo and in vitro than the nonmutated enzyme
T402C
-
cells carrying the mutation are able to grow at 42°C
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EcoR124I methylase is purified from Escherichia coli strain JM109(DE3) harboring plasmid pJS4M
enzyme EcoB
-
enzyme EcoK
-
mixture of two enzyme species, the larger species has the stoichiometry R2M2S1, the smaller species has the stoichiometry of R1M2S1.only the R2M2S1 complex is capable of DNA cleavage, the R1M2S1 complex retains ATPase activity
-
Mtase(DELTA50)
-
mutant methylase
-
pHluorin-assisted purification of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I
recombinant motor subunit HsdR of isoform EcoR124I
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
248-bp insertion fragments of the ptypeI plasmid inserted at the HincII site of pUC19
-
EcoR124I HsdR with selenomethionine labeling expressed in Escherichia coli
EcoR124I methylase is purified from Escherichia coli strain JM109(DE3) harboring plasmid pJS4M
enzyme with and without a temperature sensitive mutation in the hsdS gene are cloned in pBR322 plamid and introduced into Escherichia coli C3-6
-
expressed in Escherichia coli BL21(DE3) Gold cells
expressed in Escherichia coli strains BNH670 or GM31 harboring a plasmid with various versions of the EcoRII RM gene complex
-
HsdR subunit of isoform EcoR124I, expression in Escherichia coli
-
of hsdS(DELTA50)
-
pHluorin-assisted expression of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I
recombinant plasmid pJS4M overproducing HsdM compared to HsdS
-
transforming the Escherichia coli BL21(DE3) strains with a BAC C4/1 carrying the hsdR, hsdM and hsdS genes of EcoAO83I and with plasmids carrying the hsdS and hsdM genes of EcoAI
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
potential uses for EcoR124I as a nanoactuator within a biosensor in the field of bionanotechnology. It may be used as a molecular dynamo that can measure events from single molecules of DNA, providing a highly sensitive biosensor for detecting events that interrupt translocation events
medicine
identification of a putative restriction-modification system EcoA0ORF42P in the commensal Escherichia coli strain A0 34/86 (O83: K24: H31), which is efficiently used at Czech paediatric clinics for prophylaxis and treatment of nosocomial infections and diarrhoea of preterm and newborn infants. This type I R-M system is a member of the type IB family, but is not an isoschizomer of either any prototype of the type IB members or any sequenced putative IB R-M systems. It is designated as EcoAO83I, the DNA recognition sequence of the EcoAO83I is GGA(8N)ATGC. Combination of the classical biochemical and bacterial genetics approaches with comparative genomics may contribute effectively to further classification of many other putative type-I enzymes, especially in clinical samples
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Janscak, P.; Abadjieva, A.; Firman, K.
The type I restriction endonuclease R.EcoR124I: Over-production and biochemical properties
J. Mol. Biol.
257
977-991
1996
Escherichia coli
Manually annotated by BRENDA team
Gubler, M.; Braguglia, D.; Meyer, J.; Piekarowicz, A.; Bickle, T.A.
Recombination of constant and variable modules alters DNA sequence recognition by type IC restriction-modification enzymes
EMBO J.
11
233-240
1992
Escherichia coli
Manually annotated by BRENDA team
Abadjieva, A.; Patel, J.; Webb, M.; Zinkevich, V.; Firman, K.
A deletion mutant of the type IC restriction endonuclease EcoR124I expressing a novel DNA specificity
Nucleic Acids Res.
21
4435-4443
1993
Escherichia coli
Manually annotated by BRENDA team
Taylor, I.; Watts, D.; Kneale, G.
Substrate recognition and selectivity in the type IC DNA modification methylase M.EcoR124I
Nucleic Acids Res.
2
4929-4935
1993
Escherichia coli
Manually annotated by BRENDA team
Davies, G.P.; Martin, I.; Sturrock, S.S.; Cronshaw, A.; Murray, N.E.; Dryden, D.T.F.
On the structure and operation of type I DNA restriction enzymes
J. Mol. Biol.
290
565-579
1999
Escherichia coli
Manually annotated by BRENDA team
Zinkevich, V.; Heslop, P.; Glover, S.W.; Weiserova, M.; Hubacek, J.; Firman, K.
Mutation in the specificity polypeptide of the type I restriction endonuclease R*EcoK that affects subunit assembly
J. Mol. Biol.
227
597-601
1992
Escherichia coli
Manually annotated by BRENDA team
Meister, J.; MacWilliams, M.; Hubner, P.; Jutte, H.; Skrzypek, E.; Piekarowicz, A.; Bickle, T.A.
Macroevolution by transposition: drastic modification of DNA recognition by a type I restriction enzyme following Tn5 transposition
EMBO J.
12
4585-4591
1993
Escherichia coli
Manually annotated by BRENDA team
Janscak, P.; Dryden, D.T.F.; Firman, K.
Analysis of the subunit assembly of the typeIC restriction-modification enzyme EcoR124I
Nucleic Acids Res.
26
4439-4445
1998
Escherichia coli
Manually annotated by BRENDA team
Endlich, B.; Linn, S.
Type I restriction enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
14
137-156
1981
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
-
Manually annotated by BRENDA team
Sjoestroem, J.E.; Loefdahl, S.; Philipson, L.
Biological characteristics of a type I restriction-modification system in Staphylococcus aureus
J. Bacteriol.
133
1144-1149
1978
Citrobacter freundii, Escherichia coli, Staphylococcus aureus, Staphylococcus aureus RN450
Manually annotated by BRENDA team
Roberts, R.J.
Restriction enzymes and their isoschizomers
Nucleic Acids Res.
18
2331-2365
1990
Citrobacter freundii, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhi
Manually annotated by BRENDA team
Roberts, R.J.
Restriction and modification enzymes and their recognition sequences
Nucleic Acids Res.
11
r135-r167
1983
Escherichia coli
Manually annotated by BRENDA team
Weiserova, M.; Janscak, P.; Benada, O.; Hubacek, J.; Zinkevich, V.E.; Glover, S.W.; Firman, K.
Cloning, production and characterisation of wild type and mutant forms of the R*EcoK endonucleases
Nucleic Acids Res.
21
373-379
1993
Escherichia coli
Manually annotated by BRENDA team
Roberts, R.J.; Macelis, D.
REBASE - restriction enzymes and methylases
Nucleic Acids Res.
29
268-269
2001
Escherichia coli
Manually annotated by BRENDA team
Holubova, I.; Vejsadova, S.; Firman, K.; Weiserova, M.
Cellular localization of Type I restriction-modification enzymes is family dependent
Biochem. Biophys. Res. Commun.
319
375-380
2004
Escherichia coli
Manually annotated by BRENDA team
Szczelkun, M.D.
Kinetic models of translocation, head-on collision, and DNA cleavage by type I restriction endonucleases
Biochemistry
41
2067-2074
2002
Escherichia coli
Manually annotated by BRENDA team
Thomas, A.T.; Brammar, W.J.; Wilkins, B.M.
Plasmid R16 ArdA protein preferentially targets restriction activity of the type I restriction-modification system EcoKI
J. Bacteriol.
185
2022-2025
2003
Escherichia coli
Manually annotated by BRENDA team
McClelland, S.E.; Dryden, D.T.F.; Szczelkun, M.D.
Continous asay for DNA translocation using fluorescent triplex dissociation: application to type I restriction endonucleases
J. MOl. Biol.
348
895-915
2005
Escherichia coli
Manually annotated by BRENDA team
Bianco, P.R.; Hurley, E.M.
The type I restriction endonuclease EcoR124I, couples ATP hydrolysis to bidirectional DNA translocation
J. Mol. Biol.
352
837-859
2005
Escherichia coli
Manually annotated by BRENDA team
Seidel, R.; van Noort, J.; van der Scheer, C.; Bloom, J.G.; Dekker, N.H.; Dutta, C.F.; Blundell, A.; Robinson, T.; Firman, K.; Dekker, C.
Real-time observation of DNA translocation by the type I restriction modification enzyme EcoR124I
Nat. Struct. Mol. Biol.
11
838-843
2004
Escherichia coli
Manually annotated by BRENDA team
van Noort, J.; van der Heijden, T.; Dutta, C.F.; Firman, K.; Dekker, C.
Initiation of translocation by Type I restriction-modification enzymes is associated with a short DNA extrusion
Nucleic Acids Res.
32
6540-6547
2004
Escherichia coli
Manually annotated by BRENDA team
Jindrova, E.; Schmid-Nuoffer, S.; Hamburger, F.; Janscak, P.; Bickle, T.A.
On the DNA cleavage mechanism of type I restriction enzymes
Nucleic Acids Res.
33
1760-1766
2005
Escherichia coli
Manually annotated by BRENDA team
Kasarjian, J.K.; Kodama, Y.; Iida, M.; Matsuda, K.; Ryu, J.
Four new type I restriction enzymes identified in Escherichia coli clinical isolates
Nucleic Acids Res.
33
e114
2005
Escherichia coli
Manually annotated by BRENDA team
Lapkouski, M.; Panjikar, S.; Kuta Smatanova, I.; Csefalvay, E.
Purification, crystallization and preliminary X-ray analysis of the HsdR subunit of the EcoR124I endonuclease from Escherichia coli
Acta Crystallogr. Sect. F
63
582-585
2007
Escherichia coli
Manually annotated by BRENDA team
Cajthamlova, K.; Sisakova, E.; Weiser, J.; Weiserova, M.
Phosphorylation of Type IA restriction-modification complex enzyme EcoKI on the HsdR subunit
FEMS Microbiol. Lett.
270
171-177
2007
Escherichia coli
Manually annotated by BRENDA team
Obarska-Kosinska, A.; Taylor, J.E.; Callow, P.; Orlowski, J.; Bujnicki, J.M.; Kneale, G.G.
HsdR subunit of the type I restriction-modification enzyme EcoR124I: biophysical characterisation and structural modelling
J. Mol. Biol.
376
438-452
2008
Escherichia coli (Q304R3)
Manually annotated by BRENDA team
Ohno, S.; Handa, N.; Watanabe-Matsui, M.; Takahashi, N.; Kobayashi, I.
Maintenance forced by a restriction-modification system can be modulated by a region in its modification enzyme not essential for methyltransferase activity
J. Bacteriol.
190
2039-2049
2008
Escherichia coli
Manually annotated by BRENDA team
Weiserova, M.; Ryu, J.
Characterization of a restriction modification system from the commensal Escherichia coli strain A0 34/86 (O83:K24:H31)
BMC Microbiol.
8
106
2008
Escherichia coli, Escherichia coli (Q07736), Escherichia coli (Q47281), Escherichia coli A0 34/86 (O83:K24:H31), Escherichia coli A0 34/86 (O83:K24:H31) (Q07736), Escherichia coli A0 34/86 (O83:K24:H31) (Q47281)
Manually annotated by BRENDA team
Youell, J.; Firman, K.
EcoR124I: from plasmid-encoded restriction-modification system to nanodevice
Microbiol. Mol. Biol. Rev.
72
365-77
2008
Escherichia coli
Manually annotated by BRENDA team
Ryu, J.; Rowsell, E.
Quick identification of type I restriction enzyme isoschizomers using newly developed ptypeI and reference plasmids
Nucleic Acids Res.
36
e81
2008
Escherichia coli, Salmonella-Escherichia coli hybrid
Manually annotated by BRENDA team
Neaves, K.J.; Cooper, L.P.; White, J.H.; Carnally, S.M.; Dryden, D.T.; Edwardson, J.M.; Henderson, R.M.
Atomic force microscopy of the EcoKI type I DNA restriction enzyme bound to DNA shows enzyme dimerization and DNA looping
Nucleic Acids Res.
37
2053-2063
2009
Escherichia coli
Manually annotated by BRENDA team
Lapkouski, M.; Panjikar, S.; Janscak, P.; Smatanova, I.K.; Carey, J.; Ettrich, R.; Csefalvay, E.
Structure of the motor subunit of type I restriction-modification complex EcoR124I
Nat. Struct. Mol. Biol.
16
94-95
2009
Escherichia coli (Q304R3)
Manually annotated by BRENDA team
Sinha, D.; Shamayeva, K.; Ramasubramani, V.; Reha, D.; Bialevich, V.; Khabiri, M.; Guzanova, A.; Milbar, N.; Weiserova, M.; Csefalvay, E.; Carey, J.; Ettrich, R.
Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I
J. Mol. Model.
20
2334
2014
Escherichia coli (P10486)
Manually annotated by BRENDA team
Loenen, W.A.; Dryden, D.T.; Raleigh, E.A.; Wilson, G.G.
Type I restriction enzymes and their relatives
Nucleic Acids Res.
42
20-44
2014
Escherichia coli
Manually annotated by BRENDA team
Taylor, J.E.; Swiderska, A.; Artero, J.B.; Callow, P.; Kneale, G.
Structural and functional analysis of the symmetrical Type I restriction endonuclease R.EcoR124I(NT)
PLoS ONE
7
e35263
2012
Escherichia coli
Manually annotated by BRENDA team
Grinkevich, P.; Iermak, I.; Luedtke, N.A.; Mesters, J.R.; Ettrich, R.; Ludwig, J.
pHluorin-assisted expression, purification, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I
Acta Crystallogr. Sect. F
72
672-676
2016
Escherichia coli (Q304R3), Escherichia coli
Manually annotated by BRENDA team
Csefalvay, E.; Lapkouski, M.; Guzanova, A.; Csefalvay, L.; Baikova, T.; Shevelev, I.; Bialevich, V.; Shamayeva, K.; Janscak, P.; Kuta Smatanova, I.; Panjikar, S.; Carey, J.; Weiserova, M.; Ettrich, R.
Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme
PLoS ONE
10
e0128700
2015
Escherichia coli (P10486), Escherichia coli
Manually annotated by BRENDA team