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Literature summary for 3.5.1.28 extracted from

  • Oliveira, A.; Leite, M.; Kluskens, L.D.; Santos, S.B.; Melo, L.D.; Azeredo, J.
    The first Paenibacillus larvae bacteriophage endolysin (PlyPl23) with high potential to control american foulbrood (2015), PLoS ONE, 10, e0132095 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene IBBPl23_21, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged in Escherichia coli strains JM109 and BL21(DE3) Paenibacillus phage phiIBB_P123

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information no signal peptide is identified Paenibacillus phage phiIBB_P123
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-

Organism

Organism UniProt Comment Textmining
Paenibacillus phage phiIBB_P123 R9VY83 i.e. Paenibacillus larvae phage phiIBB_Pl23 or Paenibacillus larvae bacteriophage
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Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged from Escherichia coli strains JM109 and BL21(DE3) by nickel affinity chromatography and ultrafiltration Paenibacillus phage phiIBB_P123

Source Tissue

Source Tissue Comment Organism Textmining
additional information the Paenibacillus larvae strain Pl02-23 is used as the host for phiIBB_Pl23 amplification Paenibacillus phage phiIBB_P123
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Subunits

Subunits Comment Organism
? x * 25800, about, sequence calculation, x * 25000, SDS-PAGE Paenibacillus phage phiIBB_P123

Synonyms

Synonyms Comment Organism
endolysin
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Paenibacillus phage phiIBB_P123
PlyPl23
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Paenibacillus phage phiIBB_P123

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Paenibacillus phage phiIBB_P123

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Paenibacillus phage phiIBB_P123

pH Range

pH Minimum pH Maximum Comment Organism
5 9 over 70% of maximal activity Paenibacillus phage phiIBB_P123

pI Value

Organism Comment pI Value Maximum pI Value
Paenibacillus phage phiIBB_P123 sequence calculation
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6.08

General Information

General Information Comment Organism
evolution the enzyme's the C-terminus does not display homology to any identifiable domain Paenibacillus phage phiIBB_P123
additional information the enzyme has an N-acetylmuramoyl-L-alanine amidase catalytic domain and exhibits a broad-spectrum activity against common Paenibacillus larvae genotypes. Identification of five putative amidase catalytic residues: His29, His129, Phe53, Lys135, and Cys137 Paenibacillus phage phiIBB_P123
physiological function phage phiIBB_Pl23 is able to lyse 16 of the 20 strains (80%), its endolysin is active against all Paenibacillus larvae strains tested, but Bacillus and Lactobacillus strains are not lysed by the phage or by the enzyme, overview Paenibacillus phage phiIBB_P123