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Information on EC 3.1.21.4 - type II site-specific deoxyribonuclease
for references in articles please use BRENDA:EC3.1.21.4
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters
3.1.21.4 type II site-specific deoxyribonuclease
IUBMB Comments
This is a large group of enzymes which, together with those now listed as EC 3.1.21.3 (type 1 site-specific deoxyribonuclease) and EC 3.1.21.5.
The enzyme appears in viruses and cellular organisms
- 3.1.21.4
- endonucleases
- phage
- lambda
- agarose
- strand
- rrna
- bacteriophage
-
pcr-rflp
- viruses
-
serotype
-
pulsed-field
-
single-stranded
-
spacers
-
cosmid
-
amplicons
- adenovirus
-
outbreak
- simplex
- herpes
- mtdnas
- cytosine
- duplex
-
serological
-
pcr-based
-
nested
-
epstein-barr
- cpg
-
caucasian
-
methylase
-
reaction-restriction
- herpesvirus
- virion
- satellite
- tetracycline
-
nosocomial
-
32p-labeled
-
proviral
- beta-globin
-
simian
- ethidium
- globin
- ampicillin
-
discriminatory
-
dna-dna
-
unmethylated
-
supercoiled
- serogroups
-
biotype
-
subfragment
- analysis
- biotechnology
- beta-thalassemia
- molecular biology
Reaction Schemes
showendonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
Synonyms
restriction enzyme, restriction endonuclease, ecori, hindiii, bamhi, pvuii, haeiii, hpaii, bglii, ecorv, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AfeI
AflII
aflIIR
AgeI
AloI
ApaI
ApaLI
AvrII
BamHI
BbvI
Bfi2411I
BglII
BmtI
BpuEI
BspD6I
BsrGI
BstEII
BstF5I
BstXI
Bsu2413I
CspCI
CstMI
DNA restriction endonuclease
-
-
-
-
DNA restriction enzyme
-
-
-
-
DpnI
EC 3.1.23
-
-
-
-
EC 3.1.24
-
-
-
-
Eco31I
Eco57I
eco57IR
EcoP15I
ecoP15Ires
EcoRI
EcoRII
EcoRV
-
-
Endonuclease AbrI
-
-
-
-
Endonuclease AccI
-
-
-
-
Endonuclease AgeI
-
-
-
-
Endonuclease ApaLI
-
-
-
-
Endonuclease AvaI
-
-
-
-
Endonuclease BamHI
-
-
-
-
Endonuclease BanI
-
-
-
-
Endonuclease BglI
-
-
-
-
Endonuclease BglII
-
-
-
-
Endonuclease BsoBI
-
-
-
-
Endonuclease Bsp6I
-
-
-
-
Endonuclease BstVI
-
-
-
-
Endonuclease BsuBI
-
-
-
-
Endonuclease BsuFI
-
-
-
-
Endonuclease BsuRI
-
-
-
-
Endonuclease CeqI
-
-
-
-
Endonuclease Cfr10I
-
-
-
-
Endonuclease Cfr9I
-
-
-
-
Endonuclease CfrBI
-
-
-
-
Endonuclease CviAII
-
-
-
-
Endonuclease CviJI
-
-
-
-
Endonuclease DdeI
-
-
-
-
Endonuclease DpnI
-
-
-
-
Endonuclease DpnII
-
-
-
-
Endonuclease Eco47I
-
-
-
-
Endonuclease Eco47II
-
-
-
-
Endonuclease EcoRI
-
-
-
-
Endonuclease EcoRII
-
-
-
-
Endonuclease EcoRV
-
-
-
-
Endonuclease FokI
-
-
-
-
Endonuclease HaeII
-
-
-
-
Endonuclease HaeIII
-
-
-
-
Endonuclease HgAI
-
-
-
-
Endonuclease HgiBI
-
-
-
-
Endonuclease HgiCI
-
-
-
-
Endonuclease HgiCII
-
-
-
-
Endonuclease HgiDI
-
-
-
-
Endonuclease HgiEI
-
-
-
-
Endonuclease HgiGI
-
-
-
-
Endonuclease HhaII
-
-
-
-
Endonuclease HincII
-
-
-
-
Endonuclease HindII
-
-
-
-
Endonuclease HindIII
-
-
-
-
Endonuclease HindVP
-
-
-
-
Endonuclease HinfI
-
-
-
-
Endonuclease HpaI
-
-
-
-
Endonuclease HpaII
-
-
-
-
Endonuclease HphI
-
-
-
-
Endonuclease KpnI
-
-
-
-
Endonuclease LlaDCHI
-
-
-
-
Endonuclease MamI
-
-
-
-
Endonuclease MboI
-
-
-
-
Endonuclease MboII
-
-
-
-
Endonuclease MjaI
-
-
-
-
Endonuclease MjaII
-
-
-
-
Endonuclease MjaIII
-
-
-
-
Endonuclease MjaIV
-
-
-
-
Endonuclease MjaV
-
-
-
-
Endonuclease MjaVIP
-
-
-
-
Endonuclease MspI
-
-
-
-
Endonuclease MthTI
-
-
-
-
Endonuclease MthZI
-
-
-
-
Endonuclease MunI
-
-
-
-
Endonuclease MwoI
-
-
-
-
Endonuclease NaeI
-
-
-
-
Endonuclease NgoBI
-
-
-
-
Endonuclease NgoBV
-
-
-
-
Endonuclease NgoFVII
-
-
-
-
Endonuclease NgoMIV
-
-
-
-
Endonuclease NgoPII
-
-
-
-
Endonuclease NlaIII
-
-
-
-
Endonuclease NlaIV
-
-
-
-
Endonuclease NmeDIP
-
-
-
-
Endonuclease NspV
-
-
-
-
Endonuclease PaeR7I
-
-
-
-
Endonuclease PstI
-
-
-
-
Endonuclease PvuI
-
-
-
-
Endonuclease PvuII
-
-
-
-
Endonuclease RsrI
-
-
-
-
Endonuclease SacI
-
-
-
-
Endonuclease SalI
-
-
-
-
Endonuclease Sau3AI
-
-
-
-
Endonuclease Sau96I
-
-
-
-
Endonuclease ScaI
-
-
-
-
Endonuclease ScrFI
-
-
-
-
Endonuclease SfiI
-
-
-
-
Endonuclease SinI
-
-
-
-
Endonuclease SmaI
-
-
-
-
Endonuclease SsoII
-
-
-
-
Endonuclease StsI
-
-
-
-
Endonuclease TaqI
-
-
-
-
Endonuclease TthHB8I
-
-
-
-
Endonuclease XamI
-
-
-
-
Endonuclease XcyI
-
-
-
-
FokI
GsuI
gva14018IR
HincII
HindIII
hindIIIR
HinfI
HpaI
Hpy188I
HpyF17I
KpnI
LlaII
-
-
-
-
LmoJ2
LmoJ3
MmeI
MseI
MspA1I
NcoI
NheI
Nt.BspD6I
nuclease, deoxyribonucleic restriction endo-
-
-
-
-
nuclease, restriction endodeoxyribo-
-
-
-
-
PflMI
PsasM2I
PspGI
PstI
PvuII
R.AbrI
-
-
-
-
R.AccI
-
-
-
-
R.AgeI
-
-
-
-
R.ApaLI
-
-
-
-
R.AvaI
-
-
-
-
R.BamHI
-
-
-
-
R.BanI
-
-
-
-
R.BglI
-
-
-
-
R.BglII
-
-
-
-
R.BsoBI
-
-
-
-
R.Bsp6I
-
-
-
-
R.BstVI
-
-
-
-
R.BsuBI
-
-
-
-
R.BsuRI
-
-
-
-
R.CeqI
-
-
-
-
R.Cfr10I
-
-
-
-
R.Cfr9I
-
-
-
-
R.CfrBI
-
-
-
-
R.CviAII
-
-
-
-
R.CviJI
-
-
-
-
R.DdeI
-
-
-
-
R.DpnI
-
-
-
-
R.DpnII
-
-
-
-
R.Eco47I
-
-
-
-
R.Eco47II
-
-
-
-
R.EcoRI
-
-
-
-
R.EcoRII
R.EcoRV
-
-
-
-
R.FokI
-
-
-
-
R.Gva14018I
R.HaeII
-
-
-
-
R.HaeIII
-
-
-
-
R.HgAI
-
-
-
-
R.HgiBI
-
-
-
-
R.HgiCI
-
-
-
-
R.HgiCII
-
-
-
-
R.HgiDI
-
-
-
-
R.HgiEI
-
-
-
-
R.HgiGI
-
-
-
-
R.HhaII
-
-
-
-
R.HincII
-
-
-
-
R.HindII
-
-
-
-
R.HindIII
-
-
-
-
R.HindVP
-
-
-
-
R.HinfI
-
-
-
-
R.HpaI
-
-
-
-
R.HpaII
-
-
-
-
R.HphI
-
-
-
-
R.KpnI
R.LlaDCHI
-
-
-
-
R.MamI
-
-
-
-
R.MboI
-
-
-
-
R.MboII
-
-
-
-
R.MjaI
-
-
-
-
R.MjaII
-
-
-
-
R.MjaIII
-
-
-
-
R.MjaIV
-
-
-
-
R.MjaV
-
-
-
-
R.MjaVIP
-
-
-
-
R.MspI
-
-
-
-
R.MthTI
-
-
-
-
R.MthZI
-
-
-
-
R.MunI
-
-
-
-
R.MwoI
-
-
-
-
R.NaeI
-
-
-
-
R.NgoBI
-
-
-
-
R.NgoBV
-
-
-
-
R.NgoFVII
-
-
-
-
R.NgoI
-
-
-
-
R.NgoMIV
-
-
-
-
R.NgoPII
-
-
-
-
R.NgoV
-
-
-
-
R.NgoVII
-
-
-
-
R.NlaIII
-
-
-
-
R.NlaIV
-
-
-
-
R.NmeDIP
-
-
-
-
R.NspV
-
-
-
-
R.PaeR7I
-
-
-
-
R.PstI
-
-
-
-
R.PvuI
-
-
-
-
R.PvuII
-
-
-
-
R.RsrI
-
-
-
-
R.SacI
-
-
-
-
R.SalI
-
-
-
-
R.Sau3AI
-
-
-
-
R.Sau96I
-
-
-
-
R.ScaI
-
-
-
-
R.ScrFI
-
-
-
-
R.SfiI
-
-
-
-
R.SinI
-
-
-
-
R.SmaI
-
-
-
-
R.SsoII
-
-
-
-
R.StsI
-
-
-
-
R.TaqI
-
-
-
-
R.TthHB8I
-
-
-
-
R.XamI
-
-
-
-
R.XcyI
-
-
-
-
REase
restriction endodeoxyribonuclease
-
-
-
-
restriction endonuclease
-
-
-
-
restriction enzyme
-
-
-
-
RsaI
SacI
sau96I
ScaI
site-specific endonuclease BME142I
site-specific endonuclease Bme216I
site-specific endonuclease BmeI
site-specific type II endonuclease
SmaI
SmuI
SnaBI
ss.BspD6I
SuiI
TfiI
TstI
type II REase
type II restriction endonuclease
type II restriction enzyme
type II restriction-modification protein
type II restriction-modification system
type II RM system
type IIB restriction endonuclease
type IIS restriction endonuclease
type IIS restriction enzyme
typeIIS restriction endonuclease
UpaP162
UPV_230
XcmI
XhoI
additional information
R.EcoRII
-
-
-
-
R.KpnI
-
-
-
-
site-specific endonuclease Bme216I
-
recognition site is identical with the endonuclease AvaII from Anabaena variabilis
site-specific endonuclease Bme216I
-
recognition site is identical with the endonuclease AvaII from Anabaena variabilis
-
additional information
-
a complete listing of all these enzymes and their recognition sites has been produced by R.J. Roberts, this list is updated annually
additional information
-
a complete listing of all these enzymes and their recognition sites has been produced by R.J. Roberts, this list is updated annually
additional information
-
BspRI and the related putative restriction endonucleases belong to the PD-(D/E)XK nuclease superfamily
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
-
-
-
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
autoinhibition/activation mechanism
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
residues D311 and N334 coordinate the cofactor. H312 acts as a general base actiating a water molecule for the nucleophilic attack. K337 together with R340 and D345 are located close to the active center and are essential for correct folding of cataloytic motif, while D345, R264 and D273 may be directly involved in DNA binding
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
residue H291 is the direct catalytic residue, N308 is important for the structural integrity of the betabetaalpha motif, while D317 and D321 are involved in metal ion binding
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9075-08-5
not distinguished from EC 3.1.21.5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
d(G-G-T-T-5'-bromodeoxyuridine-C-C) + H2O
?
-
Substrates: -
Products: -
Products: -
?
DNA containing AGATCC + H2O
?
A0A7R7A8H4
Substrates: -
Products: -
Products: -
?
DNA containing F5dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing F5dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dU
Products: -
Products: -
?
DNA containing GGATCT + H2O
?
A0A7R7A8H4
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with 3-base 5'-overhangs
Q5D6Y5; Q5D6Y4
Substrates: the enzyme recognizes and cleaves the seven base pair sequence 5'-CCTCAGC-3', generating 3-base, 5'-overhangs
Products: -
Products: -
?
pBR322 DNA + H2O
two fragments of 3200 bp and 1700 bp
-
Substrates: -
Products: -
Products: -
?
pBR322DNA + H2O
pBR322 DNA fragments
-
Substrates: the tetranucleotide GGCC can be cleaved by SuaI either symmetrically or nonsymmetrically, thus producing termini with a single-stranded end
Products: -
Products: -
?
d(G-G-T-5-bromodeoxyuridine-A-A-C-C) + H2O
?
-
Substrates: -
Products: -
Products: -
?
d(G-G-T-5-bromodeoxyuridine-A-A-C-C) + H2O
?
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: primary function is the inactivation of foreign DNA invading bacteria
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: sequence-specific endonucleolytic digestion of infecting DNA
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: -
Products: the isolated C-terminal domain dimer has an interface that binds a single cognate DNA molecule whereas the N-terminal domain is a monomer that also binds a single copy of cognate DNA
Products: the isolated C-terminal domain dimer has an interface that binds a single cognate DNA molecule whereas the N-terminal domain is a monomer that also binds a single copy of cognate DNA
?
DNA + H2O
?
Substrates: the enzyme recognizes a degenerated sequence 5'-W/CCGGW-3' (W stands for A or T and / denotes the cleavage site). It belongs to a large family of restriction enzymes that contain a conserved CCGG tetranucleotide in their target sites. It requires binding of two target sites for the optimal catalytic activity
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: sequence-specific endonucleolytic digestion of infecting DNA
Products: -
Products: -
?
DNA + H2O
?
Substrates: the enzyme is resilient to specificity changes at the first position of the recognition sequence (5'-TCCRAC-3')
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: the enzyme recognizes interrupted palindromes, i.e., 5'-CCNGG-3' sequences and cleaves DNA leaving 5-nucleotide long, single-stranded, 5'-cohesive ends
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: sequence-specific endonucleolytic digestion of infecting DNA
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: enzyme cuts DNA at the recognition site GcwGC, cleavage occurs after the first guanosine base
Products: -
Products: -
?
DNA + H2O
?
Saccharolobus islandicus REN2H1
-
Substrates: enzyme cuts DNA at the recognition site GcwGC, cleavage occurs after the first guanosine base
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: recognition site is GGCC, enzyme does not cut Sulfolobus acidocaldarius DNA, as the recognition site in this DNA contains modified nucleotides
Products: -
Products: -
?
DNA + H2O
?
A0A291ATB4
Substrates: the enzyme is specific for the pseudosymmetric DNA sequence 5'-CC/WGG-3' (where W = A/T, and / marks the cleavage position). UbaLAI requires two recognition sites for optimal activity, and, like other type IIE enzymes, uses one copy of a recognition site to stimulate cleavage of a second copy. It is proposed that during the reaction the UbaLAI N-terminal domain acts as a handle that tethers the monomeric UbaLAI C-terminal domain to the DNA, thereby helping UbaLAI-C to perform two sequential DNA nicking reactions on the second recognition site during a single DNA-binding event
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: enzyme ApaBI recognizes 35 cleavage sites on bacteriophage lamda DNA, 20 sites on adenovirus-2 DNA and 2 sites on plasmid pBR322 DNA. The recognition sequence is 5'-GCANNNNN/TGC-3'\\3'-CGT/NNNNNACG-5', enzyme ApaDI has 6 sites of cleavage on the pBR327 DNA, 7 sites on pAT153 DNA and more than 20 sites on bacteriophage lamda DNA. ApaCI cleaves linear lambda DNA at five sites, circular pBR DNA, pMRFb DNA and pHC 624 DNA at one site
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: mechanochemical model of induced-fit reactions on DNA. Strongly decreased association rate is obtained on streched DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of BamHI: GGATCC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: BspD6I cleaves both DNA strands within the recognition sequence
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: BspD6I cleaves both DNA strands within the recognition sequence
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: the enzyme recognizes the target DNA sequence 5'CCGG and cleaves between the two cytosines to produce sticky ends with 5'CG overhangs
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of BgII: GCCNNNNNGGC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of BglII: AGATCT. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: BbvCI cleaves the assymetric DNA sequence, 5'-CC-/-TCAGC-3'/5'-GC-/-TGAGG-3'. The R1 subunit of the enzyme acts at GC-/-TGAGG and the R2 subunit acts at CC-/-TCAGC. the DNA is cleaved initially in one strand, mainly that targeted by the R1 subunit. The other strand is then cleaved slowly by R2 before the enzyme dissociates from the DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage at 5'-GGCGC-/-C-3. The enzyme displays an absolute requirement for two sites in close physical proximity, which are cleaved concertedly
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage of the DNA strand in DNA,RNA hybrids
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of Cfr10I: RCCGGY. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Dactylococcus salina
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: ColE1 DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: pBR322 DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: SV40 DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage of the DNA strand in DNA,RNA hybrids
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: lambda DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: EcoRII cleaves DNA molecules with only a single recognition site or with very distant sites
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of BstYI: GATATC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of EcoO109I: RGGNCCY. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: Eco1524I recognizes the sequence 6-bp palindromic 5'AGG downward arrow CCT3', producing blunt end
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: EcoRII requires simultaneous binding of three rather than two recognition sites in cis to achieve concerted DNA cleavage at a single site
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: one metal ion and two water molecules are observed near the active site of the DNA complex. The metal ion is a Lewis acid that stabilizes the pentavalent phosphorus atom in the transition state. One water molecule, activated by Lys126, attacks the phosphorous atom in an SN2 mechanism, whereas the other water interacts with the 3'-leaving oxygen to donnate a proton to the oxygen
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: mechanochemical model of induced-fit reactions on DNA. Strongly decreased association rate is obtained on streched DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of EcoRII: CCWGG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of EcoRI: GAATTC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: EcoRII recognizes two units of recognition sequences (5'-CCWGG-3') included in one DNA chain (cis-binding) or in two DNA chains one by one (trans-binding), and cleaves either site
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Eucapsis sp.
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of Bse634I: RCCGGY. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of BsoBI: CYCGRG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: BstYI recognizes the degenerate sequence 5'-RGATCY-3' (where R is A/G and Y is C/T)
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of BstYI: RGATCY. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: BstF5I cleaves DNA 2 bases 3' to the recognition site on one strand and immediately 3' to the recognition site on the opposite strand, leaving a two base overhang
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: BstF5I cleaves DNA 2 bases 3' to the recognition site on one strand and immediately 3' to the recognition site on the opposite strand, leaving a two base overhang
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage of the DNA strand in DNA,RNA hybrids
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage of the DNA strand in DNA,RNA hybrids
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of HincII: GTYRAC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: HinP1I recognizes and cleaves a palindromic tetranucleotide sequence (G-/-CGC) in double-stranded DNA, producing 2 nt 5' overhanging ends
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of HindIII: AAGCTT. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: R.Hpy188I recognizes the sequence TCNGA and cleaves between nucleotides N and G to generate a one-base 3' overhang
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: HpyAXII effectively restricts both unmethylated plasmid and chromosomal DNA during natural transformation, the enzyme targets the tetramer 5'-GTAC-3'
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: R.Hpy188I recognizes the sequence TCNGA and cleaves between nucleotides N and G to generate a one-base 3' overhang
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: R.KpnI cleaves the DNA sequence 5'-GGTAC-/-C-3', generating 3' four base overhangs
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage at 5'-G-/-GCGCC-3'. The enzyme cuts only one bond per turnover but acts at individual sites, preferring intact to nicked sites
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: Mva1269I restriction endonuclease recognizes an asymmetric DNA sequence 5'-GAATGCN-/-3'/5'-NG-/-CATTC-3' and cuts top and bottom DNA strands. The enzyme possesses two active sites responsible for the sequential cleavage of each DNA strand, which has evolved by fusion of a sequence specific nuclease domain, similar to EcoRI, to a nonspecific nuclease domain, similar to FokI
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of NaeI: GCCGGC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: single strandede DNA and double stranded DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: MmeI cuts DNA two turns of the helix away from its asymmetric recognition sequence, 5'-TCCRACN20/N18-3', 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', MmeI methylates its recognition site following DNA cleavage
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage at 5'-GG-/-CGCC-3'. The enzyme cuts both strands of its recognition sites, but shows full activity only when bound to two sites, which are then cleaved concertedly
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of MspI: CCGG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of MunI: CAATTG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of NgoMIV: GCCGGC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Neisseria mucosa heidelbergensis
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage at 5'-GG-/-CGCC-3'. The enzyme binds two sites, but cleaves only one bond per DNA-binding event
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage at 5'-GGC-/-GCC-3'. The enzyme cuts both strands at individual sites
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of FokI: GGATG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: the FokI enzyme cleaves DNA 9 bases 3' to the recognition site on one strand and 13 bases from the recognition site on the other strand, leaving a four base overhang protruding 5' end
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage at 5'-GGC-/-GCC-3'. The enzyme cuts both strands at individual sites
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: recognition sequence of PvuII: CAGCTG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: the enzyme recognizes 5'-GTAC and leaves a 3'-TA overhang (5'-GTA/C)
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleaves DNA before the first C in the sequence 5'-CCWGG3'. W is A or T
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage at 5'-GGC-/-GCC-3'. The enzyme cuts both strands at individual sites
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Q194N8
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage of the DNA strand in DNA,RNA hybrids
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing 5-fluoro-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dU
Products: -
Products: -
?
DNA containing 5-fluoro-dU + H2O
?
Substrates: hydrolyzes the DNA containing 5-fluoro-dU
Products: -
Products: -
?
DNA containing 5-methyl-dC + H2O
?
Substrates: hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-methyl-dC + H2O
?
Substrates: hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-methyl-dC + H2O
?
Substrates: hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-methyl-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing F5dC
Products: -
Products: -
?
DNA containing 5-methyl-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-methyl-dC
Products: -
Products: -
?
DNA containing 5-methyl-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing 5-methyl-dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-methyl-dC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: the enzyme recognizes the sequence 5'-Pu*CCGGPy and cleaves it as indicated by the star
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage by EcoRI is staggered, producing fragments with 4-nucleotide single-stranded overhangs, recognition sequence is GAATTC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage by EcoRV is staggered, producing fragments with 4-nucleotide single-stranded overhangs, recognition sequence is GATATC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: EcoRI recognizes 5'-GAATTC-3' while EcoRV recognizes 5'-GATATC-3', leaving overhangs and blunt DNA segments, respectively
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage by HindII is blunt, producing fragments with flush ends
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: LmoJ3 recognizes GCNGC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: LmoJ2 recognizes GCWGC (W is A or T)
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: LmoJ2 recognizes GCWGC (W is A or T)
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: LmoJ3 recognizes GCNGC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
dsDNA + H2O
?
-
Substrates: recognition sequence is 5-GGACC-3/3-CCTGG-5, enzyme cleaves between the guanosin residues at both strands
Products: sticky end fragments
Products: sticky end fragments
?
dsDNA + H2O
?
-
Substrates: recognizes a specific pentanucleotide
Products: -
Products: -
?
dsDNA + H2O
?
-
Substrates: recognition sequence is 5-GCGC-3/3-CGCG-5, enzyme cleaves in the middle of the tetranucleotide sequence
Products: blunt end fragments
Products: blunt end fragments
?
dsDNA + H2O
?
-
Substrates: recognition sequence is 5-GCGC-3/3-CGCG-5, enzyme cleaves in the middle of the tetranucleotide sequence
Products: blunt end fragments
Products: blunt end fragments
?
dsDNA + H2O
?
-
Substrates: recognition sequence is 5-GGACC-3/3-CCTGG-5, enzyme cleaves between the guanosin residues at both strands
Products: sticky end fragments
Products: sticky end fragments
?
dsDNA + H2O
?
-
Substrates: recognizes a specific pentanucleotide
Products: -
Products: -
?
Escherichia coli LMG194 DNA + H2O
?
-
Substrates: -
Products: -
Products: -
?
linear mNeonGreen DNA + H2O
?
Substrates: -
Products: -
Products: -
?
linear mNeonGreen DNA + H2O
?
Substrates: -
Products: -
Products: -
?
linear mNeonGreen DNA + H2O
?
-
Substrates: -
Products: -
Products: -
?
mScarlet DNA + H2O
?
Substrates: -
Products: -
Products: -
?
mTurquoise2 DNA + H2O
?
Substrates: -
Products: -
Products: -
?
mTurquoise2 DNA + H2O
?
Substrates: -
Products: -
Products: -
?
pNH20 + H2O
?
-
Substrates: 84 bp SacI/HindII-fragment
Products: -
Products: -
?
pT7Blue plasmid + H2O
?
-
Substrates: the enzyme partially digests the CATG site within the pT7Blue plasmid. The digestion efficiency of UpaP162 depends on the sequences around CATG motifs
Products: -
Products: -
?
pT7Blue plasmid + H2O
?
Ureaplasma parvum OMC-P162
-
Substrates: the enzyme partially digests the CATG site within the pT7Blue plasmid. The digestion efficiency of UpaP162 depends on the sequences around CATG motifs
Products: -
Products: -
?
additional information
?
-
-
Substrates: StuI displays 93.8% digest efficiency by digitial counting and a digest efficiency of 98.5% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: no hydrolysis of DNA containing 5-methyl-dC
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolysis of DNA containing 5-methyl-dC
Products: -
Products: -
?
additional information
?
-
-
Substrates: AfeI displays 95.18% digest efficiency by digitial counting
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (10/12) GCAN6TGC (12/10), of which it needs 2 on the substrate to be active. It excises 32 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (7/12) GAACN6TCC (12/7), of which it needs 2 on the substrate to be active. It excises 27 bp, and does not require S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolysis of DNA containing 5-methyl-dC
Products: -
Products: -
?
additional information
?
-
-
Substrates: BamHI displays 98.53% digest efficiency by digitial counting and a digest efficiency of 98.1% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (8/13) GAGN5CTC (13/8), of which it needs 1 on the substrate to be active. It excises 27 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolysis of DNA containing 5-methyl-dC
Products: -
Products: -
?
additional information
?
-
-
Substrates: NdeI displays 67.12% digest efficiency by digitial counting and a digest efficiency of 59.9% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
-
Substrates: BbsI displays 87.35% digest efficiency by digitial counting and a digest efficiency of 91.1% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (8/14) CCAN6GT (15/9): It excises 28 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (11/13) CAAN5GTGG (12/10), of which it needs 2 on the substrate to be active. It excises 33 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (11/13) CAAN5GTGG (12/10), of which it needs 2 on the substrate to be active. It excises 33 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolysis of DNA containing 5-methyl-dC
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolysis of DNA containing 5-methyl-dC
Products: -
Products: -
?
additional information
?
-
-
Substrates: restriction endonuclease activity and modification methylase activity occur as separate proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the REBASE database contains information about recognition sites and cleavage sites
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity is observed using 1-site DNA as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: schematic view of the hydrogen-bond interactions of the DNA with each subunit of the protein for the 2TA and 1TA complexes, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: development of a self-cleavage assay to measure EcoRV-DNA competitive binding and to evaluate the influence of water activity, pH and salt concentration on the DNA substrate binding stringency of the enzyme in the absence of divalent ions. The enzyme can readily distinguish specific and nonspecific sequences. The relative specific-nonspecific binding constant increases strongly with increasing neutral solute concentration and with decreasing pH. In addition to divalent ions, water activity and pH are key parameters that strongly modulate binding specificity of EcoRV
Products: -
Products: -
?
additional information
?
-
-
Substrates: EcoRV utilizes intersegmental hopping to a greater extent than does EcoRI
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (9/12) ACN5CTCC (10/7), of which it needs 2 on the substrate to be active. It excises 27 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
Substrates: BstXI displays 77.76% digest efficiency by digitial counting and a digest efficiency of 61.5% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BstXI displays 77.76% digest efficiency by digitial counting and a digest efficiency of 61.5% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BstXI displays 77.76% digest efficiency by digitial counting and a digest efficiency of 61.5% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BsrGI displays 93.78% digest efficiency by digitial counting and a digest efficiency of 97.7% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BsrGI displays 93.78% digest efficiency by digitial counting and a digest efficiency of 97.7% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BsrGI displays 93.78% digest efficiency by digitial counting and a digest efficiency of 97.7% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BstEII displays 97.72% digest efficiency by digitial counting and a digest efficiency of 99.2% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BstEII displays 97.72% digest efficiency by digitial counting and a digest efficiency of 99.2% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BstEII displays 97.72% digest efficiency by digitial counting and a digest efficiency of 99.2% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: BsrGI displays 93.78% digest efficiency by digitial counting and a digest efficiency of 97.7% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: no hydrolysis of DNA containing 5-methyl-dC
Products: -
Products: -
?
additional information
?
-
Substrates: NcoI displays 94.42% digest efficiency by digitial counting
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (7/13) GAYN5RTC (14/9). It excises 27 bp, and does not require S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: restriction endonuclease activity and modification methylase activity occur as separate proteins
Products: -
Products: -
?
additional information
?
-
Substrates: HpaI displays 95.84% digest efficiency by digitial counting and a digest efficiency of 99.4% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (10/12) CGAN6TGC (12/10), of which it needs 2 on the substrate to be active. It excises 32 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: MvaI restriction endonuclease cuts 5'-CC-/-AGG-3'/5'-CC-/-TGG-3' sites. N4-methylation of the inner cytosines, Cm4CAGG/Cm4CTGG, protects the site against MvaI cleavage. MvaI nicks the G-strand of the related sequence (CCGGG/CCCGG, BcnI site) if the inner cytosines are C5-methylated: Cm5C-/-GGG/CCm5CGG. At M.SssI-methylated SmaI sites, of M.SssI DNA methyltransferase, where two oppositely oriented methylated BcnI sites partially overlap, double-nicking leads to double-strand cleavage (CCm5C-/-GGG/CCm5C-/-GGG) generating fragments with blunt ends
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (10/15) ACN4GTAYC (12/7), of which it needs 2 on the substrate to be active. It excises 28 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: usage of a plasmid containing a single BspRI recognition site to analyze kinetically nicking and second-strand cleavage under steady-state conditions. Cleavage of the supercoiled plasmid goes through a relaxed intermediate indicating sequential hydrolysis of the two strands. BspRI cleaves the two DNA strands sequentially
Products: -
Products: -
?
additional information
?
-
-
Substrates: BsgI displays 94.74% digest efficiency by digitial counting and a digest efficiency of 99.3% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
Substrates: the head-to-head configuration substrate, pUC19HH1, is digested both as closed circular DNA and linear DNA
Products: -
Products: -
?
additional information
?
-
Substrates: MmeI recognizes an asymmetric sequence TCCRAC and cuts 20 bp downstream
Products: -
Products: -
-
additional information
?
-
Substrates: MmeI can cut across a double-strand break. MMeI shows78.5% digestion with a 2-base overhang, 96.6% with a 3-base overhang, and 90.6% with two sites on the same DNA molecule. A DNA molecule containing a 1-base overhang shows minimal digestion, and blunt-ended oligos with no complementary overhang produce no digestion at all
Products: -
Products: -
-
additional information
?
-
-
Substrates: recognition site is 5-GAAGA-3, cleavage occurs 7 or 8 bp downstream and generates a single 3-protruding nucleotide
Products: -
Products: -
?
additional information
?
-
-
Substrates: recognition site is 5-GAAGA-3, cleavage occurs 7 or 8 bp downstream and generates a single 3-protruding nucleotide
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (12/7) RCCGGY (7/12), of which it needs 2 on the substrate to be active. It excises 20 bp, and does not require S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: NheI displays 96.06% digest efficiency by digitial counting and a digest efficiency of 96.3% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
-
Substrates: BtsI recognizes and digests at GCAGTG(2/0)
Products: -
Products: -
?
additional information
?
-
-
Substrates: BmtI displays 73.23% digest efficiency by digitial counting and a digest efficiency of 72.8% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
-
Substrates: BmtI displays 73.23% digest efficiency by digitial counting and a digest efficiency of 72.8% by Bioanalyzer analysis
Products: -
Products: -
-
additional information
?
-
-
Substrates: restriction endonuclease activity and modification methylase activity occur as separate proteins
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolysis DNA containing 5-methyl-dC or 5-fluoro-dU
Products: -
Products: -
?
additional information
?
-
Substrates: PflMI displays 96.03% digest efficiency by digitial counting
Products: -
Products: -
-
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (7/12) GAACN6CTC (13/8), of which it needs 2 on the substrate to be active. It excises 28 bp, and does not require S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolysis DNA containing 5-methy-dC
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme does not cut Sulfolobus acidocaldarius DNA, as the recognition sequence GGCC in this DNA contains modified nucleotides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme recognizes tetranucleotide GGCC and cleaves DNA in the center of this sequence. DNA of Sulfolobus acidocaldarius is not cleaved by the enzyme
Products: -
Products: -
?
additional information
?
-
-
Substrates: TatI recognition site is 5-AGTACA-3, the enzyme cleaves between first and second nucleotides generating 5-ends protruding four bases, TauI recognition site is 5-GCGSGC-3, the enzyme cleaves between fourth and fifth nucleotides generating 3-ends protruding three bases
Products: -
Products: -
?
additional information
?
-
Substrates: XcmI displays 98.05% digest efficiency by digitial counting
Products: -
Products: -
-
additional information
?
-
-
Substrates: XbaI displays 99.25% digest efficiency by digitial counting
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA containing F5dC + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dC
Products: -
Products: -
?
DNA containing F5dU + H2O
?
Substrates: perfectly hydrolyzes the DNA containing 5-fluoro-dU
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: primary function is the inactivation of foreign DNA invading bacteria
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: sequence-specific endonucleolytic digestion of infecting DNA
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: sequence-specific endonucleolytic digestion of infecting DNA
Products: -
Products: -
?
DNA + H2O
?
-
Substrates: sequence-specific endonucleolytic digestion of infecting DNA
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: the enzyme recognizes the sequence 5'-Pu*CCGGPy and cleaves it as indicated by the star
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage by EcoRI is staggered, producing fragments with 4-nucleotide single-stranded overhangs, recognition sequence is GAATTC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage by EcoRV is staggered, producing fragments with 4-nucleotide single-stranded overhangs, recognition sequence is GATATC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: EcoRI recognizes 5'-GAATTC-3' while EcoRV recognizes 5'-GATATC-3', leaving overhangs and blunt DNA segments, respectively
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: cleavage by HindII is blunt, producing fragments with flush ends
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: LmoJ3 recognizes GCNGC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: LmoJ2 recognizes GCWGC (W is A or T)
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: LmoJ2 recognizes GCWGC (W is A or T)
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
Substrates: LmoJ3 recognizes GCNGC
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
double-stranded DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
-
Substrates: -
Products: -
Products: -
?
dsDNA + H2O
?
-
Substrates: recognition sequence is 5-GGACC-3/3-CCTGG-5, enzyme cleaves between the guanosin residues at both strands
Products: sticky end fragments
Products: sticky end fragments
?
dsDNA + H2O
?
-
Substrates: recognition sequence is 5-GGACC-3/3-CCTGG-5, enzyme cleaves between the guanosin residues at both strands
Products: sticky end fragments
Products: sticky end fragments
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (10/12) GCAN6TGC (12/10), of which it needs 2 on the substrate to be active. It excises 32 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (7/12) GAACN6TCC (12/7), of which it needs 2 on the substrate to be active. It excises 27 bp, and does not require S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (8/13) GAGN5CTC (13/8), of which it needs 1 on the substrate to be active. It excises 27 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
Substrates: no hydrolysis of DNA containing 5-methyl-dC
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (8/14) CCAN6GT (15/9): It excises 28 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (11/13) CAAN5GTGG (12/10), of which it needs 2 on the substrate to be active. It excises 33 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (11/13) CAAN5GTGG (12/10), of which it needs 2 on the substrate to be active. It excises 33 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: schematic view of the hydrogen-bond interactions of the DNA with each subunit of the protein for the 2TA and 1TA complexes, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: EcoRV utilizes intersegmental hopping to a greater extent than does EcoRI
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (9/12) ACN5CTCC (10/7), of which it needs 2 on the substrate to be active. It excises 27 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (7/13) GAYN5RTC (14/9). It excises 27 bp, and does not require S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (10/12) CGAN6TGC (12/10), of which it needs 2 on the substrate to be active. It excises 32 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (10/15) ACN4GTAYC (12/7), of which it needs 2 on the substrate to be active. It excises 28 bp, and requires S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (12/7) RCCGGY (7/12), of which it needs 2 on the substrate to be active. It excises 20 bp, and does not require S-adenosyl-L-methionine
Products: -
Products: -
?
additional information
?
-
-
Substrates: BtsI recognizes and digests at GCAGTG(2/0)
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has the recognition sequence (7/12) GAACN6CTC (13/8), of which it needs 2 on the substrate to be active. It excises 28 bp, and does not require S-adenosyl-L-methionine
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
does not need S-adenosyl-L-methionine as cofactor
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
NaCl
optimally active at NaCl concentrations ranging from 100-200 mM
Ni2+
-
can replace Mn2+ but yields a much lower activity than Mg2+, highest activity at 0.1 mM, inhibitory at high concentrations
additional information
Ca2+
-
site-specific binding of enzyme to DNA in presence of Ca2+, without the catalytic cleavage. Binding kinetic parameters in presence of Ca2+ are consistent with those in presence of Mg2+
Ca2+
-
in the presence of Ca2+ ions, EcoRII binds to the target DNA but does not cleave the DNA strand
Co2+
-
may substitute for Mg2+, much less effective, relaxed specificity of enzyme
Co2+
-
can replace Mn2+ but yields a much lower activity than Mg2+, highest activity at 0.1 mM, inhibitory at high concentrations
Mg2+
-
site-specific binding of enzyme to DNA in presence of Mg2+, and site-specific cleavage reaction. Binding kinetic parameters in presence of Ca2+ are consistent with those in presence of Mg2+
Mg2+
-
EcoRV binds two magnesium ions in the active site. One of these ions, Mg2+A, binds to the phosphate group where the cleavage occurs and is required for catalysis. The other, Mg2+B, is crucial for achieving a tightly bound protein-DNA complex and stabilizing a conformation that allows cleavage, structure analysis, molecular dynamics simulations, overview
Mn2+
-
may substitute for Mg2+, much less effective, relaxed specificity of enzyme
Mn2+
-
can replace Mn2+ but yields a much lower activity than Mg2+, highest activity at 0.3 mM, inhibitory at high concentrations
Mn2+
-
required for activity of mutant which carries an insertion of the Green Fluorescence Protein into a loop which is located between the endonuclease and splicing domains of the Sce VMA1 intein
additional information
-
the salt dependence of Knsp-sp for EcoRV-DNA binding, kinetics, overview
additional information
-
the positioning and role of metal ions in DNA recognition sites might reflect important properties of protein-DNA interaction. Detection of 5 different metal ion mechanisms, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cucurbit[6]uril
cucurbiturils are supramolecular inhibitors of DNA restriction by type II endonucleases. They inhibit the enzymatically catalyzed restriction of plasmids and linear DNA
cucurbit[6]uril
cucurbiturils are supramolecular inhibitors of DNA restriction by type II endonucleases. They inhibit the enzymatically catalyzed restriction of plasmids and linear DNA
cucurbit[7]uril
cucurbiturils are supramolecular inhibitors of DNA restriction by type II endonucleases. They inhibit the enzymatically catalyzed restriction of plasmids and linear DNA
cucurbit[7]uril
cucurbiturils are supramolecular inhibitors of DNA restriction by type II endonucleases. They inhibit the enzymatically catalyzed restriction of plasmids and linear DNA
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
benzo[a]pyrene-deoxyguanosine lesions diminish the binding of R.EcoRII to its DNA recognition sequences in a site-selective manner. Cleavage of this lesions is completely blocked. Sequences with the lesions at the 5'-guanine are effectors of cleavage in contrast to those at the 3'-guanine
-
additional information
-
a substitution of DNA with 2'-O-methyl nucleotide and phosphorothioate shows inhibitory effect on enzyme activity
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
MmeI endonuclease is sensitive only to top strand methylation
-
additional information
-
a substitution of DNA with 2'-O-methyl nucleotide and phosphorothioate shows inhibitory effect on enzyme activity
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
cleavage is inhibitied by 5-methyl-cytosine methylation
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
a substitution of DNA with 2'-O-methyl nucleotide and phosphorothioate shows inhibitory effect on enzyme activity
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
a substitution of DNA with 2'-O-methyl nucleotide and phosphorothioate shows inhibitory effect on enzyme activity
-
additional information
-
increasing proportions of uracil in DNA substrates increases inhibition of restriction enzyme digests
-
additional information
-
a substitution of DNA with 2'-O-methyl nucleotide and phosphorothioate shows inhibitory effect on enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
MmeI endonuclease activity requires S-adenosyl-L-methionine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000027
linear mNeonGreen DNA
-
37°C, pH not specified in the publication
-
additional information
additional information
-
determination of kinetic parameters for two-step DNA cleavage reactions by the enzyme using a DNA-immobilized 27 Mhz quartz crystal microbalance
-
additional information
additional information
-
kinetics of EcoRV-DNA binding, detailed overview. Slow kinetics of complex formation at pH 7.6
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0037
linear mNeonGreen DNA
-
37°C, pH not specified in the publication
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.5 - 8
7.6
7.9
8.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
-
strong pH dependence of the specific-nonspecific association binding constant ratio, increasing about 500fold between pH 8.0 and pH 5.5, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60 - 70
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 70
-
at 40°C the activity is about 5times lower than at 60-70°C
55
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC14688, enzyme NcuI, a homoisoschizomer of MboII
-
-
brenda
Q5D6Y5: endonuclease subunit R1, Q5D6Y4: endonuclease subunit R2
Q5D6Y5; Q5D6Y4
UniProt
brenda
-
-
-
brenda
enzyme Eco311, Eco47III, Eco571, EcoNI, EcoRI, EcoRII, EcoRV and EciI
-
-
brenda
enzymes BsaAI, BsaBI, BsrI, BstEII, BstXI, BsmI, BsmAI, and enzyme BsePI
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
evolution
-
the fact that these enzymes cut DNA at specific locations mark them as type II systems, as opposed to the type I enzymes that cut DNA randomly, but in terms of gene organization and protein assembly, most type IIB restriction-modification systems have more in common with type I than with other type II systems
-
malfunction
-
treatment of pT7Blue plasmid with recombinant protein UPV229 completely blocks UpaP162 restriction enzyme activity
malfunction
Ureaplasma parvum OMC-P162
-
treatment of pT7Blue plasmid with recombinant protein UPV229 completely blocks UpaP162 restriction enzyme activity
-
metabolism
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
the balance between DNA methylation and cleavage of the type II restriction-modification system may be severely affected by transcriptional signals coming from outside the restriction-modification operon. By modulating the activity of the promoter, a broad range of restriction phenotypes for the EcoRI R-M system can be obtained that differ by up to 4 orders of magnitude in biological assays
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
enzyme shows a random, sequential mechanism in which one double-stranded DNA at a time is cleaved within a fully-formed reaction synapse containing multiple bound DNA target sites
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
-
metabolism
-
measurement of restriction digest efficiency using digital cell-free protein synthesis. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
-
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
physiological function
A0A7R7A8H4
REase R.Nph3I constitutes an active restriction-modification system with the adjacent putative MTase NRS3_07 and is sensitive to 6-methyl-adenosine DNA methylation
physiological function
-
the endonucleases from the type IIB restriction-modification systems differ from all other restriction enzymes. The type IIB enzymes cleave both DNA strands at specified locations distant from their recognition sequences, like Type IIS nucleases, but they are unique in that they do so on both sides of the site, to liberate the site from the remainder of the DNA on a short duplex
-
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
type IIP restriction endonucleases are characterized by recognition sequences displaying dyad axes of symmetry (palindromes), and constitute the most abundant class of characterized restriction enzymes
additional information
-
subunit BtsIB mutant shows a different digestion pattern from the wild type BtsI. The mutant BtsIB(R119A) acts as a different restriction enzyme with a previously unreported recognition sequence CAGTG(2/0), which is named as BtsI-1. Compared with wild-type BtsI, BtsI-1 shows different relative activities in NEB restriction enzyme reaction buffers NEB1, NEB2, NEB3 and NEB4 and less star activity. Similar to the wild-type BtsIB subunit, the BtsI-1 B subunit alone can act as a bottom nicking enzyme recognizing CAGTG(-/0)
additional information
-
comparison of the interatomic distances between metal ions and proposed key catalytic residues in the binding sites of seventeen type II restriction endonucleases, data taken from crystal structures
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
additional information
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
-
Show AA Sequence and Transmembrane Helices (958 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
27000
30000
40000
67000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
homodimer
homotetramer
monomer
tetramer
additional information
dimer
Q5D6Y5; Q5D6Y4
the enzyme exists in a dynamic equilibrium between dimeric, tetrameric, and perhaps larger assemblages. BbvCI is composed of two protein subunits (R1 and R2), each containing one catalytic site. Crystallization of the R2 subunit at low pH reveals an elongated dimer with the two catalytic sites located on opposite sides. Subsequent crystallization at physiological pH reveals a tetramer comprising two copies of each subunit, with a pair of deep clefts each containing two catalytic sites appropriately positioned and oriented for DNA cleavage
dimer
in solution the BsaWI protein exists in a dimer-tetramer-oligomer equilibrium, but in the presence of specific DNA forms a tetramer bound to two target sites. Site-directed mutagenesis and kinetic experiments show that BsaWI is active as a tetramer and requires two target sites for optimal activity
dimer
-
subunits, BtsIA and BtsIB. The BtsIB subunit contains the recognition domain, one catalytic domain for bottom strand nicking and part of the catalytic domain for the top strand nicking. BtsIA has the rest of the catalytic domain that is responsible for the DNA top strand nicking. BtsIA alone has no activity unless it mixes with BtsIB to reconstitute the BtsI activity
monomer
-
1 * 28000, the enzyme can form a dimer or a higher order molecule weight complex at high protein concentrations
monomer
the enzyme possesses two active sites responsible for the sequential cleavage of each DNA strand, which has evolved by fusion of a sequence specific nuclease domain, similar to EcoRI, to a nonspecific nuclease domain, similar to FokI
tetramer
Q5D6Y5; Q5D6Y4
the enzyme exists in a dynamic equilibrium between dimeric, tetrameric, and perhaps larger assemblages. BbvCI is composed of two protein subunits (R1 and R2), each containing one catalytic site. Crystallization of the R2 subunit at low pH reveals an elongated dimer with the two catalytic sites located on opposite sides. Subsequent crystallization at physiological pH reveals a tetramer comprising two copies of each subunit, with a pair of deep clefts each containing two catalytic sites appropriately positioned and oriented for DNA cleavage
tetramer
in solution the BsaWI protein exists in a dimer-tetramer-oligomer equilibrium, but in the presence of specific DNA forms a tetramer bound to two target sites. Site-directed mutagenesis and kinetic experiments show that BsaWI is active as a tetramer and requires two target sites for optimal activity
additional information
-
denatured molecular weights of 33000 Da and 67000 Da are obtained
additional information
-
denatured molecular weights of 33000 Da and 67000 Da are obtained
-
additional information
-
denatured molecular weights of 39000 Da and 67000 Da are obtained
additional information
Cytobacillus firmus 2411
-
denatured molecular weights of 39000 Da and 67000 Da are obtained
-
additional information
-
the isolated C-terminal domain dimer has an interface that binds a single cognate DNA molecule whereas the N-terminal domain is a monomer that also binds a single copy of cognate DNA
additional information
-
peptide mapping, tryptic digestion and mass spectrometry analysis, overview
additional information
-
consists of two different polypeptide chains R and M
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of the R2 subunit at low pH reveals an elongated dimer with the two catalytic sites located on opposite sides. Subsequent crystallization at physiological pH reveals a tetramer comprising two copies of each subunit, with a pair of deep clefts each containing two catalytic sites appropriately positioned and oriented for DNA cleavage
Q5D6Y5; Q5D6Y4
structure of BstYI bound to a cognate DNA sequence (AGATCT). The structure reveals the basis for degenerate DNA recognition and offers insight into possibilities and limitations in changing the specificities of closely related restriction enzymes
-
crystal structures of mutant enzyme Q138F bound to GTTAAC, GTCGAC both with and without Ca2+, as well as the structure of the wild-type HincII bound to GTTAAC
the DNA-free apo-enzyme forms a compact enzyme tetramer in the crystal. Four target recognition domains and four endonuclease domains form a starburst-like structure. The complex with a 50 bp double-stranded DNA construct shows all four target recognition domains within the tetramer are individually engaged with four corresponding double-stranded DNA duplexes
crystal structure of MmeI in complex with its DNA substrate (a 29-mer DNA duplex containing a single MmeI recognition site (TCCGAC)) and an S-adenosylmethionine analog sinefungin. The co-crystals are obtained in the presence of sinefungin and diffracted to 2.6 A resolution with synchrotron radiation. They belong to space group P1 with unit cell dimensions of a = 61.87 A, b = 95.29 A, c = 161.96 A, alpha = 72.84°, beta = 89.15°, and gamma = 71.61°, and contain two MmeI/DNA/sinefungin complexes in the crystallographic asymmetric unit
crystal structures of a specific MspI-DNA complex in a monoclinic space group and an orthorhombic space group, at 1.95 A and 2.7 A resolution, respectively. Native enzyme, Hg(OAc)2 derivatives, CH3HgCl derivatives, Sm(OAc)3 derivative
-
single-chain variant scPvuII constructed by tandemly joining the two subunits through the peptide linker Gly-Ser-Gly-Gly. Resolution of 2.35 A, space group P42
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C-terminal 232-419 amino acids fragment, space group P212121, resolution 2.8 A, one molecule per asymmetric unit
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sitting drop vapor diffusion method at 19°C. 1.6 A co-crystal structure of UbaLAI N-terminal domain
A0A291ATB4
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D140A
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
D140A/E167A/K169A
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
D144A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit
D146A
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit
D146A/E177A
Q5D6Y5; Q5D6Y4
slight detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit
D146A/E177A/K179A
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit
D149A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit
D226A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit
E139A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit
E147A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit
E155A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, low activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
E163A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit
E165A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit
E167A
Q5D6Y5; Q5D6Y4
slight activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
E167A/K169A
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
E167G
Q5D6Y5; Q5D6Y4
slight activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
E177A
Q5D6Y5; Q5D6Y4
slight activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit
E177G
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit
E201A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit
E211A
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking and no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit
E218A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, no activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
E227A
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking and no detectable activity in ssDNA nicking, mutant R2 subunit/wild-type R1 subunit
E95A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA and in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
K169A
Q5D6Y5; Q5D6Y4
low activity in dsDNA nicking, mutant R1 subunit/wild-type R2 subunit
K179A
Q5D6Y5; Q5D6Y4
no detectable activity in dsDNA nicking, mutant R2 subunit/wild-type R1 subunit
N138A
Q5D6Y5; Q5D6Y4
no detectable activity in ssDNA nicking, mutant R1 subunit/wild-type R2 subunit
D299A
-
no catalytic activity, mutant like wild-type remains in dimeric form
D329A
-
less than 0.01% residual activity, mutant like wild-type remains in dimeric form
E271A
-
no catalytic activity, mutant like wild-type remains in dimeric form
E337A
-
less than 0.01% residual activity, mutant like wild-type remains in dimeric form
K324A
-
no catalytic activity, mutant like wild-type remains in dimeric form
K328A
-
less than 0.01% residual activity, mutant like wild-type remains in dimeric form
L80P
the mutant enzyme shows decreased DNA methyltransferase activity at a higher temperature in vivo and in vitro than the wild type enzyme, the activity of the L80P mutant is completely lost at a high temperature
M357P
-
mutation converts DNA methyltransferase to a type II endonuclease with 5'-CAGCAG-3' restriction site that cleaves only supercoiled DNA but does not act on nicked or linearized DNA
R330A
L80P
-
the mutant enzyme shows decreased DNA methyltransferase activity at a higher temperature in vivo and in vitro than the wild type enzyme, the activity of the L80P mutant is completely lost at a high temperature
-
DELTA362-465
-
nicking variant of BsaI, nicking occurs on top strand
DELTA440-544
-
nicking variant of BsaI, nicking occurs on bottom strand
K150R/R236G
-
nicking variant of BsaI, nicking occurs on top strand
N349Y
-
nicking variant of BsmAI, nicking occurs on top strand
N415D/R416G
-
variant of BsmAI, both nicking activity and dsDNA cleavage
N441D/R442G
-
nicking variant of BsaI, nicking occurs on bottom strand
R233D
-
nicking variant of BsmBI, nicking on top strand, about 5-10% cleavage of dsDNA
R236D
-
nicking variant of BsaI, nicking on top strand, no cleavage of dsDNA
S128L/R236G
-
nicking variant of BsaI, nicking occurs on top strand
W8C/G207E
-
nicking variant of BsaI, nicking occurs on top strand
Q138F
mutation results in a change in the sequence specificity at the center two base pairs of the cognate recognition site. Alteration in preference of HicII for cutting, but not binding, the three cognate sites differening in the center two base pairs.The Q138F HincII/DNA crystal structures show conformational changes in the protein, bound DNA, and at the protein-DNA interface
D148G
H149L
Q115E
-
deprotonated mutant EcoRI is defective in DNA binding at neutral pH
R119A
-
subunit BtsIB mutant shows a different digestion pattern from the wild type BtsI. The mutant BtsIB(R119A) acts as a different restriction enzyme with a previously unreported recognition sequence CAGTG(2/0), which is named as BtsI-1
E64A
-
monomer crystallizes in space group C2221, two molecules per asymmetric unit
additional information
R330A
-
no catalytic activity, mutant like wild-type remains in dimeric form
D148G
-
binds DNA with 2times reduced affinity compared to wild-type protein
H149L
-
binds DNA with 10times reduced affinity compared to wild-type protein
additional information
-
generation of cleavage specificities of restriction endonucleases by swapping putative target recognition domains between the type IIB enzymes AloI, PpiI from Pseudomonas putida, and TstI from Thermus scotoductus. Individual target recognition domains recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Engineering of a functional type IIB restriction endonuclease having previously undescribed DNA specificity and application in generation of type II enzymes with predetermined specificity
additional information
-
generation of cleavage specificities of restriction endonucleases by swapping putative target recognition domains between the type IIB enzymes AloI, PpiI from Pseudomonas putida, and TstI from Thermus scotoductus. Individual target recognition domains recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Engineering of a functional type IIB restriction endonuclease having previously undescribed DNA specificity and application in generation of type II enzymes with predetermined specificity
-
additional information
-
mutants of BbvCI with defects in one subunit, either R1-R2+ or R1+R2-, cleave only one strand of the 5'-CC-/-TCAGC-3'/5'-GC-/-TGAGG-3' sequence
additional information
-
a truncated protein comprising the first 259 amino acids of the wild-typedisplays wild-type specificity
additional information
-
a truncated protein comprising the first 259 amino acids of the wild-typedisplays wild-type specificity
-
additional information
-
construction of a chimeric endonucelase consisiting of the DNA cleavage domain of isoform BmrI and controller protein C.BclI of the BclI restriction-modification system. The chimeric protein cleaves DNA at specific site in the vicinity of the recognition sequence of C.BclI and requires only half of the C-box sequence for specific cleavage
additional information
-
conversion of enzyme from its wild-type homodimeric form into the enzymatically active single-chain variant scPvuII by tandemly joining the two subunits through the peptide linker Gly-Ser-Gly-Gly, crystallization data
additional information
-
generation of cleavage specificities of restriction endonucleases by swapping putative target recognition domains between the type IIB enzymes AloI, PpiI from Pseudomonas putida, and TstI from Thermus scotoductus. Individual target recognition domains recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Engineering of a functional type IIB restriction endonuclease having previously undescribed DNA specificity and application in generation of type II enzymes with predetermined specificity
additional information
-
enzyme is an endonuclease encoded as a protein insert or intein within the yeast V-ATPase catalytic subunit encoding gene vma1. Insertion of the Green Fluorescence Protein into a loop which is located between the endonuclease and splicing domains of the Sce VMA1 intein. The GFP is functional and the additional GFP domain does not prevent intein excision and endonuclease activity. Contrary to wild-type, mutant requires the presence of Mn2+ and not Mg2+ ions for activity
additional information
-
evolvement of mutant enzymes with altered DNA cleavage specificities by application of an in vivo positive and negative selection system that applies evolutionary pressure either to favor the cleavage of a desired target sequence or to disfavor the cleavage of a nontarget sequence
additional information
-
generation of cleavage specificities of restriction endonucleases by swapping putative target recognition domains between the type IIB enzymes AloI, PpiI from Pseudomonas putida, and TstI from Thermus scotoductus. Individual target recognition domains recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Engineering of a functional type IIB restriction endonuclease having previously undescribed DNA specificity and application in generation of type II enzymes with predetermined specificity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 42
the extract from cells expressing the wild type EcoRII shows the activity both at 30°C and 37°C, the extract from cells expressing the L80P mutant form shows activity at 30°C but not at 37°C, the L80P mutant protein is significantly unstable at 42°C compared with the wild type protein
80
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM phosphate buffer, pH 7.4, 0.1 mM EDTA, 2 mM dithiothreitol, 0.2 M NaCl, 50% glycerol, fully stable for at least 1 year
-
-20°C, phosphate buffer, pH 7.0, 0.1 mM EDTA, 2 mM dithiothreitol, 50% glycerol, stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, phosphocellulose P-11 column chromatography, heparin-Sepharose column chromatography, AH-Sepharose column chromatography, and Blue-Sepharose column chromatography
extremely fast and economical method of restriction endonucleases free from contaminating nuclease activity by a combination of affity partitioning and ion-exchange chromatography
-
heparin column chromatography, Source Q column chromatography, Source S column chromatography, Superdex 75 gel filtration, and ceramic HTP column chromatography
partial
phosphocellulose P-11 column chromatography, heparin Sepharose column chromatography, CM Sephadex C-50 gel filtration or Blue-agarose column chromatography
phosphocellulose P-11 column chromatography, heparin Sepharose column chromatography, CM Sephadex C-50 gel filtration or Blue-agarose column chromatography
-
phosphocellulose P-11 column chromatography, heparin Sepharose column chromatography, CM Sephadex C-50 gel filtration or Blue-agarose column chromatography
-
phosphocellulose P-11 column chromatography, heparin Sepharose column chromatography, CM Sephadex C-50 gel filtration or Blue-agarose column chromatography
-
phosphocellulose P-11 column chromatography, heparin Sepharose column chromatography, CM Sephadex C-50 gel filtration or Blue-agarose column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the complete restriction -modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
expression in Escheichia coli, induction at 15°C results in accumulation in the cytoplasm, induction at 20-37°C results in formation of inclusion bodies
-
expression in Escherichia coli
gene bspRIR, cloning from R genomic DNA, expression in Escherichia coli, which is dependent on the replacement of the native TTG initiation codon with an ATG codon, method development, overview
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a high expression level of the restriction-modification system results in loss of cell viability. High expression levels of the restriction-modification proteins are associated with reduced restriction of invading bacteriophage DNA
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
molecular biology
analysis
-
method for following the digestion of DNA by restriction endonucleases in real time without the use of any extrinsic dyes or labels via linear dichroism spectroscopy
analysis
-
method for following the digestion of DNA by restriction endonucleases in real time without the use of any extrinsic dyes or labels via linear dichroism spectroscopy
analysis
-
method for following the digestion of DNA by restriction endonucleases in real time without the use of any extrinsic dyes or labels via linear dichroism spectroscopy
analysis
-
method for following the digestion of DNA by restriction endonucleases in real time without the use of any extrinsic dyes or labels via linear dichroism spectroscopy
analysis
-
method for following the digestion of DNA by restriction endonucleases in real time without the use of any extrinsic dyes or labels via linear dichroism spectroscopy
analysis
-
method for following the digestion of DNA by restriction endonucleases in real time without the use of any extrinsic dyes or labels via linear dichroism spectroscopy
analysis
-
genetic analysis of 24 Hungarian canine parvovirus strains collected from 2004 to 2008 revealed that all of them are type 2a strains. Due to a seemingly constant point mutation present in most of the Hungarian canine parvovirus 2a strains, a previously described MboII-based rapid identification of CPV2c strains unfortunately cannot be reliably used any more
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
A0A7R7A8H4
sequential 1-day and one-pot workflow covering in vitro protein synthesis and enzymatic assays to confirm the exact function of putative restriction-modification systems. Fluorogenic molecular beacon probes containing all the probable recognition sequences, are designed and used for the fluorogenicenzyme assay
analysis
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
-
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
-
analysis
-
measurement of restriction digest efficiency using digital cell-free protein synthesis, which enables a sensitive trace analysis of undigested DNA at the single-molecule level in a PCR-free manner. The quantitative measurements reveal a considerable variation in the digest efficiency among restriction endonucleases, from less than 70% to more than 99%. None of them shows truly complete digestion within reasonably long periods of reaction time
-
biotechnology
-
evolvement of mutant enzymes with altered DNA cleavage specificities by application of an in vivo positive and negative selection system that applies evolutionary pressure either to favor the cleavage of a desired target sequence or to disfavor the cleavage of a nontarget sequence
biotechnology
-
generation of cleavage specificities of restriction endonucleases by swapping putative target recognition domains between the type IIB enzymes AloI, PpiI from Pseudomonas putida, and TstI from Thermus scotoductus. Individual target recognition domains recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Engineering of a functional type IIB restriction endonuclease having previously undescribed DNA specificity and application in generation of type II enzymes with predetermined specificity
biotechnology
-
generation of cleavage specificities of restriction endonucleases by swapping putative target recognition domains between the type IIB enzymes AloI, PpiI from Pseudomonas putida, and TstI from Thermus scotoductus. Individual target recognition domains recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Engineering of a functional type IIB restriction endonuclease having previously undescribed DNA specificity and application in generation of type II enzymes with predetermined specificity
biotechnology
-
generation of cleavage specificities of restriction endonucleases by swapping putative target recognition domains between the type IIB enzymes AloI, PpiI from Pseudomonas putida, and TstI from Thermus scotoductus. Individual target recognition domains recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Engineering of a functional type IIB restriction endonuclease having previously undescribed DNA specificity and application in generation of type II enzymes with predetermined specificity
biotechnology
-
generation of cleavage specificities of restriction endonucleases by swapping putative target recognition domains between the type IIB enzymes AloI, PpiI from Pseudomonas putida, and TstI from Thermus scotoductus. Individual target recognition domains recognize distinct parts of the bipartite DNA targets of these enzymes and are interchangeable. Engineering of a functional type IIB restriction endonuclease having previously undescribed DNA specificity and application in generation of type II enzymes with predetermined specificity
-
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
tools for the dissection, analysis and reconstruction of DNA
molecular biology
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for future studies of large sets of restriction endonucleases and their activity
molecular biology
site-directed mutagenesis methods are very important in modern molecular biology, biochemistry, and protein engineering. A site-directed mutagenesis method that can be used for multiple mutation generation using type IIs restriction enzymes. This approach is faster and more convenient than the overlap polymerase chain reaction method due to its having fewer reaction steps and being cheaper than, but as convenient as, enzymatic assembly
molecular biology
protein tagging with a wide variety of epitopes and/or fusion partners is used routinely to dissect protein function molecularly. Frequently the required DNA subcloning is inefficient, especially in cases where multiple constructs are desired for a given protein with unique tags. The generated clones have unwanted junction sequences introduced. To add versatile tags into the extracellular domain of the transmembrane protein THSD1, a protein tagging technique is developed that utilizes non-classical type IIS restriction enzymes that recognize non-palindromic DNA sequences and cleave outside of their recognition sites. The method is highly efficient and can precisely fuse any tag into any position of a protein in a scarless manner. IT is cost-efficient and adaptable because it uses commercially available type IIS restriction enzymes and is compatible with the traditional cloning system used by many labs
molecular biology
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
molecular biology
protocol to quickly assemble multigene constructs using a series of simple one-pot assembly steps starting from libraries of cloned and sequenced parts. Basic parts consist of a DNA fragment of interest flanked by two BsaI restriction sites in opposite orientations cloned in a conventional cloning vector with a spectinomycin resistance cassette
molecular biology
protocol to quickly assemble multigene constructs using a series of simple one-pot assembly steps starting from libraries of cloned and sequenced parts
molecular biology
DNA recombination methods employ commerciually available DNA methyltransferase expression vectors, that protect selected sites on different plasmids from particular Type II restriction endonucleases. One methods employs 4 restriction endonuclease and 2 methyltransferases in a discontinuous DNA assembly and produces more desired recombinant plasmids and produces fewer undesired recombination products as conventional subcloning. The 5 restriction endonucleases/methyltransferases continuous DNA assembly is approximately as efficient and specific as conventional Golden Gate assembly, even though in vivo methylation of one plasmid is incomplete
molecular biology
DNA recombination methods employ commercially available DNA methyltransferase expression vectors, that protect selected sites on different plasmids from particular Type II restriction endonucleases. One method employs 4 restriction endonuclease and 2 methyltransferases in a discontinuous DNA assembly and produces more desired recombinant plasmids and produces fewer undesired recombination products as conventional subcloning. The 5 restriction endonucleases/methyltransferases continuous DNA assembly is approximately as efficient and specific as conventional Golden Gate assembly, even though in vivo methylation of one plasmid is incomplete
molecular biology
direct labeling of target RNAs using two consecutive steps of RNA cleavage and enzymatic modification by the combinatorial use of RNA-compatible endonucleases and RNA-extending polymerases for sequence-specific RNA cleavage and subsequent RNA functionalization. The recognition site in the RNA-DNA heteroduplexesis precisely cut with high efficiency. The 3' ends of the cleaved RNAs are selectively and effectively modified by Therminator DNA polymerase, which template-dependently extends the RNA primers with a variety of modified nucleotides
molecular biology
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
-
molecular biology
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
-
molecular biology
Escherichia coli P15
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
-
molecular biology
Gluconobacter oxydans H-15T
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
-
molecular biology
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
-
molecular biology
Bacillus pumilus 2187a
-
a straightforward, general and automatable model system for studying the activity of restriction endonucleases by using massively parallel sequencing is described, which should be highly applicable for the future studies of large sets of restriction endonucleases and their activity
-
molecular biology
-
direct labeling of target RNAs using two consecutive steps of RNA cleavage and enzymatic modification by the combinatorial use of RNA-compatible endonucleases and RNA-extending polymerases for sequence-specific RNA cleavage and subsequent RNA functionalization. The recognition site in the RNA-DNA heteroduplexesis precisely cut with high efficiency. The 3' ends of the cleaved RNAs are selectively and effectively modified by Therminator DNA polymerase, which template-dependently extends the RNA primers with a variety of modified nucleotides
-
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Release 2026.1 (March 2026)
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