3.1.21.5: type III site-specific deoxyribonuclease

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For detailed information about type III site-specific deoxyribonuclease, go to the full flat file.

Reaction

endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates =

Synonyms

ATP-dependent type III restriction endonuclease, BceSI, BsaHI, cj0031, EC 3.1.23, EC 3.1.24, EcoP1, EcoP15, EcoP15I, EcoPI, HinFIII, LlaFI, MmyCI, More, NgoAXP, PhaBI, PspGI, PstII, R.EcoP15I, R.MmyCI, REase, restriction endonuclease PstII, restriction-modification system, StyLTI, type III DNA restriction/modification enzyme, type III R-M enzyme, type III R/M enzyme, type III RE, type III restriction endonuclease, type III restriction enzyme, type III restriction-modification enzyme, type III restriction-modification system, type III RM system, type III testriction-modification enzyme, type III-like restriction endonuclease

ECTree

     3 Hydrolases

         3.1 Acting on ester bonds

             3.1.21 Endodeoxyribonucleases producing 5'-phosphomonoesters

                3.1.21.5 type III site-specific deoxyribonuclease

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Results	in table
7	Activating Compound
831	AA Sequence
2	Application
1	CAS Registry Number
7	Cloned(Commentary)
24	Cofactor
3	Crystallization (Commentary)
7	General Information
1	General Stability
5	Inhibitors
14	Metals/Ions
19	Molecular Weight [Da]
23	Natural Substrates/ Products (Substrates)
65	Organism
2	PDB ID
1	pH Optimum
22	Protein Variants
6	Purification (Commentary)
5	Reaction
1	Reaction Type
62	Reference
1	Renatured (Commentary)
65	Substrates and Products (Substrate)
12	Subunits
97	Synonyms
2	Temperature Optimum [°C]
1	Temperature Stability [°C]

Crystallization

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Crystallization on EC 3.1.21.5 - type III site-specific deoxyribonuclease

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

database information: http://rebase.neb.com

Escherichia coli

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134254

real-time imaging of enzyme at scan rates of 1-3 frames per s. EcoP15I translocates DNA in an ATP-dependent manner, at a rate of 79 bp/s, resulting in the accumulation of supercoiling. EcoP15I bound to its recognition site also makes nonspecific contacts with other DNA sites, thus forming DNA loops and reducing the distance between the two recognition sites

Escherichia coli

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684006

study of enzyme-DNA pre-cleavage complexes by atomic force microscopy. DNA loops observed are formed by a contact between site-bound EcoP15I enzyme and a nonspecific region of DNA, and do not result from translocation. Model for restricition by type III enzymes involving both structural elements, and a functional reason for the unusual site orientation required for the cleavage reaction

Escherichia coli

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683409