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

BRENDA support

Literature summary extracted from

  • Marshall, J.J.; Halford, S.E.
    The type IIB restriction endonucleases (2010), Biochem. Soc. Trans., 38, 410-416.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.21.4 S-adenosyl-L-methionine required Geobacillus stearothermophilus
3.1.21.4 S-adenosyl-L-methionine required Lysinibacillus sphaericus
3.1.21.4 S-adenosyl-L-methionine required Weizmannia coagulans
3.1.21.4 S-adenosyl-L-methionine required Bacillus pumilus
3.1.21.4 S-adenosyl-L-methionine required Citrobacter sp.
3.1.21.4 S-adenosyl-L-methionine required Acinetobacter lwoffii
3.1.21.4 S-adenosyl-L-methionine required Campylobacter jejuni

Application

EC Number Application Comment Organism
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Geobacillus stearothermophilus
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Lysinibacillus sphaericus
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Pseudomonas putida
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Neisseria meningitidis
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Weizmannia coagulans
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Bacillus pumilus
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Citrobacter sp.
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Haemophilus aegyptius
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Acinetobacter lwoffii
3.1.21.4 analysis type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Campylobacter jejuni
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Geobacillus stearothermophilus
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Lysinibacillus sphaericus
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Pseudomonas putida
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Neisseria meningitidis
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Weizmannia coagulans
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Bacillus pumilus
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Citrobacter sp.
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Haemophilus aegyptius
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Acinetobacter lwoffii
3.1.21.4 molecular biology type II REases are widely used as tools for the dissection, analysis and reconstruction of DNA Campylobacter jejuni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.21.4 additional information Weizmannia coagulans 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 ?
-
 ?
3.1.21.4 additional information Acinetobacter lwoffii 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 ?
-
 ?
3.1.21.4 additional information Lysinibacillus sphaericus 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 ?
-
 ?
3.1.21.4 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 ?
-
 ?
3.1.21.4 additional information Neisseria meningitidis 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 ?
-
 ?
3.1.21.4 additional information Pseudomonas putida 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 ?
-
 ?
3.1.21.4 additional information Acinetobacter lwoffii 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 ?
-
 ?
3.1.21.4 additional information Haemophilus aegyptius the enzyme has the recognition sequence (7/13) GAYN5RTC (14/9). It excises 27 bp, and does not require S-adenosyl-L-methionine ?
-
 ?
3.1.21.4 additional information Bacillus pumilus 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 ?
-
 ?
3.1.21.4 additional information Campylobacter jejuni the enzyme has the recognition sequence (8/14) CCAN6GT (15/9): It excises 28 bp, and requires S-adenosyl-L-methionine ?
-
 ?
3.1.21.4 additional information Geobacillus stearothermophilus 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 ?
-
 ?
3.1.21.4 additional information Citrobacter sp. 2144 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.21.4 Acinetobacter lwoffii
-
-
-
3.1.21.4 Bacillus pumilus
-
-
-
3.1.21.4 Campylobacter jejuni
-
-
-
3.1.21.4 Citrobacter sp.
-
-
-
3.1.21.4 Citrobacter sp. 2144
-
-
-
3.1.21.4 Geobacillus stearothermophilus
-
-
-
3.1.21.4 Haemophilus aegyptius
-
-
-
3.1.21.4 Lysinibacillus sphaericus
-
-
-
3.1.21.4 Neisseria meningitidis
-
-
-
3.1.21.4 Pseudomonas putida
-
-
-
3.1.21.4 Weizmannia coagulans
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.21.4 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 Weizmannia coagulans ?
-
 ?
3.1.21.4 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 Acinetobacter lwoffii ?
-
 ?
3.1.21.4 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 Lysinibacillus sphaericus ?
-
 ?
3.1.21.4 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 Citrobacter sp. ?
-
 ?
3.1.21.4 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 Neisseria meningitidis ?
-
 ?
3.1.21.4 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 Pseudomonas putida ?
-
 ?
3.1.21.4 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 Acinetobacter lwoffii ?
-
 ?
3.1.21.4 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 Haemophilus aegyptius ?
-
 ?
3.1.21.4 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 Bacillus pumilus ?
-
 ?
3.1.21.4 additional information the enzyme has the recognition sequence (8/14) CCAN6GT (15/9): It excises 28 bp, and requires S-adenosyl-L-methionine Campylobacter jejuni ?
-
 ?
3.1.21.4 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 Geobacillus stearothermophilus ?
-
 ?
3.1.21.4 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 Citrobacter sp. 2144 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.21.4 dimer
-
 Lysinibacillus sphaericus
3.1.21.4 heterodimer
-
 Weizmannia coagulans
3.1.21.4 heterodimer
-
 Bacillus pumilus
3.1.21.4 monomer
-
 Pseudomonas putida
3.1.21.4 monomer
-
 Haemophilus aegyptius
3.1.21.4 monomer
-
 Acinetobacter lwoffii
3.1.21.4 monomer
-
 Campylobacter jejuni
3.1.21.4 More consists of two different polypeptide chains R and M Neisseria meningitidis

Synonyms

EC Number Synonyms Comment Organism
3.1.21.4 AlfI
-
 Acinetobacter lwoffii
3.1.21.4 AloI
-
 Acinetobacter lwoffii
3.1.21.4 BaeI
-
 Lysinibacillus sphaericus
3.1.21.4 BcgI
-
 Weizmannia coagulans
3.1.21.4 BplI
-
 Bacillus pumilus
3.1.21.4 BsaXI
-
 Geobacillus stearothermophilus
3.1.21.4 CjeI
-
 Campylobacter jejuni
3.1.21.4 CspCI
-
 Citrobacter sp.
3.1.21.4 HaeVI
-
 Haemophilus aegyptius
3.1.21.4 NmeDI
-
 Neisseria meningitidis
3.1.21.4 PPII
-
 Pseudomonas putida
3.1.21.4 type II REase
-
 Geobacillus stearothermophilus
3.1.21.4 type II REase
-
 Lysinibacillus sphaericus
3.1.21.4 type II REase
-
 Pseudomonas putida
3.1.21.4 type II REase
-
 Neisseria meningitidis
3.1.21.4 type II REase
-
 Weizmannia coagulans
3.1.21.4 type II REase
-
 Bacillus pumilus
3.1.21.4 type II REase
-
 Citrobacter sp.
3.1.21.4 type II REase
-
 Haemophilus aegyptius
3.1.21.4 type II REase
-
 Acinetobacter lwoffii
3.1.21.4 type II REase
-
 Campylobacter jejuni
3.1.21.4 type IIB restriction endonuclease
-
 Geobacillus stearothermophilus
3.1.21.4 type IIB restriction endonuclease
-
 Lysinibacillus sphaericus
3.1.21.4 type IIB restriction endonuclease
-
 Pseudomonas putida
3.1.21.4 type IIB restriction endonuclease
-
 Neisseria meningitidis
3.1.21.4 type IIB restriction endonuclease
-
 Weizmannia coagulans
3.1.21.4 type IIB restriction endonuclease
-
 Bacillus pumilus
3.1.21.4 type IIB restriction endonuclease
-
 Citrobacter sp.
3.1.21.4 type IIB restriction endonuclease
-
 Haemophilus aegyptius
3.1.21.4 type IIB restriction endonuclease
-
 Acinetobacter lwoffii
3.1.21.4 type IIB restriction endonuclease
-
 Campylobacter jejuni

General Information

EC Number General Information Comment Organism
3.1.21.4 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 Geobacillus stearothermophilus
3.1.21.4 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 Lysinibacillus sphaericus
3.1.21.4 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 Pseudomonas putida
3.1.21.4 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 Neisseria meningitidis
3.1.21.4 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 Weizmannia coagulans
3.1.21.4 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 Bacillus pumilus
3.1.21.4 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 Citrobacter sp.
3.1.21.4 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 Haemophilus aegyptius
3.1.21.4 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 Acinetobacter lwoffii
3.1.21.4 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 Campylobacter jejuni
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Geobacillus stearothermophilus
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Lysinibacillus sphaericus
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Pseudomonas putida
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Neisseria meningitidis
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Weizmannia coagulans
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Bacillus pumilus
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Citrobacter sp.
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Haemophilus aegyptius
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Acinetobacter lwoffii
3.1.21.4 additional information reaction mode of type IIB enzyme in one or two polypeptide systems, overview Campylobacter jejuni
3.1.21.4 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 Geobacillus stearothermophilus
3.1.21.4 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 Lysinibacillus sphaericus
3.1.21.4 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 Pseudomonas putida
3.1.21.4 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 Neisseria meningitidis
3.1.21.4 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 Weizmannia coagulans
3.1.21.4 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 Bacillus pumilus
3.1.21.4 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 Citrobacter sp.
3.1.21.4 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 Haemophilus aegyptius
3.1.21.4 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 Acinetobacter lwoffii
3.1.21.4 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 Campylobacter jejuni