Information on EC 3.1.21.4 - type II site-specific deoxyribonuclease

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
3.1.21.4
-
RECOMMENDED NAME
GeneOntology No.
type II site-specific deoxyribonuclease
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
show the reaction diagram
autoinhibition/activation mechanism
-
endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
show the reaction diagram
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
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AloI
Acinetobacter lwoffii Ks 4-8
-
-
-
ApaI
Acetobacter pasteurianus ApaI
-
-
-
ApaLI
Acetobacter pasteurianus ApaLI
-
-
-
AsuI
Anabaena subcylindrica
-
-
AsuII
Anabaena subcylindrica
-
-
Bfi2411I
-
-
Bfi2411I
Bacillus firmus 2411
-
-
-
BspD6I
-
-
BspD6I
-
-
-
BstF5I
Geobacillus stearothermophilus F5
-
-
-
Bsu2413I
-
-
Bsu2413I
Bacillus subtilis 2413
-
-
-
CfrBI
Q04852
-
CspCI
Citrobacter sp.
-
-
CspCI
-
-
-
CstMI
Corynebacterium striatum M82B
-
-
-
DNA restriction endonuclease
-
-
-
-
DNA restriction enzyme
-
-
-
-
DpnI
Streptococcus pneumoniae G41
-
-
-
DsaI
Dactylococcus salina
-
-
EC 3.1.23
-
-
-
-
EC 3.1.24
-
-
-
-
Eco1524I
-
-
Eco31I
Q8RNY7
-
Eco47III
-
-
EcoO109I
-
-
EcoRII
P14633
-
EcoRII
Escherichia coli BNH2586
P14633
-
-
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
-
-
-
-
Esp3I
Eucapsis sp.
-
-
EspI
Eucapsis sp.
-
-
FseI
-
-
GGCC-specific restriction endonuclease
-
-
Hpy188I
Helicobacter pylori J188
-
-
-
Hpy8I
C3XF19
-
Hpy99II
Q9ZN14
-
Hpy99IV
Q9ZLF0
-
Hpy99VIIIP
-
-
HpyAXII
B6ED46
-
HpyF17I
Helicobacter pylori J188
-
-
-
LlaDI
Q93K18
-
LlaII
-
-
-
-
MseI
Q2I0D9
-
MseI
Q2I0D9
-
-
MspA1I
Q6S4U8
-
MspA1I
Q6S4U8
-
-
Mva1269I
Q2QHU9
-
Mva1269I restriction endonuclease
Q2QHU9
-
NheI
Neisseria mucosa heidelbergensis
-
-
NmeDIP
Q9RLM3
-
NspBII
-
-
NspV
P35677
-
Nt.BspD6I
-
large subunit of Bsp6DI
Nt.BspD6I
-
large subunit of Bsp6DI
-
nuclease, deoxyribonucleic restriction endo-
-
-
-
-
nuclease, restriction endodeoxyribo-
-
-
-
-
PabI
G8ZFZ3
-
PvuII
P23657
-
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.EcoRII
-
-
R.EcoRV
-
-
-
-
R.FokI
-
-
-
-
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
Q04852
-
REase
Corynebacterium striatum M82B
-
-
-
REase
-, C3XF19, Q9ZLF0, Q9ZN14
-
REase
Q93K18
-
REase
Q58723, Q58895
-
REase
Q2I0D9
-
REase
Q2I0D9
-
-
REase
Q6S4U8
-
REase
Q6S4U8
-
-
REase
P35677
-
REase
P14229
-
REase
Q6SA25
-
REase
Q194N8
-
REase
P23736
-
REase
Q9F8S3
-
REase
Q9KVZ7
-
restriction endodeoxyribonuclease
-
-
-
-
restriction endonuclease
-
-
-
-
restriction endonuclease EcoRV
-
-
restriction endonuclease SuaI
-
-
restriction enzyme
-
-
-
-
sau96I
P23736
-
sau96I
Staphylococcus aureus Sau96I
-
-
-
site-specific endonuclease BME142I
-
-
site-specific endonuclease BME142I
Bacillus megaterium 142
-
-
-
site-specific endonuclease Bme216I
-
recognition site is identical with the endonuclease AvaII from Anabaena variabilis
site-specific endonuclease Bme216I
Bacillus megaterium 216
-
recognition site is identical with the endonuclease AvaII from Anabaena variabilis
-
site-specific endonuclease BmeI
-
-
site-specific endonuclease BmeI
Bacillus megaterium 216
-
-
-
SmaI
P14229
-
SnaBI
Q6SA25
-
ss.BspD6I
-
small subunit of Bsp6DI
ss.BspD6I
-
small subunit of Bsp6DI
-
Sse9I
Q194N8
-
SspI
Sphaerotilus sp.
-
-
SuiI
Sulfolobus islandicus REN2H1
-
-
-
TfiI
Q9F8S3
-
Tsp451
-
-
TspEI
-
-
type II REase
-
-
type II REase
-
-
-
type II REase
Campylobacter jejuni, Citrobacter sp.
-
-
type II REase
-
-
-
type II REase
Q8RNY7
-
type II REase
-
-
type II REase
Helicobacter pylori J188
-
-
-
type II REase
P23657
-
type II REase
-
-
type II restriction endonuclease
-
-
type II restriction endonuclease
-
-
type II restriction endonuclease
B6ED46
-
type II restriction endonuclease
Helicobacter pylori J188
-
-
-
type II restriction endonuclease
-
-
type II restriction endonuclease
P23657
-
type II restriction endonuclease
-
-
type II restriction endonuclease EcoO109I
-
-
type II restriction enzyme
-
-
-
-
type II restriction enzyme
-
-
type II restriction enzyme
Q04852
-
type II restriction enzyme
-
-
type II restriction enzyme
Corynebacterium striatum M82B
-
-
-
type II restriction enzyme
Q8L3A5
-
type II restriction enzyme
P20588
-
type II restriction enzyme
P00643
-
type II restriction enzyme
-, C3XF19, Q9ZLF0, Q9ZN14
-
type II restriction enzyme
P25260
-
type II restriction enzyme
Q93K18
-
type II restriction enzyme
Q58723, Q58895
-
type II restriction enzyme
-
-
type II restriction enzyme
B2MU09
-
type II restriction enzyme
Q2I0D9
-
type II restriction enzyme
Q2I0D9
-
-
type II restriction enzyme
Q6S4U8
-
type II restriction enzyme
Q6S4U8
-
-
type II restriction enzyme
Q9RLM3
-
type II restriction enzyme
P35677
-
type II restriction enzyme
-
-
type II restriction enzyme
Q6SA27
-
type II restriction enzyme
P14229
-
type II restriction enzyme
Q6SA25
-
type II restriction enzyme
Q194N8
-
type II restriction enzyme
P23736
-
type II restriction enzyme
-
-
type II restriction enzyme
O31074
-
type II restriction enzyme
-
-
type II restriction enzyme
Q9KHV6
-
type II restriction enzyme
-
-
type II restriction enzyme
Q9F8S3
-
type II restriction enzyme
Q9KVZ7
-
type IIB restriction endonuclease
-
-
type IIB restriction endonuclease
-
-
-
type IIE restriction endonuclease
-
-
type IIP REase
-
-
type IIP restriction endonuclease
-
-
type IIS restriction endonuclease
-
-
type IIS restriction endonuclease
-
-
-
type IIS restriction endonuclease
Q8RNY7
-
type IIS restriction endonuclease
-
-
type IIS restriction endonuclease
Q2QHU9
-
type IIS restriction enzyme
-
-
type IIS restriction enzyme
Streptococcus pneumoniae G41
-
-
-
typeIIS restriction endonuclease
-
-
typeIIS restriction endonuclease
Geobacillus stearothermophilus F5
-
-
-
typeIIS restriction endonuclease
-
-
VspI
-
-
XbaI
Xanthomonas badrii
-
-
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
CAS REGISTRY NUMBER
COMMENTARY
9075-08-5
not distinguished from EC 3.1.21.5
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme AatII, and StuI
-
-
Manually annotated by BRENDA team
3 enzymes: Apa BI, Apa CI and Apa DI
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus ApaI
ApaI
-
-
Manually annotated by BRENDA team
Acetobacter pasteurianus ApaLI
ApaLI
-
-
Manually annotated by BRENDA team
enzyme AlwNI
-
-
Manually annotated by BRENDA team
strain Ks 4-8, isoform AloI
-
-
Manually annotated by BRENDA team
Acinetobacter lwoffii Ks 4-8
strain Ks 4-8, isoform AloI
-
-
Manually annotated by BRENDA team
enzyme AcyI
-
-
Manually annotated by BRENDA team
Anabaena subcylindrica
enzymes AsuI and AsuII
-
-
Manually annotated by BRENDA team
enzyme AvaI, AvaII, AvaIII and enzyme AvrII
-
-
Manually annotated by BRENDA team
strain ATCC 27892
-
-
Manually annotated by BRENDA team
enzyme AhaIII
-
-
Manually annotated by BRENDA team
enzyme SpiI
-
-
Manually annotated by BRENDA team
enzyme BclI
-
-
Manually annotated by BRENDA team
enzyme BcefI
-
-
Manually annotated by BRENDA team
enzyme BcgI
-
-
Manually annotated by BRENDA team
strain 2411
-
-
Manually annotated by BRENDA team
Bacillus firmus 2411
strain 2411
-
-
Manually annotated by BRENDA team
isoform BmrI
-
-
Manually annotated by BRENDA team
strain 142
-
-
Manually annotated by BRENDA team
Bacillus megaterium 142
strain 142
-
-
Manually annotated by BRENDA team
Bacillus megaterium 216
strain 216
-
-
Manually annotated by BRENDA team
enzyme BpuIOI
-
-
Manually annotated by BRENDA team
strain D6
-
-
Manually annotated by BRENDA team
strain D6
-
-
Manually annotated by BRENDA team
enzyme BglI and BglII
-
-
Manually annotated by BRENDA team
enzyme Bsu121I
-
-
Manually annotated by BRENDA team
enzyme BsuRI
-
-
Manually annotated by BRENDA team
enzyme R.BsuFI
-
-
Manually annotated by BRENDA team
strain 2413
-
-
Manually annotated by BRENDA team
Bacillus subtilis 2413
strain 2413
-
-
Manually annotated by BRENDA team
enzyme BbvI and BbvII
-
-
Manually annotated by BRENDA team
enzyme ClaI
-
-
Manually annotated by BRENDA team
enzyme CauII
-
-
Manually annotated by BRENDA team
enzymes CfrI and Cfr101
-
-
Manually annotated by BRENDA team
Citrobacter sp.
-
-
-
Manually annotated by BRENDA team
Corynebacterium striatum M82B
strain M82B
-
-
Manually annotated by BRENDA team
enzyme BalI
-
-
Manually annotated by BRENDA team
Dactylococcus salina
enzyme DsaI
-
-
Manually annotated by BRENDA team
enzyme DrdI and DrdII
-
-
Manually annotated by BRENDA team
enzymes DraII and DraIII
-
-
Manually annotated by BRENDA team
enzymes AflII and AflIII
-
-
Manually annotated by BRENDA team
enzyme SduI
-
-
Manually annotated by BRENDA team
enzyme SfaNI; enzyme SfeI
-
-
Manually annotated by BRENDA team
EcoO109I; EcoRI; EcoRV
-
-
Manually annotated by BRENDA team
EcoRI; EcoRII; EcoRV
-
-
Manually annotated by BRENDA team
enzyme Eco311, Eco47III, Eco571, EcoNI, EcoRI, EcoRII, EcoRV and EciI
-
-
Manually annotated by BRENDA team
enzyme EcoRII
-
-
Manually annotated by BRENDA team
isoform Eco31I
-
-
Manually annotated by BRENDA team
isoform EcoRI
-
-
Manually annotated by BRENDA team
isoform EcoRII
-
-
Manually annotated by BRENDA team
isoform EcoRV
-
-
Manually annotated by BRENDA team
mutant of isoform M.EcoP15I
-
-
Manually annotated by BRENDA team
strain BNH2586
UniProt
Manually annotated by BRENDA team
Escherichia coli BNH2586
strain BNH2586
UniProt
Manually annotated by BRENDA team
Eucapsis sp.
enzymes EspI and Esp3I
-
-
Manually annotated by BRENDA team
enzyme FseI
-
-
Manually annotated by BRENDA team
enzymes Fnu4HI and FnuSII
-
-
Manually annotated by BRENDA team
enzymes BsaAI, BsaBI, BsrI, BstEII, BstXI, BsmI, BsmAI, and enzyme BsePI
-
-
Manually annotated by BRENDA team
enzymes BsaI, BsmBI, BsmAI
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus BstXI
BstXI
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus BstZI
BstZI
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus F5
strain F5
-
-
Manually annotated by BRENDA team
enzyme GdiII; enzyme GsuI
-
-
Manually annotated by BRENDA team
enzyme HaeII
-
-
Manually annotated by BRENDA team
enzyme HaeIII
-
-
Manually annotated by BRENDA team
enzymes HaeI, HaeII and HaeIII
-
-
Manually annotated by BRENDA team
enzyme HhaI; enzyme HhaII
-
-
Manually annotated by BRENDA team
enzyme HhaII
-
-
Manually annotated by BRENDA team
enzymes HindII, HindIII and HinfI
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
enzyme HpaII; enzymes HpaI
-
-
Manually annotated by BRENDA team
-
C3XF19
UniProt
Manually annotated by BRENDA team
fragment
B6ED46
UniProt
Manually annotated by BRENDA team
strain J188
-
-
Manually annotated by BRENDA team
Helicobacter pylori J188
strain J188
-
-
Manually annotated by BRENDA team
enzymes HgiAI, HgiEII, HgiJII and enzyme HgiCI
-
-
Manually annotated by BRENDA team
enzyme KpnI
-
-
Manually annotated by BRENDA team
enzyme KpnI; enzyme Ksp6321
-
-
Manually annotated by BRENDA team
isoform KpnI
-
-
Manually annotated by BRENDA team
subspecies Lactococcus lactis cremoris
UniProt
Manually annotated by BRENDA team
subsp. cremonis LC17-1
-
-
Manually annotated by BRENDA team
enzyme Bsp CI, BspGI, BspHI, BspMI and enzyme BSPMII
-
-
Manually annotated by BRENDA team
enzyme endoR*Bsp
-
-
Manually annotated by BRENDA team
enzymes MaeI, MaeII and MaeIII
-
-
Manually annotated by BRENDA team
enzyme MluI
-
-
Manually annotated by BRENDA team
enzyme MlyI
-
-
Manually annotated by BRENDA team
strain NEB 446
UniProt
Manually annotated by BRENDA team
strain NEB 446
UniProt
Manually annotated by BRENDA team
enzyme MstI
-
-
Manually annotated by BRENDA team
enzymes MboI and MboII
-
-
Manually annotated by BRENDA team
isoform MboII
-
-
Manually annotated by BRENDA team
strain ATCC14688, enzyme NcuI, a homoisoschizomer of MboII
-
-
Manually annotated by BRENDA team
Moraxella cuniculi ATCC14688
strain ATCC14688, enzyme NcuI, a homoisoschizomer of MboII
-
-
Manually annotated by BRENDA team
strain A1
UniProt
Manually annotated by BRENDA team
strain A1
UniProt
Manually annotated by BRENDA team
enzyme MfeI
-
-
Manually annotated by BRENDA team
enzyme NlaIII and NlaIV
-
-
Manually annotated by BRENDA team
isoform NotI
-
-
Manually annotated by BRENDA team
serogroup C
UniProt
Manually annotated by BRENDA team
Neisseria mucosa heidelbergensis
enzyme NheI
-
-
Manually annotated by BRENDA team
enzyme NarI
-
-
Manually annotated by BRENDA team
enzyme NspBII
-
-
Manually annotated by BRENDA team
strain PCC 7524
UniProt
Manually annotated by BRENDA team
enzyme PleI
-
-
Manually annotated by BRENDA team
enzyme PshAI
-
-
Manually annotated by BRENDA team
enzyme PvuII
-
-
Manually annotated by BRENDA team
enzyme PvuII; enzymes PvuI
-
-
Manually annotated by BRENDA team
isoform PvuII
-
-
Manually annotated by BRENDA team
enzyme PstI
-
-
Manually annotated by BRENDA team
enzyme PflMI
-
-
Manually annotated by BRENDA team
enzyme PpuMI
-
-
Manually annotated by BRENDA team
isoform PpiI
-
-
Manually annotated by BRENDA team
enzyme PstI
-
-
Manually annotated by BRENDA team
enzyme SgrAI
-
-
Manually annotated by BRENDA team
strain GI-H, enzyme PspGI
-
-
Manually annotated by BRENDA team
enzyme RleAI
-
-
Manually annotated by BRENDA team
enzyme NruI
-
-
Manually annotated by BRENDA team
isoform Sce-I
-
-
Manually annotated by BRENDA team
isoform SceI
-
-
Manually annotated by BRENDA team
enzymes SnaI, SnaBI and SpeI
-
-
Manually annotated by BRENDA team
Sphaerotilus sp.
enzyme SspI
-
-
Manually annotated by BRENDA team
enzyme SauI
-
-
Manually annotated by BRENDA team
isoform Sau3AI
-
-
Manually annotated by BRENDA team
Staphylococcus aureus Sau96I
Sau96I
-
-
Manually annotated by BRENDA team
enzyme DpnI; enzyme Dpn II
-
-
Manually annotated by BRENDA team
Streptococcus pneumoniae G41
strain G41
-
-
Manually annotated by BRENDA team
enzyme SacI; enzyme SacII
-
-
Manually annotated by BRENDA team
; isoform SuaI, isoschizomer of BspRI
-
-
Manually annotated by BRENDA team
strain REN2H1, isoform SuiI
-
-
Manually annotated by BRENDA team
Sulfolobus islandicus REN2H1
strain REN2H1, isoform SuiI
-
-
Manually annotated by BRENDA team
enzyme SecI
-
-
Manually annotated by BRENDA team
enzymes TaqI
-
-
Manually annotated by BRENDA team
enzymes TaqI; enzyme TaqII
-
-
Manually annotated by BRENDA team
enzymes TatI, TauI
-
-
Manually annotated by BRENDA team
enzyme TfiI
-
-
Manually annotated by BRENDA team
isoform TstI
-
-
Manually annotated by BRENDA team
enzymes Tsp451 and TspEI
-
-
Manually annotated by BRENDA team
enzymes Tth111I and Tth111II
-
-
Manually annotated by BRENDA team
enzymes Uba1105I and Uba1108I
-
-
Manually annotated by BRENDA team
enzyme VspI
-
-
Manually annotated by BRENDA team
Xanthomonas badrii
enzyme XbaI
-
-
Manually annotated by BRENDA team
Xanthomonas badrii
isoform XbaI
-
-
Manually annotated by BRENDA team
enzyme XcmI
-
-
Manually annotated by BRENDA team
enzyme XhoI and XhoII
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
-
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
-
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
-
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
-
reaction mode of type IIB enzyme in one or two polypeptide systems, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
d(G-G-T-T-5'-bromodeoxyuridine-C-C) + H2O
?
show the reaction diagram
-
-
-
-
-
d(G-G-T-T-A-A-C-C) + H2O
?
show the reaction diagram
-
-
-
-
-
d(pT-G-A-A-T-T-C-A) + H2O
?
show the reaction diagram
-
-
-
-
-
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P17743
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
C3XF19, -, Q9ZLF0, Q9ZN14
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
uncultured bacterium, Xanthomonas badrii
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Xanthomonas badrii
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P25260
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q9KVZ7
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P23736
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P35677
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q2I0D9
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q6SA25
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q58723, Q58895
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P00643
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q9F8S3
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q194N8
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q8L3A5
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q9RLM3
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q6SA27
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P14229
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q93K18
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q9KHV6
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
O31074
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q6S4U8
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q04852
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P14633
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P23657
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q8RNY7
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
P20588
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
ColE1 DNA, pBR322 DNA, SV40 DNA
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
single strandede DNA and double stranded DNA
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
cleavage of the DNA strand in DNA,RNA hybrids
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
lambda DNA
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
cleaves DNA before the first C in the sequence 5'-CCWGG3'. W is A or T
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
EcoRII cleaves DNA molecules with only a single recognition site or with very distant sites
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
the enzyme recognizes the target DNA sequence 5'CCGG and cleaves between the two cytosines to produce sticky ends with 5'CG overhangs
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
BstYI recognizes the degenerate sequence 5'-RGATCY-3' (where R is A/G and Y is C/T)
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
cleavage at 5'-G-/-GCGCC-3'. The enzyme cuts only one bond per turnover but acts at individual sites, preferring intact to nicked sites
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
cleavage at 5'-GG-/-CGCC-3'. The enzyme binds two sites, but cleaves only one bond per DNA-binding event
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
cleavage at 5'-GGC-/-GCC-3'. The enzyme cuts both strands at individual sites
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
cleavage at 5'-GGCGC-/-C-3. The enzyme displays an absolute requirement for two sites in close physical proximity, which are cleaved concertedly
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
Eco1524I recognizes the sequence 6-bp palindromic 5'AGG downward arrow CCT3', producing blunt end
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
EcoRII requires simultaneous binding of three rather than two recognition sites in cis to achieve concerted DNA cleavage at a single site
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
HinP1I recognizes and cleaves a palindromic tetranucleotide sequence (G-/-CGC) in double-stranded DNA, producing 2 nt 5' overhanging ends
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
mechanochemical model of induced-fit reactions on DNA. Strongly decreased association rate is obtained on streched DNA
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-, Q2QHU9
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
R.KpnI cleaves the DNA sequence 5'-GGTAC-/-C-3', generating 3' four base overhangs
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of BamHI: GGATCC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of BgII: GCCNNNNNGGC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes, recognition sequence of BglII: AGATCT. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of Bse634I: RCCGGY. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes, recognition sequence of BsoBI: CYCGRG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of BstYI: GATATC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of BstYI: RGATCY. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of Cfr10I: RCCGGY. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of EcoO109I: RGGNCCY. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes, recognition sequence of EcoRI: GAATTC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes, recognition sequence of EcoRII: CCWGG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of FokI: GGATG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of HincII: GTYRAC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes, recognition sequence of HindIII: AAGCTT. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of MspI: CCGG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of MunI: CAATTG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of NaeI: GCCGGC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of NgoMIV: GCCGGC. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
recognition sequence of PvuII: CAGCTG. Recognition sites of type II restriction enzymes are underrepresented in host genomes and in phage genomes
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
BspD6I cleaves both DNA strands within the recognition sequence
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
B6ED46, -
HpyAXII effectively restricts both unmethylated plasmid and chromosomal DNA during natural transformation, the enzyme targets the tetramer 5'-GTAC-3'
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
B2MU09
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
R.Hpy188I recognizes the sequence TCNGA and cleaves between nucleotides N and G to generate a one-base 3' overhang
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
G8ZFZ3, -
the enzyme recognizes 5'-GTAC and leaves a 3'-TA overhang (5'-GTA/C)
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Corynebacterium striatum M82B
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Streptococcus pneumoniae G41
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q6S4U8
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Acetobacter pasteurianus ApaLI
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Staphylococcus aureus Sau96I
-
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Escherichia coli BNH2586
P14633
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Geobacillus stearothermophilus F5
-
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
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Helicobacter pylori J188
-
R.Hpy188I recognizes the sequence TCNGA and cleaves between nucleotides N and G to generate a one-base 3' overhang
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
Q2I0D9
-
-
-
?
DNA + H2O
double-stranded DNA fragments with terminal 5'-phosphates
show the reaction diagram
-
BspD6I cleaves both DNA strands within the recognition sequence
-
-
?
DNA + H2O
?
show the reaction diagram
-
-
-
-
-
DNA + H2O
?
show the reaction diagram
-
-
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
?
show the reaction diagram
-
primary function is the inactivation of foreign DNA invading bacteria
-
-
-
DNA + H2O
?
show the reaction diagram
-
sequence-specific endonucleolytic digestion of infecting DNA
-
-
-
DNA + H2O
?
show the reaction diagram
-
DNA recognition site is GTCTC
-
-
?
DNA + H2O
?
show the reaction diagram
-
enzyme cuts DNA at the recognition site GcwGC, cleavage occurs after the first guanosine base
-
-
?
DNA + H2O
?
show the reaction diagram
-
recognition site is GGCC, enzyme does not cut Sulfolobus acidocaldarius DNA, as the recognition site in this DNA contains modified nucleotides
-
-
?
DNA + H2O
?
show the reaction diagram
Sulfolobus islandicus REN2H1
-
enzyme cuts DNA at the recognition site GcwGC, cleavage occurs after the first guanosine base
-
-
?
dsDNA + H2O
?
show the reaction diagram
-
recognition sequence is 5-GGACC-3/3-CCTGG-5, enzyme cleaves between the guanosin residues at both strands
sticky end fragments
-
?
dsDNA + H2O
?
show the reaction diagram
-
recognition sequence is 5-GCGC-3/3-CGCG-5, enzyme cleaves in the middle of the tetranucleotide sequence
blunt end fragments
-
?
dsDNA + H2O
?
show the reaction diagram
Bacillus megaterium, Bacillus megaterium 216
-
recognizes a specific pentanucleotide
-
-
?
dsDNA + H2O
?
show the reaction diagram
Bacillus megaterium 216
-
recognition sequence is 5-GGACC-3/3-CCTGG-5, enzyme cleaves between the guanosin residues at both strands
sticky end fragments
-
?
pBR322 DNA + H2O
two fragments of 3200 bp and 1700 bp
show the reaction diagram
-
-
-
?
pBR322 DNA + H2O
?
show the reaction diagram
Bacillus megaterium, Bacillus megaterium 216
-
-
-
-
?
pBR322DNA + H2O
pBR322 DNA fragments
show the reaction diagram
-
the tetranucleotide GGCC can be cleaved by SuaI either symmetrically or nonsymmetrically, thus producing termini with a single-stranded end
-
-
?
phage lambda DNA
?
show the reaction diagram
-
-
-
?
pNH20 + H2O
?
show the reaction diagram
Moraxella cuniculi, Moraxella cuniculi ATCC14688
-
84 bp SacI/HindII-fragment
-
?
dsDNA + H2O
?
show the reaction diagram
Bacillus megaterium 142
-
recognition sequence is 5-GCGC-3/3-CGCG-5, enzyme cleaves in the middle of the tetranucleotide sequence
blunt end fragments
-
?
additional information
?
-
-
restriction endonuclease activity and modification methylase activity occur as separate proteins
-
-
-
additional information
?
-
-
the REBASE database contains information about recognition sites and cleavage sites
-
-
-
additional information
?
-
-
recognition site is 5-GAAGA-3, cleavage occurs 7 or 8 bp downstream and generates a single 3-protruding nucleotide
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme does not cut Sulfolobus acidocaldarius DNA, as the recognition sequence GGCC in this DNA contains modified nucleotides
-
-
-
additional information
?
-
-
no activity is observed using 1-site DNA as substrate
-
-
-
additional information
?
-
B2MU09
the head-to-head configuration substrate, pUC19HH1, is digested both as closed circular DNA and linear DNA
-
-
-
additional information
?
-
-
BtsI recognizes and digests at GCAGTG(2/0)
-
-
-
additional information
?
-
-
schematic view of the hydrogen-bond interactions of the DNA with each subunit of the protein for the 2TA and 1TA complexes, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Citrobacter sp.
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme has the recognition sequence (7/13) GAYN5RTC (14/9). It excises 27 bp, and does not require S-adenosyl-L-methionine
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme has the recognition sequence (8/14) CCAN6GT (15/9): It excises 28 bp, and requires S-adenosyl-L-methionine
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme recognizes tetranucleotide GGCC and cleaves DNA in the center of this sequence. DNA of Sulfolobus acidocaldarius is not cleaved by the enzyme
-
-
-
additional information
?
-
Moraxella cuniculi ATCC14688
-
recognition site is 5-GAAGA-3, cleavage occurs 7 or 8 bp downstream and generates a single 3-protruding nucleotide
-
?
additional information
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DNA + H2O
?
show the reaction diagram
-
-
-
-
-
DNA + H2O
?
show the reaction diagram
-
primary function is the inactivation of foreign DNA invading bacteria
-
-
-
DNA + H2O
?
show the reaction diagram
-
sequence-specific endonucleolytic digestion of infecting DNA
-
-
-
dsDNA + H2O
?
show the reaction diagram
Bacillus megaterium, Bacillus megaterium 216
-
recognition sequence is 5-GGACC-3/3-CCTGG-5, enzyme cleaves between the guanosin residues at both strands
sticky end fragments
-
?
additional information
?
-
-
BtsI recognizes and digests at GCAGTG(2/0)
-
-
-
additional information
?
-
-
schematic view of the hydrogen-bond interactions of the DNA with each subunit of the protein for the 2TA and 1TA complexes, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
Citrobacter sp.
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme has the recognition sequence (7/13) GAYN5RTC (14/9). It excises 27 bp, and does not require S-adenosyl-L-methionine
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme has the recognition sequence (8/14) CCAN6GT (15/9): It excises 28 bp, and requires S-adenosyl-L-methionine
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
may substitute for Mg2+, as effective as Mg2+
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+
-
can replace for Mg2+
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
K+
-
10-30 mM required for maximal activity
Mg2+
-
optimal MgCl2 concentraion: 5 mM
Mg2+
-
optimal concentration is 20 mM; required
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mg2+
-
highest activity at 5-7 mM
Mg2+
-
required, optimal concentration: 5 mM
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+
-
required for wild-type activity
Mg2+
-
required for activity
Mg2+
Q04852
required for activity
Mg2+
-
required for activity
Mg2+
Q8L3A5
required for activity
Mg2+
P20588
required for activity
Mg2+
P00643
required for activity
Mg2+
C3XF19, -, Q9ZLF0, Q9ZN14
required for activity; required for activity; required for activity; required for activity
Mg2+
P25260
required for activity
Mg2+
Q93K18
required for activity
Mg2+
Q58723, Q58895
required for activity; required for activity
Mg2+
-
required for activity
Mg2+
Q2I0D9
required for activity
Mg2+
Q6S4U8
required for activity
Mg2+
Q9RLM3
required for activity
Mg2+
P35677
required for activity
Mg2+
-
required for activity
Mg2+
Q6SA27
required for activity
Mg2+
P14229
required for activity
Mg2+
Q6SA25
required for activity
Mg2+
Q194N8
required for activity
Mg2+
P23736
required for activity
Mg2+
-
required for activity
Mg2+
O31074
required for activity
Mg2+
-
required for activity
Mg2+
Q9KHV6
required for activity
Mg2+
-
required for activity
Mg2+
Q9F8S3
required for activity
Mg2+
Q9KVZ7
required for activity
Mg2+
B2MU09
MmeI endonuclease activity requires magnesium ions
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
Mg2+
-
the enzyme requires Mg2+, the optimal concentration is 6 mM
Mn2+
-
can partially replace Mg2+, optimal concentration is 10 mM
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
NaCl
G8ZFZ3
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
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
-
Fe2+, Ni2+, Zn2+ may not substitute for Mg2+
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
additional information
-
the salt dependence of Knsp-sp for EcoRV-DNA binding, kinetics, overview
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ammonium sulfate
-
-
Co2+
-
complete inhibition at 1 mM
High ionic strength
-
irreversible inactivation
-
K+
-
above 100 mM, significant inhibition
NaCl
-
inhibitory above 0.2 mM
Ni2+
-
complete inhibition at 1 mM
Sodium chloride
-
-
Zn2+
-
2 mM, complete inhibition
Mn2+
-
complete inhibition at 3 mM
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
-
cleavage is inhibitied by 5-methyl-cytosine methylation
-
additional information
B2MU09
MmeI endonuclease is sensitive only to top strand methylation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
DNA oligoduplexes
-
containing the specific recognition site activate
-
S-adenosyl-L-methionine
B2MU09
MmeI endonuclease activity requires S-adenosyl-L-methionine
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0004
-
ColE1
-
EcoRI, activated by Co2+, 37C
-
0.003
0.008
ColE1
-
EcoRI, activated by Mg2+
-
0.03
-
d(G-G-T-5-bromodeoxyuridine-A-A-C-C)
-
Hpa, 25C
0.03
-
d(G-G-T-5-bromodeoxyuridine-A-A-C-C)
-
-
0.18
-
d(G-G-T-T-A-A-C-C)
-
HpaI, 25C
7
-
d(pT-G-A-A-T-T-C-A)
-
EcoR1, 12 C
0.005
-
pBR322
-
EcoRI, 37C
-
0.9
-
pJC linearized plasmid DNA
-
BamHI, 37C
-
0.3
0.36
pJC80 DNA
-
BamHI, 37C
-
0.03
-
SV40 DNA
-
EcoRI, 37C
-
0.01
-
Lambda DNA
-
EcoRI, 37C
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0167
-
ColE1
-
EcoRI, activated by Co2+, 37C
-
0.0667
0.133
ColE1
-
EcoRI, activated by Mg2+
-
600
-
d(G-G-T-5-bromodeoxyuridineA-A-C-C)
-
Hpa, 25C
600
-
d(G-G-T-5-bromodeoxyuridineA-A-C-C)
-
-
2830
-
d(G-G-T-T-A-A-C-C)
-
HpaI, 25C
0.0667
-
d(pT-G-A-A-T-T-C-A)
-
EcoRI, 12C
0.0025
-
DNA
-
37C, R1+-R2- mutant
0.0037
-
DNA
-
37C, R1-R2+ mutant
0.018
-
DNA
-
wild type enzyme with 2-site DNA
0.048
-
DNA
-
37C, wild-type enzyme
0.0217
-
Lambda DNA
-
EcoR1, 37C
-
0.0267
-
NTP14 DNA
-
BamHI, 37C
-
0.03
-
pBR322
-
EcoRI, pBR322, 37C
-
0.0367
-
pJC80 DNA
-
BamHI, 37C
-
0.025
-
SV40 DNA
-
EcoR1, 37C
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.1
-
-
pH 7.0, 65C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
G8ZFZ3
-
7.1
7.5
-
EcoRI
7.4
-
-
Sau96I
7.4
-
-
Tth111I
7.5
8.8
-
AvaI
7.5
9
-
AvaII
7.5
-
-
HaeIII
7.5
-
-
Sau3AI
7.5
-
-
Tth111II
7.5
-
-
assay at
7.6
-
-
enzyme form Apa BI and Apa DI
7.6
-
-
DpnI and DpnII
7.9
-
-
Fnu4HI, FnuDII and FnuEI
7.9
-
-
MboI and MboII
7.9
-
-
SalI and SalPI
7.9
-
Xanthomonas badrii
-
XbaI
8
-
-
enzyme form Apa CI
9.5
-
-
BglI and BglII
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
10
-
some activity is detected even at pH 5 and pH 10
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
6
10
-
active from pH 6.0 to pH 10.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
assay at
30
40
-
BglI and BglII
30
-
-
Sau96I and Sau3AI
37
-
-
Ava I and AvaII
37
-
-
EcoRI
37
-
-
FnuEI, FnuHI and FnuDII
37
-
-
HhaI and HhaII
37
-
-
HinfI, Hind II and HindIII
37
-
-
MboI and MboII
37
-
-
DpnI, DPNII
37
-
-
SalI and SalPI
37
-
Xanthomonas badrii
-
XbaI
37
-
-
assay
60
70
-
Tth111I
65
70
-
Tth111II
65
-
-
assay
85
-
G8ZFZ3
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40
70
-
at 40C the activity is about 5times lower than at 60-70C
65
85
-
digestion of T7 DNA
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20000
-
-
enzyme DpnI
22000
-
-
enzyme BamHI
24000
-
-
enzyme HhaII
25000
-
-
enzyme BclI
26000
-
-
enzyme BstI
27000
-
-
enzyme BglII
28000
-
-
gel filtration
28500
-
-
enzyme EcoRI
31000
-
-
enzyme BglI
35000
-
-
gel filtration
40000
-
-
enzyme HpaII
40000
-
-
gel filtration
51000
-
-
gel filtration
54000
57000
-
gel-filtration, wild-type and mutants
60000
-
-
gel filtration
62000
-
Q8RNY7
gel filtration
67000
-
Q8RNY7
calculated molecular mass of Eco31I
68000
-
-
enzyme BsuI
70000
-
-
enzyme HindII
70000
-
-
enzyme DpnII
95000
-
-
enzyme Tth111II
105100
-
B2MU09
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, SDS-PAGE; x * 45600, calculation from nucleotide sequence
?
-
x * 66314, calculation from nucleotide sequence
?
-
x * 67000 + x * 23000, SDS-PAGE
dimer
-
crystallization data, mutant R88A
dimer
-
crystallization data
dimer
-
x * 30000, SDS-PAGE, native mass by gel filtration
dimer
-
2 * 26000, calculated
dimer
-
and monomer, crystallization data
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
dimer
Bacillus megaterium 216
-
x * 30000, SDS-PAGE, native mass by gel filtration
-
heterodimer
-
1 * 70800 + 1 * ?, X-ray crystallography
heterodimer
-
1 * 70800 + 1 * ?, X-ray crystallography
-
homodimer
-
-
monomer
-
1 * 35000, SDS-PAGE
monomer
-
1 * 48000, SDS-PAGE, N-terminal amino acid sequence
monomer
-, Q2QHU9
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
monomer
-
1 * 28000, the enzyme can form a dimer or a higher order molecule weight complex at high protein concentrations
monomer
-
and dimer, crystallization data
tetramer
-
crystallization data
monomer
Moraxella cuniculi ATCC14688
-
1 * 48000, SDS-PAGE, N-terminal amino acid sequence
-
additional information
-
denatured molecular weights of 39000 Da and 67000 Da are obtained
additional information
-
denatured molecular weights of 33000 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
-
consists of two different polypeptide chains R and M
additional information
-
peptide mapping, tryptic digestion and mass spectrometry analysis, overview
additional information
Bacillus firmus 2411
-
denatured molecular weights of 39000 Da and 67000 Da are obtained
-
additional information
Bacillus subtilis 2413
-
denatured molecular weights of 33000 Da and 67000 Da are obtained
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
small and large subunit of Bsp6I
-
crystal structure of EcoO109I and its complex with DNA
-
database information: http://rebase.neb.com
-
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
P17743
hanging-drop method
-
three-dimensional model of the enzyme's catalytic domain
-
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
-
C-terminal 232-419 amino acids fragment, space group P212121, resolution 2.8 A, one molecule per asymmetric unit
-
both native enzyme and as selenomethionyl derivative
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
10
-
stable from pH 6.0 to pH 10.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
42
P14633
the extract from cells expressing the wild type EcoRII shows the activity both at 30C and 37C, the extract from cells expressing the L80P mutant form shows activity at 30C but not at 37C, the L80P mutant protein is significantly unstable at 42C compared with the wild type protein
55
-
-
stable up to
80
-
-
30 min, 50% loss of activity
80
-
-
the enzyme is highly stable at temperatures up to 80C
85
-
G8ZFZ3
1 h, the enzyme retains approximately 50% of its activity
95
-
-
half-life: 2 h
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in dilute solutions at 37C, 50% inactivation after 30 min
-
inactivation by lyophilization
-
enzyme remains active following 30 cycles of thermocycling
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 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
-
-20C, phosphate buffer, pH 7.0, 0.1 mM EDTA, 2 mM dithiothreitol, 50% glycerol, stable
-
-20C, stable for at least 6 months
-
4C, stable
-
-20C, 50% glycerol, 8-12 months no appreciable loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate fractionation, phosphocellulose P-11 column chromatography, heparin-Sepharose column chromatography, AH-Sepharose column chromatography, and Blue-Sepharose column chromatography
Q8RNY7
EcoRI and EcoRV; extremely fast and economical method of restriction endonucleases free from contaminating nuclease activity by a combination of affity partitioning and ion-exchange chromatography
-
HiTrap heparin column chromatography
-
wild-type and mutant enzymes
P17743
heparin column chromatography, Source Q column chromatography, Source S column chromatography, Superdex 75 gel filtration, and ceramic HTP column chromatography
B2MU09
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloning of the complete restriction-modification system in Escherichia coli
-
expressed in Escherichia coli
-
cloning of the complete restriction -modification system in Escherichia coli
-
expression in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
expressed in Escherichia coli strain BNH670
P14633
expressed in Escherichia coli strain JM109
-
expressed in Escherichia coli strains ER2267 and HMS174
Q8RNY7
cloning of the complete restriction-modification system in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
expressed in Escherichia coli strains ER2925(DE3) and BL21(DE3)
B6ED46
cloning of the complete restriction-modification system 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
-
expressed in Escherichia coli strain ER2683
B2MU09
cloning of the complete restriction-modification system in Escherichia coli
-
expressed in Escherichia coli strain K-12
P23657
expression in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
expression in Escherichia coli via a T7 expression system
-
expression in Escheichia coli, induction at 15C results in accumulation in the cytoplasm, induction at 20-37C results in formation of inclusion bodies
-
expression in Escherichia coli
-
cloning of the complete restriction-modification system in Escherichia coli
-
expressed in Escherichia coli JM109 DE3 cells
-
cloning of the complete restriction-modification system in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
K263A
-
inactive mutant with truncated EcoRII N-domain
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
P14633
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
-
no catalytic activity, mutant like wild-type remains in dimeric form
R330A
-
inactive mutant with truncated EcoRII C-domain
R88A
-
crystallization data, autoinhibition/activation mechanism
L80P
Escherichia coli BNH2586
-
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
DELTA446-544
-
nicking variant of BsaI
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
-
variant of BsaI, cleavage of dsDNA
N441D/R442G
-
nicking variant of BsaI, nicking occurs on bottom strand
R221D
-
nicking variant of BsmAI, nicking on top 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
R236G
-
nicking variant of BsaI, 5-10% cleavage of dsDNA
R386S
-
nicking variant of BsaI, nicking occurs on top strand
R438D
-
nicking variant of BsmBI, nicking on bottom strand
R438G
-
nicking variant of BsmBI
R442G
-
nicking variant of BsaI, 5% 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
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
Q138F
P17743
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
D317A
-
84% of DNA binding compared to wild-type
D321A
-
119% of DNA binding compared to wild-type
D328A
-
76% of DNA binding compared to wild-type
D329A
-
123% of DNA binding compared to wild-type
H291A
-
96% of DNA binding compared to wild-type
H368A
-
129% of DNA binding compared to wild-type
N308A
-
104% of DNA binding compared to wild-type
D148A
-
only traces of DNA cleavage activity when used in large excess
D148G
-
binds DNA with 2times reduced affinity compared to wild-type protein; only traces of DNA cleavage activity when used in large excess
H149L
-
binds DNA with 10times reduced affinity compared to wild-type protein; no cleavage activity
Q115E
-
deprotonated mutant EcoRI is defective in DNA binding at neutral pH
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
Acinetobacter lwoffii Ks 4-8
-
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
-
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
-
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
Q175E
-
only traces of DNA cleavage activity when used in large excess
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
E64A
-
monomer crystallizes in space group C2221, two molecules per asymmetric unit
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
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
biotechnology
Acinetobacter lwoffii Ks 4-8
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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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analysis
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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
analysis
-
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
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
-
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
analysis
Citrobacter sp.
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type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
molecular biology
Citrobacter sp.
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type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
analysis
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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
-
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
-
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
analysis
-
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
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
-
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
analysis
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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
-
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
-
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
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
-
type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA
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
G8ZFZ3
tools for the dissection, analysis and reconstruction of DNA
analysis
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the enzyme can be used in DNA-based diagnostic applications
biotechnology
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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
analysis
Xanthomonas badrii
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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