Application | Comment | Organism |
---|---|---|
agriculture | the recombinant thermostable chimeric endolysin can potentially be utilized as a feed additive to control the bacterium Clostridium perfringens during poultry production | Clostridium phage phiCP26F |
agriculture | the recombinant thermostable chimeric endolysin can potentially be utilized as a feed additive to control the bacterium Clostridium perfringens during poultry production | Geobacillus virus E2 |
drug development | a thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability, overview | Clostridium phage phiCP26F |
drug development | a thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability, overview | Geobacillus virus E2 |
Cloned (Comment) | Organism |
---|---|
synthesis of a gene, codon optimized for Escherichia coli expression, that encodes the catalytic domain of the bacteriophage phiGVE2 amidase and the cell-wall binding (CWB) domain of the endolysin encoded by the genome of phiCP26F, recombinant expression of His-tagged chimeric enzyme PlyGVE2CpCWB in Escherichia coli strain BL21(DE3) | Clostridium phage phiCP26F |
synthesis of a gene, codon optimized for Escherichia coli expression, that encodes the catalytic domain of the bacteriophage phiGVE2 amidase and the cell-wall binding (CWB) domain of the endolysin encoded by the genome of phiCP26F, recombinant expression of His-tagged chimeric enzyme PlyGVE2CpCWB in Escherichia coli strain BL21(DE3) | Geobacillus virus E2 |
Protein Variants | Comment | Organism |
---|---|---|
additional information | a codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) of Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F which is identical to the PlyCP39O endolysin CWB domain. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures | Clostridium phage phiCP39-O |
additional information | a thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability, overview. A codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) from Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F which is identical to the PlyCP39O endolysin CWB domain from Clostridium phage phiCP39-O. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures | Clostridium phage phiCP26F |
additional information | a thermophilic phage endolysin fusion to a Clostridium perfringens-specific cell wall binding domain creates an anti-Clostridium antimicrobial with improved thermostability, overview. A codon optimized gene for the PlyGVE2 predicted N-acetylmuramoyl-L-alanine amidase endolysin domain (179 amino acids) from Geobacillus virus E2 page phiGVE2 is synthesized in-frame with the CWB domain (53 amino acids) of PlyCP26F from Clostridium perfringens-specific bacteriophage phiCP26F. The resulting protein, PlyGVE2CpCWB, lyses Clostridium perfringens in liquid and solid cultures | Geobacillus virus E2 |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
NaCl | the recombinant chimeric enzyme PlyGVE2CpCWB shows full activity at 10 mM NaCl, 40% activity at 150 mM NaCl, and 16% active at 600 mM NaCl, pH 8.0 | Clostridium phage phiCP26F | |
NaCl | the recombinant chimeric enzyme PlyGVE2CpCWB shows full activity at 10 mM NaCl, 40% activity at 150 mM NaCl, and 16% active at 600 mM NaCl, pH 8.0 | Geobacillus virus E2 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Clostridium phage phiCP26F | F2VHX9 | - |
- |
Clostridium phage phiCP39-O | B6CXF7 | - |
- |
Geobacillus virus E2 | A6M970 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged chimeric enzyme PlyGVE2CpCWB from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Clostridium phage phiCP26F |
recombinant His-tagged chimeric enzyme PlyGVE2CpCWB from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Geobacillus virus E2 |
Subunits | Comment | Organism |
---|---|---|
? | x * 27261, chimeric enzyme PlyGVE2CpCWB, sequence calculation, x * 27300, His-tagged chimeric enzyme PlyGVE2CpCWB, SDS-PAGE | Clostridium phage phiCP26F |
? | x * 27261, chimeric enzyme PlyGVE2CpCWB, sequence calculation, x * 27300, His-tagged chimeric enzyme PlyGVE2CpCWB, SDS-PAGE | Geobacillus virus E2 |
Synonyms | Comment | Organism |
---|---|---|
amidase-hydrolase | UniProt | Clostridium phage phiCP39-O |
bacteriophage phiGVE2 amidase | - |
Geobacillus virus E2 |
endolysin | - |
Clostridium phage phiCP39-O |
endolysin | - |
Clostridium phage phiCP26F |
endolysin | - |
Geobacillus virus E2 |
phage endolysin | - |
Clostridium phage phiCP39-O |
phage endolysin | - |
Clostridium phage phiCP26F |
phi26F_gp22 | - |
Clostridium phage phiCP26F |
phiCP26F endolysin | - |
Clostridium phage phiCP26F |
phiGVE2 endolysin | - |
Geobacillus virus E2 |
PlyCP26F | - |
Clostridium phage phiCP26F |
PlyCP39O | - |
Clostridium phage phiCP39-O |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | 37 | assay at | Clostridium phage phiCP26F |
22 | 37 | assay at, chimeric enzyme PlyGVE2CpCWB | Geobacillus virus E2 |
60 | - |
wild-type N-acetylmuramoyl-L-alanine amidase | Geobacillus virus E2 |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
40 | 80 | activity range, wild-type N-acetylmuramoyl-L-alanine amidase | Geobacillus virus E2 |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
PlyGVE2CpCWB is more tolerant to heat treatment than PlyCP26F | Clostridium phage phiCP26F |
4 | 42 | recombinant chimeric endolysin PlyGVE2CpCWB is completely stable for at least 30 min | Geobacillus virus E2 |
4 | 22 | PlyCP26F and PlyGVE2CpCWB are completely stable for at least 30 min | Clostridium phage phiCP26F |
37 | - |
PlyCP26F loses roughly 10% of its activity after 30 min at 37°C, while PlyGVE2CpCWB is fully active | Clostridium phage phiCP26F |
42 | - |
PlyCP26F loses roughly 40% of its activity after 30 min at 42°C, while PlyGVE2CpCWB is fully active | Clostridium phage phiCP26F |
50 | - |
recombinant chimeric endolysin PlyGVE2CpCWB, over 95% activity remaining after 30 min | Geobacillus virus E2 |
50 | - |
recombinant chimeric endolysin PlyGVE2CpCWB, over 95% activity remaining after 30 min, PlyCP26F loses over 95% activity | Clostridium phage phiCP26F |
55 | - |
recombinant chimeric endolysin PlyGVE2CpCWB, 57% activity remaining after 30 min | Geobacillus virus E2 |
55 | - |
recombinant chimeric endolysin PlyGVE2CpCWB, 57% activity remaining after 30 min, PlyCP26F loses over 95% activity | Clostridium phage phiCP26F |
65 | - |
recombinant chimeric endolysin PlyGVE2CpCWB, 10% activity remaining after 30 min, inactivation of PlyCP26F | Clostridium phage phiCP26F |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
recombinant isolated catalytic domain of PlyGVE2CpCWB | Clostridium phage phiCP26F |
6 | - |
recombinant isolated catalytic domain of PlyGVE2CpCWB | Geobacillus virus E2 |
8 | - |
recombinant chimeric enzyme PlyGVE2CpCWB | Clostridium phage phiCP26F |
8 | - |
recombinant chimeric enzyme PlyGVE2CpCWB | Geobacillus virus E2 |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 10 | activity range, recombinant chimeric enzyme PlyGVE2CpCWB | Clostridium phage phiCP26F |
4 | 10 | activity range, recombinant chimeric enzyme PlyGVE2CpCWB | Geobacillus virus E2 |
General Information | Comment | Organism |
---|---|---|
physiological function | PlyGVE2CpCWB chimeric mutant effectiveness in lysis against various bacteria, overview | Geobacillus virus E2 |
physiological function | the two N-acetylmuramoyl-L-alanine amidases from two bacteriophages, PhiCP26F and PhiCP39O, are identical in the C-terminal cell-wall binding domain, but have only 55% identity to each other in the N-terminal catalytic domain. Both endolysins, PlyCP26F and PlyCP39O, lyse their parental phage host strains of Clostridium perfringens as well as other strains of the bacterium when exposed externally, but do not lyse bacteria beyond the species | Clostridium phage phiCP39-O |
physiological function | the two N-acetylmuramoyl-L-alanine amidases from two bacteriophages, PhiCP26F and PhiCP39O, are identical in the C-terminal cell-wall binding domain, but have only 55% identity to each other in the N-terminal catalytic domain. Both endolysins, PlyCP26F and PlyCP39O, lyse their parental phage host strains of Clostridium perfringens as well as other strains of the bacterium when exposed externally, but do not lyse bacteria beyond the species. PlyGVE2CpCWB chimeric mutant effectiveness in lysis against various bacteria, overview | Clostridium phage phiCP26F |