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PMID:22416675

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Citation

Son, B, Yun, J, Lim, JA, Shin, H, Heu, S and Ryu, S (2012) Characterization of LysB4, an endolysin from the Bacillus cereus-infecting bacteriophage B4. BMC Microbiol. 12:33

Abstract

Bacillus cereus is a foodborne pathogen that causes emetic or diarrheal types of food poisoning. The incidence of B. cereus food poisoning has been gradually increasing over the past few years, therefore, biocontrol agents effective against B. cereus need to be developed. Endolysins are phage-encoded bacterial peptidoglycan hydrolases and have received considerable attention as promising antibacterial agents.

Links

PubMed PMC3315420 Online version:10.1186/1471-2180-12-33

Keywords

Amino Acid Sequence; Bacillus Phages/enzymology; Bacillus Phages/genetics; Bacillus cereus/virology; Catalytic Domain; Cations, Divalent/metabolism; Coenzymes/metabolism; Computational Biology/methods; DNA, Viral/chemistry; DNA, Viral/genetics; Endopeptidases/chemistry; Endopeptidases/genetics; Endopeptidases/metabolism; Enzyme Stability; Hydrogen-Ion Concentration; Molecular Sequence Data; N-Acetylmuramoyl-L-alanine Amidase/chemistry; N-Acetylmuramoyl-L-alanine Amidase/genetics; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Peptidoglycan/metabolism; Protein Structure, Tertiary; Sequence Analysis, DNA; Sequence Homology; Substrate Specificity; Temperature; Zinc/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

9CAUD:H9NAL3

GO:0004175: endopeptidase activity

ECO:0000314:

F

Figure 4, data not shown.

complete
CACAO 11491

9CAUD:H9NAL3

GO:0061786: peptidoglycan cross-bridge peptide endopeptidase activity

ECO:0000314:

F

Figure 4 A and B. The specific LysB4 cleavage site in the peptidoglycan was determined by reverse-phase (RP)-HPLC and LC-MS.

complete
CACAO 12122

Notes

See also

References

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