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PMID:21682850
| Citation |
Rodríguez, L, Martínez, B, Zhou, Y, Rodríguez, A, Donovan, DM and García, P (2011) Lytic activity of the virion-associated peptidoglycan hydrolase HydH5 of Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88. BMC Microbiol. 11:138 |
|---|---|
| Abstract |
Staphylococcus aureus is a food-borne pathogen and the most common cause of infections in hospitalized patients. The increase in the resistance of this pathogen to antibacterials has made necessary the development of new anti-staphylococcal agents. In this context, bacteriophage lytic enzymes such as endolysins and structural peptidoglycan (PG) hydrolases have received considerable attention as possible antimicrobials against gram-positive bacteria. |
| Links |
PubMed PMC3150257 Online version:10.1186/1471-2180-11-138 |
| Keywords |
Bacteriolysis; Cloning, Molecular; DNA Mutational Analysis; Escherichia coli/genetics; Gene Expression; Microbial Viability/drug effects; Models, Molecular; N-Acetylmuramoyl-L-alanine Amidase/genetics; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Phylogeny; Protein Structure, Tertiary; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Deletion; Sequence Homology; Staphylococcus Phages/enzymology; Staphylococcus Phages/genetics; Staphylococcus aureus/drug effects; Staphylococcus aureus/virology; Temperature; Virion/enzymology; Virion/genetics |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0009253: peptidoglycan catabolic process |
ECO:0005801: enzymatic activity assay evidence used in manual assertion |
P |
other:involved_in |
Zymogram in Figure 2 |
complete | |||
See also
References
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