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Information on EC 3.4.24.75 - lysostaphin and Organism(s) Staphylococcus simulans and UniProt Accession P10547
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- 3.4.24.75
-
staphylococci
-
methicillin-resistant
- vancomycin
- simulans
-
bactericidal
- pentaglycine
-
bacteriolytic
- methicillin
- epidermidis
- mastitis
-
antistaphylococcal
-
cross-bridge
-
bacteriocins
- staphylolyticus
- medicine
- autolysins
- oxacillin
- endolysins
-
interpeptide
-
teichoic
-
biovar
-
intramammary
-
coagulase-negative
-
muropeptide
- teicoplanin
-
methicillin-sensitive
-
cowan
-
micrococci
- murein
- haemolyticus
- coagulase
-
daptomycin
-
mutanolysine
- diagnostics
- pharmacology
- food industry
- analysis
The taxonomic range for the selected organisms is: Staphylococcus simulans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of the -Gly-/-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans
Synonyms
lysostaphin, ale-1, glycylglycine endopeptidase, r-lysostaphin, peptidoglycan endopeptidase, glycyl-glycine endopeptidase, sa0205, lysostaphin endopeptidase, staphylococcus aureus-specific cell wall endopeptidase lysostaphin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALE-1
-
-
-
-
Glycyl-glycine endopeptidase
-
-
-
-
Glycylglycine endopeptidase
lysostaphin
Lysostaphin endopeptidase
-
-
-
-
r-lysostaphin
Staphylococcus aureus-specific cell wall endopeptidase lysostaphin
-
-
additional information
-
lysostaphin-type enzymes belong to so-called LAS, i.e. Lysostaphin, D-Ala-D-Ala carboxypeptidase, Sonic hedgehog enzyme, enzymes
Glycylglycine endopeptidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of the -Gly-/-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans
a two-stage reaction controlled by two ionogenic groups of the active site, the active site of lysostaphin contains glutamic acid and lysine
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9011-93-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methicillin-resistant Staphylococcus aureus cell wall + H2O
?
-
-
-
?
Staphylococcus aureus cells + H2O
fragments of elastin
Staphylococcus aureus ATCC 29213
-
-
?
Staphylococcus aureus mutant strain femAB cell wall + H2O
?
-
-
-
?
L-lysine(N-e-pentaglycine-N-(2-aminobenzoyl))-[N-(2,4-dinitrophenyl)ethylenediamine]
?
-
-
-
-
?
L-lysine(N-epsilon-pentaglycine-N-(2-aminobenzoyl))-[N-(2,4-dinitrophenyl)ethylenediamine] + H2O
?
-
-
-
-
?
methicillin-resistant Staphylococcus aureus cell wall + H2O
?
-
-
-
-
?
MV11 + H2O
?
-
developing a fluorescence resonance energy transfer substrate based on MV11
-
-
?
N-(2-aminobenzoyl)pentaglycine-[N-(2,4-dinitrophenyl)ethylenediamine] + H2O
?
-
-
-
-
?
peptidoglycan + H2O
fragments of peptidogylcan
-
peptidoglycans from cell walls of Staphylococcus aureus and Staphylococcus haemolyticus
-
-
?
peptidoglycan + H2O
?
the enzyme cleaves pentaglycine crossbridges of Staphylococcus aureus peptidoglycan
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
-
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
cleaves Gly-Gly bonds in peptidoglycans
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
the enzyme is highly specific and effective against Staphylococcus aureus cleaving the pentaglycine cross-bridges in the peptidoglycan layer of staphylococcal cell walls
-
-
?
Staphylococcus aureus cell wall + H2O
?
the enzyme shows selectivity toward pentaglycine bridges in Staphylococcus aureus cell wall
-
-
?
methicillin-resistant Staphylococcus aureus cells + H2O
?
-
the enzyme causes rapid lysis of Staphylococcus aureus cells
-
-
?
peptidoglycan + H2O
?
-
the hydrolytic effect on staphylococcal peptidoglycan can be potentiated by simultaneous action of lysostaphin and lysozyme
-
-
?
peptidoglycan + H2O
?
-
The enzymes attack cell walls of staphylococcus species that do not poduce lysostaphin, species which produce lysostaphin are not attacked. Mutants of Staphylococcus simulans lacking lysostaphin are also attacked
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
-
-
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
-
92 amino acids of the C-terminus of lysostaphin are necessary and sufficiant for targeting the substrate
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
-
hydrolyis of pentaglycine interpeptide bridges of Staphylococcal peptidoglycan
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
-
activities of three enzymes namely, glycylglycine endopeptidase, endo-beta-N-acetyl glucosamidase and N-acteyl muramyl-L-alanine amidase. Lysostaphin rapidly lyses actively growing and non-dividing cells including staphylococci in biofilms. Glycylglycine endopeptidase lyses staphylococcal cells by hydrolyzing glycylglycine bonds in the polyglycine bridges which form cross links between glycopeptide chains in the cell wall peptidoglycan of Staphylococcus aureus cells. Lytic principle of lysostaphin is a peptidase which liberates N-terminal glycine and alanine from Staphylococcus aureus cell wall. Hexosaminidase is present in lysostaphin preparation is specific for the gluocainyl-muramic acid bond of the bacterial carbohydrate backbone
-
-
?
Staphylococcus aureus cell wall + H2O
?
-
Staphylococcus aureus ATCC 6538 or ATCC 33807 cells
-
-
?
additional information
?
-
lysostaphin exhibits a high degree of antistaphylococcal bacteriolytic activity, being inactive against bacteria of all other genera. The cell-wall degrading activity of lysostaphin is primarily due to a glycylglycine endopeptidase activity. Staphylococcus simulans biovar staphylolyticus peptidoglycan is resistant to the hydrolytic activity of lysostaphin, since the cells produce a resistance factor that causes the incorporation of Ser residues into the third and fifth positions of the cell wall cross bridges
-
-
?
additional information
?
-
resistance to lysostaphin is due to a FemABX-like immunity protein that inserts serines in place of some glycines in peptidoglycan cross bridges
-
-
?
additional information
?
-
lysostaphin exhibits strong lytic activity against Staphylococcus aureus mastitis isolates
-
-
?
additional information
?
-
the enzyme hydrolyzes the glycylglycine bonds of polyglycine interpeptide bridges on the cell walls of Staphylococcus aureus, Staphylococcus epidermidis and Staphylococcus carnosus
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the glycylglycine bonds of polyglycine interpeptide bridges on the cell walls of Staphylococcus aureus, Staphylococcus epidermidis and Staphylococcus carnosus
-
-
?
additional information
?
-
-
a traP mutant strain is more resistant to lysostaphin than wild-type Staphylococcus aureus, the extracellular C-terminus of TRAP can act as the specific targeting protein of the lysozyme/lysostaphin on the Staphylococcus aureus cell wall and the biological significance of the interaction might be to facilitate lysozyme/lysostaphin-mediated cell lysis, TRAP is necessary for the binding and activity of lysostaphin in vitro, overview
-
-
?
additional information
?
-
-
lysostaphin is a glycylglycine endopeptidase cleaving the pentaglycine cross-bridge structure unique to the staphylococcal cell wall and is considered to be a potential drug for Staphylococcus aureus, in vitro activity of recombinant lysostaphin against Staphylococcus aureus isolates from hospitals in Beijing, China, with MIC values of 30-2000 ng/ml, agar dilution assay, overview
-
-
?
additional information
?
-
-
lysostaphin is active in treatment of neonatal Staphylococcus aureus infection by a clinical methicillin-sensitive Staphylococcus aureus serotype 5 strain, overview
-
-
?
additional information
?
-
-
potent, synergistic inhibition of Staphylococcus aureus strains MSSA476 and MRSA252 upon exposure to a combination of the endopeptidase lysostaphin and the cationic peptide ranalexin, which is most potent, as well as with the antimicrobial peptides magainin 2 and dermaseptin s3(1-16), overview
-
-
?
additional information
?
-
-
Staphylococcus simulans secretes lysostaphin, a bacteriolytic enzyme that specifically binds to the cell wall envelope of Staphylococcus aureus and cleaves the pentaglycine cross bridges of peptidoglycan, thereby killing staphylococci, screening of a collection of Staphylococcus aureus strain Newman transposon mutants for lysostaphin resistance, transposon insertion in SAV2335 is herein named lyrA, i.e. lysostaphin resistance A, activity against diverse Staphylococcus aureus strains with MIC-values of 0.0005-0.002 mg/ml, overview
-
-
?
additional information
?
-
-
the endopeptidase rapidly lyses Staphylococcus aureus through proteolysis of the staphylococcal cell wall which allows its use as a therapeutic agent, the enzyme acts synergistically with oxacillin and with vancomycin, in vivo antimicrobial activity in different mouse tissues, overview
-
-
?
additional information
?
-
-
the enzyme is active against clinical methiciliin-resistant Staphylococcus aureus with a MIC50 value of 0.125 mg/l, it breaks down the cell wall of Staphylococcus aureus, overview
-
-
?
additional information
?
-
-
pentaglycine bridges in peptidoglycan of Staphylococci as a substrate
-
-
?
additional information
?
-
-
the enzyme is a glycylglycine endopeptidase
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methicillin-resistant Staphylococcus aureus cell wall + H2O
?
-
-
-
?
Staphylococcus aureus cells + H2O
fragments of elastin
Staphylococcus aureus ATCC 29213
-
-
?
methicillin-resistant Staphylococcus aureus cell wall + H2O
?
-
-
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
-
activities of three enzymes namely, glycylglycine endopeptidase, endo-beta-N-acetyl glucosamidase and N-acteyl muramyl-L-alanine amidase. Lysostaphin rapidly lyses actively growing and non-dividing cells including staphylococci in biofilms. Glycylglycine endopeptidase lyses staphylococcal cells by hydrolyzing glycylglycine bonds in the polyglycine bridges which form cross links between glycopeptide chains in the cell wall peptidoglycan of Staphylococcus aureus cells. Lytic principle of lysostaphin is a peptidase which liberates N-terminal glycine and alanine from Staphylococcus aureus cell wall. Hexosaminidase is present in lysostaphin preparation is specific for the gluocainyl-muramic acid bond of the bacterial carbohydrate backbone
-
-
?
peptidoglycan + H2O
fragments of peptidogylcan
-
peptidoglycans from cell walls of Staphylococcus aureus and Staphylococcus haemolyticus
-
-
?
Staphylococcus aureus cell wall + H2O
?
-
Staphylococcus aureus ATCC 6538 or ATCC 33807 cells
-
-
?
peptidoglycan + H2O
?
the enzyme cleaves pentaglycine crossbridges of Staphylococcus aureus peptidoglycan
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
cleaves Gly-Gly bonds in peptidoglycans
-
-
?
Peptidoglycan + H2O
Fragments of peptidoglycan
the enzyme is highly specific and effective against Staphylococcus aureus cleaving the pentaglycine cross-bridges in the peptidoglycan layer of staphylococcal cell walls
-
-
?
Staphylococcus aureus cell wall + H2O
?
the enzyme shows selectivity toward pentaglycine bridges in Staphylococcus aureus cell wall
-
-
?
peptidoglycan + H2O
?
-
the hydrolytic effect on staphylococcal peptidoglycan can be potentiated by simultaneous action of lysostaphin and lysozyme
-
-
?
peptidoglycan + H2O
?
-
The enzymes attack cell walls of staphylococcus species that do not poduce lysostaphin, species which produce lysostaphin are not attacked. Mutants of Staphylococcus simulans lacking lysostaphin are also attacked
-
-
?
additional information
?
-
lysostaphin exhibits a high degree of antistaphylococcal bacteriolytic activity, being inactive against bacteria of all other genera. The cell-wall degrading activity of lysostaphin is primarily due to a glycylglycine endopeptidase activity. Staphylococcus simulans biovar staphylolyticus peptidoglycan is resistant to the hydrolytic activity of lysostaphin, since the cells produce a resistance factor that causes the incorporation of Ser residues into the third and fifth positions of the cell wall cross bridges
-
-
?
additional information
?
-
resistance to lysostaphin is due to a FemABX-like immunity protein that inserts serines in place of some glycines in peptidoglycan cross bridges
-
-
?
additional information
?
-
the enzyme hydrolyzes the glycylglycine bonds of polyglycine interpeptide bridges on the cell walls of Staphylococcus aureus, Staphylococcus epidermidis and Staphylococcus carnosus
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the glycylglycine bonds of polyglycine interpeptide bridges on the cell walls of Staphylococcus aureus, Staphylococcus epidermidis and Staphylococcus carnosus
-
-
?
additional information
?
-
-
a traP mutant strain is more resistant to lysostaphin than wild-type Staphylococcus aureus, the extracellular C-terminus of TRAP can act as the specific targeting protein of the lysozyme/lysostaphin on the Staphylococcus aureus cell wall and the biological significance of the interaction might be to facilitate lysozyme/lysostaphin-mediated cell lysis, TRAP is necessary for the binding and activity of lysostaphin in vitro, overview
-
-
?
additional information
?
-
-
lysostaphin is a glycylglycine endopeptidase cleaving the pentaglycine cross-bridge structure unique to the staphylococcal cell wall and is considered to be a potential drug for Staphylococcus aureus, in vitro activity of recombinant lysostaphin against Staphylococcus aureus isolates from hospitals in Beijing, China, with MIC values of 30-2000 ng/ml, agar dilution assay, overview
-
-
?
additional information
?
-
-
lysostaphin is active in treatment of neonatal Staphylococcus aureus infection by a clinical methicillin-sensitive Staphylococcus aureus serotype 5 strain, overview
-
-
?
additional information
?
-
-
potent, synergistic inhibition of Staphylococcus aureus strains MSSA476 and MRSA252 upon exposure to a combination of the endopeptidase lysostaphin and the cationic peptide ranalexin, which is most potent, as well as with the antimicrobial peptides magainin 2 and dermaseptin s3(1-16), overview
-
-
?
additional information
?
-
-
Staphylococcus simulans secretes lysostaphin, a bacteriolytic enzyme that specifically binds to the cell wall envelope of Staphylococcus aureus and cleaves the pentaglycine cross bridges of peptidoglycan, thereby killing staphylococci, screening of a collection of Staphylococcus aureus strain Newman transposon mutants for lysostaphin resistance, transposon insertion in SAV2335 is herein named lyrA, i.e. lysostaphin resistance A, activity against diverse Staphylococcus aureus strains with MIC-values of 0.0005-0.002 mg/ml, overview
-
-
?
additional information
?
-
-
the endopeptidase rapidly lyses Staphylococcus aureus through proteolysis of the staphylococcal cell wall which allows its use as a therapeutic agent, the enzyme acts synergistically with oxacillin and with vancomycin, in vivo antimicrobial activity in different mouse tissues, overview
-
-
?
additional information
?
-
-
the enzyme is active against clinical methiciliin-resistant Staphylococcus aureus with a MIC50 value of 0.125 mg/l, it breaks down the cell wall of Staphylococcus aureus, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Co2+
10 mM, 30% decrease of activity of enzyme produced with pET vector system and 20% decrease of activity of enzyme produced with pBAD vector system
Ni2+
2 mM, 60% decrease of activity of enzyme produced with pET vector system and 20% decrease of activity of enzyme produced with pBAD vector system
ethanolamine
-
inhibits enzyme binding to the cell surface, leading to low enzyme activity, despite retention of its secondary structure. At pH 10.5 (but not at pH 7.5), methanolamine strongly deactivates the enzyme in a concentration-dependent manner
Zn2+
partial inhibition of enzyme activity is observed in the excess of zinc
additional information
no inhibitory effect of EDTA and 2 mM Co2+
-
additional information
-
no inhibitory effect of EDTA and 2 mM Co2+
-
additional information
the bacteriolytic activity of the enzyme is reduced to about 60% in the presence of 150 mM NaCl which causes contractions of bacterial peptidoglycan substrate
-
additional information
-
the bacteriolytic activity of the enzyme is reduced to about 60% in the presence of 150 mM NaCl which causes contractions of bacterial peptidoglycan substrate
-
additional information
-
not inhibitory is trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, i.e. E-64
-
additional information
-
binding of elastin to lysostaphin is not affected by exogenously added zinc, suggesting that zinc interferes directly with the catalytic activity of the enzyme
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
C-terminus of TRAP
-
i.e. target of RNAIII activating protein, a membrane-associated protein in Staphylococcus sp., can enhance the activity of lysozyme and lysostaphin, interaction analysis, overview
-
additional information
-
the enzyme acts synergistically with oxacillin and with vancomycin in lysis of the cell wall of pathogenic Staphylococcus aureus
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
L-lysine(N-e-pentaglycine-N-(2-aminobenzoyl))-[N-(2,4-dinitrophenyl)ethylenediamine]
-
value from Grafit and Hanes plot analyses
0.07
L-lysine(N-e-pentaglycyl-DABCYL)-EDANS
-
value from Hanes plot analysis
0.08
L-lysine(N-e-pentaglycyl-DABCYL)-EDANS
-
value from Grafit plot analysis
0.2
N-(2-Aminobenzoyl)pentaglycine-[N-(2,4-dinitrophenyl)ethylenediamine]
-
value from Grafit plot analysis
0.3
N-(2-Aminobenzoyl)pentaglycine-[N-(2,4-dinitrophenyl)ethylenediamine]
-
value from Hanes plot analysis
additional information
additional information
-
kinetics and thermodynamics
-
additional information
additional information
-
kinetics of lysostaphin clearance of Staphylococcus aureus infection, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
169 U/mg (prolysostaphin), 760 U/mg (mature lysostaphin), 1 unit is defined as the amount of enzyme that causes 50% reduction of turbidity in 10 min at 37 C of an inactivated Staphylococcus carnosus TM300 cell suspension
additional information
-
assay method with N-acetylhexaglycine as substrate
additional information
-
11900 units per mg, after 12 fold purification, 1 unit is defined as the amount of enzyme required to decrease the OD(A600) of a suspension of Staphylococcus aureus 237 cells by 0.001 at 37°C in 5 min in a 3 ml reaction volume
additional information
-
depending on the purification step the specific activity varied between 300 U/mg and 1500 U/mg
additional information
-
in vitro activity of recombinant lysostaphin against Staphylococcus aureus isolates from hospitals in Beijing, China, with MIC values of 30-2000 ng/ml, overview
additional information
-
activities of three enzymes namely, glycylglycine endopeptidase, endo-beta-N-acetyl glucosamidase and N-acteyl muramyl-L-alanine amidase. Lysostaphin rapidly lyses actively growing and non-dividing cells including staphylococci in biofilms. Glycylglycine endopeptidase lyses staphylococcal cells by hydrolyzing glycylglycine bonds in the polyglycine bridges which form cross links between glycopeptide chains in the cell wall peptidoglycan of Staphylococcus aureus cells. Lytic principle of lysostaphin is a peptidase which liberates N-terminal glycine and alanine from Staphylococcus aureus cell wall. Hexosaminidase is present in lysostaphin preparation is specific for the gluocainyl-muramic acid bond of the bacterial carbohydrate backbone
additional information
-
FVB albino dams infected with methicillin-resistant Staphylococcus aureus for analysis of lysostaphin impact on pharmacokinetics, minimum inhibitory concentration(0.008 microg/ml) and minimum bactericidal concentration (0.015 microg/ml)
additional information
-
lysostaphin inhibits growth of methicillin-resistant Staphylococcus aureus USA300 at a concentration of 0.096 mg/ml. Growth inhibition of the two enzymes lysostaphin and LysK in combination is greater than either enzyme alone
additional information
-
treatment of methicillin-susceptible Staphylococcus aureus strain ATCC 25923 with lysostaphin results in major structural changes in the form of cell swelling, splitting of the septum, creation of nanoscale perforations, decrease of the bacterial spring constant and cell wall stiffness (atomic force microscopy)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
additional information
-
the pH value near a negatively charged cell is supposed to be strongly shifted to acidity as compared to the pH of the solution volume. This shifts the enzyme pH dependence curve in solution to alkalinity, overview
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
lysostaphin is marginally effective at pH 6.0 (50 mM phosphate buffer), but becomes much more active at pH 7.0. A further pH increase to the range between 7.0 and 9.0 (50 mM Tris-HCl) has little effect on the activity of lysostaphin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in mouse mammary glands
physiological function
additional information
physiological function
-
the enzyme eradicates meticillin-resistant Staphylococcus aureus biofilm
physiological function
-
lysostaphin is an anti-staphylococcal enzyme resulting in bacterial lysis and biofilm reduction
physiological function
-
the enzyme lyses staphylococcus cell walls by cleaving pentaglycine cross_bridges in their peptidoglycan
additional information
-
lysostaphin clears Staphylococcus aureus biofilms in vitro and also eradicates established Staphylococcus aureus biofilms on implanted jugular vein catheters in mice, overview
additional information
-
lysostaphin is effective, in combination with antibiotic ranalexin, against methicillin-resistant Staphylococcus aureus infections in human MRSA252 cell culture for hemolysis assay, the female ICR CD-1 mouse model for systemic infection, and a rabbit model for wound infection using New Zealand White rabbits, overview. Ranalexin alone causes hemolysis and shows signs of toxicity to Vero cells at over 50 mg/L, but lysostaphin alone causes no hemolysis and has no effect on Vero cell viability
additional information
-
lysostaphin is effective, in combination with antibiotic ranalexin, against methicillin-resistant Staphylococcus aureus infections. The combination is significantly more effective than treatment with ranalexin or lysostaphin alone
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
26900
-
calculated from the plot of mobility versus log molecular weight of standards
27000
49120
-
prolysostaphin, calculation from nucleotide sequence. Prolysostaphin is processed to the mature enzyme by an extracellular cysteine protease
64000 - 68000
64000 - 68000
-
the overestimated value is due to a high glutamate content. Prolysostaphin is processed to the mature enzyme by an extracellular cysteine protease
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 64000-68000, prolysostaphin, the overestimated value is due to a high glutamate content
?
x * 45000, lysostaphin fused it with an anti-parallel alpha-helical dimerization domain, SDS-PAGE
?
x * 53000, His6-tagged recombinant preproenzyme, calculated from amino acid sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
Asn125 is the exact glycosylation site of lysostaphin expressed in CMEC-08-D cells. N-glycosylation at Asn125 of lysostaphin decreases lysostaphin bacteriolytic activity but does not affect its binding ability to Staphylococcus aureus
proteolytic modification
proteolytic modification
-
the preprolysostaphin is proteolytically processed to the mature enzyme
proteolytic modification
-
lysostaphin is secreted as a proenzyme. Proteolytic cleavage of 13 N-terminal tandem repeats generates mature lysostaphin with 2 functionally separable domains
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
lysostaphin SH3b domain in complex with a pentaglycine peptide, hanging drop vapor diffusion method
sitting drop vapor diffusion method, using 0.1 M MES/NaOH pH 6.5 and 1.6 M magnesium sulfate, 2 mM tetraglycine phosphinic acid, or 0.1 M Tris (base), bicine pH 8.5, 0.1 M amino acids [L-Na-glutamate, L-alanine (racemic), glycine, L-lysine (racemic), L-serine (racemic)], 30% (v/v) PEG 8000, or 0.05 M potassium dihydrogen phosphate and 20% (w/v) PEG 8000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D339C
the mutant shows about 37% of wild type bacteriolytic activity
K332C
the mutant shows about 82% of wild type bacteriolytic activity
K332C/T464C
the mutant retains around 25% of the bacteriolytic activity of the wild type protein
K336C
the mutant shows about 90% of wild type bacteriolytic activity
L258C
the mutant shows about 35% of wild type bacteriolytic activity
N260C
the mutant shows about 80% of wild type bacteriolytic activity
N405A
the mutation does not affect lytic activity of the mature enzyme
N405A/Y472A
the mutations do not affect lytic activity of the mature enzyme
Q256C
the mutant shows about 85% of wild type bacteriolytic activity
R470C
the mutant shows about 50% of wild type bacteriolytic activity
T464C
the mutant shows about 85% of wild type bacteriolytic activity
Y472A
the mutation does not affect lytic activity of the mature enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
when incubated at temperatures from 25 to 70°C the enzyme is stable up to 50°C, above the activity is rapidly lost
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lysostaphin degrades Staphylococcus aureus cell walls inefficiently in low conductivity buffers (10-50 mS/cm)
lysostaphin fused it with an anti-parallel alpha-helical dimerization domain has a more favorable pharmacokinetic profile with increased terminal half-life compared to monomeric lysostaphin. However, the staphylolytic activity of dimerized lysostaphin is decreased.
lysostaphin is relatively stable when conjugated with polyethylene glycol and it maintains its activity in human serum
relatively unaffected by salt concentrations between 200 and 500 mM, LysK has a higher specific activity than lysostaphin at NaCl concentrations higher than 150 mM (turbidity reduction assay)
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, recombinant enzyme in 100 mM Tris-HCl pH 7.4, 30 and 40 days, the enzyme loses approximately 25% and 40% of its activity, respectively
4°C and 25°C, recombinant enzyme in 100 mM Tris-HCl pH 7.4, 15 days, the enzyme loses approximately half of its activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Capto MMC column chromatography, and Sephadex G-50 gel filtration
glutathione Sepharose 4 column chromatography and Superdex 75 gel filtration
immobilized-Ni2+ affinity column chromatography and Superdex S200 gel filtration
SP Sepharose column chromatography and Toyopearl PPG-600M column chromatography
ammonium sulfate precipitation and Unosphere S column chromatography
-
recombinant His-tagged lysostaphin comprising residues 1 to 154 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplified from pRG5 recombinant plasmid and cloned into Escherichia coli expression pTYB12 vector which allows the overexpression of a target protein as a fusion to a self-cleavabe affinity tag
expressed as mature lysostaphin free from preprolysostaphin and prolysostaphin in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression of His-tagged lysostaphin comprising residues 1 to 154 in Escherichia coli strain BL21(DE3)
-
expression of the functional mature enzyme fused to secretion signals of the Sep protein from Lactobacillus fermentum BR11, to direct the enzyme secretion from recombinant cells, in Lactobacillus fermentum strain BR11, Lactobacillus rhamnosus strain GG, Lactobacillus plantarum ATCC 14917 and Lactococcus lactis strain MG1363, method development and production levels, overview
-
recominant expression of His-tagged lysostaphin by Escherichia coli BL21 (DE3) pEA3
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
a buffer containing proline 0.15 M and glucose 0.2 M causes the best enzyme refolding
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
pharmacology
-
lysostaphin is useful for treatment for systemic Staphylococcus aureus infection in a mouse model
additional information
-
antistaphylococcal agent in clinical laboratories
medicine
lysostaphin can be used in combination with clarithromycin for the eradication of Staphylococcus aureus biofilms with a minimal biofilm eradication concentration reduction of 9 and 6fold dilutions on meticillin-resistant S. aureus and meticillin-susceptible S. aureus, respectively
medicine
lysostaphin has potential for use as an antistaphylococcal agent for treatment of infections caused by antibiotic-resistant strains of Staphylococcus aureus
medicine
lysostaphin is an antistaphylococcal agent. The enzyme is efficacious in the treatment of bovine mastitis caused by staphylococci
medicine
lysostaphin-functionalized cellulose fibers show activity against Staphylococcus aureus in an in vitro skin model (HaCaT keratinocyte) with low toxicity toward keratinocytes, suggesting good biocompatibility for these materials as antimicrobial matrices in wound healing applications
medicine
lysostaphin exerts high levels of activity against antibiotic-resistant strains of Staphylococcus aureus
medicine
lysostaphin is a therapeutic agent for methicillin-resistant Staphylococcus aureus pneumonia
medicine
-
application as effective antibiotic drug against infections with Staphylococcus aureus
medicine
-
therapeutic agent for the treatment of Staphylococcus aureus infections
medicine
-
lysostaphin is useful in treatment of neonatal Staphylococcus aureus infection, overview
medicine
-
potential therapeutic agent against antibiotic-resistant Staphylococcus aureus infections
medicine
-
lysostaphin can be used potentially as a topical disinfectant or decolonizing agent against methicillin-resistant Staphylococcus aureus infection on on human skin prior to operations. The combination is significantly more effective than treatment with ranalexin or lysostaphin alone, overview
medicine
-
lysostaphin is an effective treatment as well as prophylaxis for Staphylococcus aureus biofilms on indwelling catheters
medicine
-
lysostaphin, in combinantion with the antibiotic ranalexin, is effective against wound or systemic infections caused by meticillin-resistant Staphylococcus aureus. The combination is significantly more effective than treatment with ranalexin or lysostaphin alone. Ranalexin and lysostaphin can be incorporated in wound dressings for the prevention and treatment of topical Staphylococcus aureus infections
medicine
-
a bone morphogenetic protein 2-loaded lysostaphin-delivering hydrogel simultaneously prevents Staphylococcus aureus infection and repairs nonhealing segmental bone defects in the murine radius
medicine
-
enzyme-functionalized gold and silver nanoparticles are an antibacterial platform for combating methicillin-resistant Staphylococcus aureus bacterial infections
medicine
-
the enzyme can be used in life-threatening infections, such as endocarditis to increase the early in vivo activity of the antibiotics, and to prevent the emergence of linezolid resistant mutants
medicine
-
the enzyme is used against established staphylococcal biofilms as an alternative to bovine mastitis control
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thumm, G.; Gtz, F.
Studies on prolysostaphin processing and characterization of lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus
Mol. Microbiol.
23
1251-1265
1997
Staphylococcus simulans
Baba, T.; Schneewind, O.
Target cell specificity of a bacteriocin molecule: a C-terminal signal directs lyostaphin to the cell wall of Staphylococcus aureus
EMBO J.
15
4789-4797
1996
Staphylococcus simulans
Recsei, P.A.; Gruss, A.D.; Novick, R.P.
Cloning, sequence, and expression of the lysostaphin gene from Staphylococcus simulans
Proc. Natl. Acad. Sci. USA
84
1127-1131
1987
Staphylococcus simulans, Staphylococcus simulans NRRL B-2628
Woo Park, P.; Senior, R.M.; Griffin, G.L.; Broekelmann, T.J.; Mudd, M.S.; Mecham, R.P.
Binding and degradation of elastin by the staphylolytic enzyme lysostaphin
Int. J. Cell Biol.
27
139-146
1995
Staphylococcus simulans
Kline, S.A.; de la Harpe, J.; Blackburn, P.
A colorimetric microtiter plate assay for lysostaphin using a hexaglycine substrate
Anal. Biochem.
217
329-331
1994
Staphylococcus simulans
Sugai, M.; Akiyama, T.; Miyake, Y.; Ishida, E.; Suginaka, H.
Rapid purification method of lysostaphin for analysis of cell-wall proteins
J. Microbiol. Methods
12
133-138
1990
Staphylococcus simulans, Staphylococcus simulans NRRL B-2628
-
Cisani, G.; Varaldo, P.E.; Grazi, G.; Soro, O.
High-level potentiation of lysostaphin anti-staphylococcal activity by lysozyme
Antimicrob. Agents Chemother.
21
531-535
1982
Staphylococcus simulans
Robinson, J.M.; Hardman, J.K.; Sloan, G.L.
Relationship between lysostaphin endopeptidase production and cell wall composition in Staphylococcus staphylolyticus
J. Bacteriol.
137
1158-1164
1979
Staphylococcus simulans
Iversen, O.J.; Grov, A.
Studies on lysostaphin. Separation and characterizateion of three enzymes
Eur. J. Biochem.
38
293-300
1973
Staphylococcus simulans, Staphylococcus simulans NRRL B-2628
Fedorov, T.V.; Surovtsev, V.I.; Pletnev, V.Z.; Borozdina, M.A.; Gusev, V.V.
Purification and some properties of lysostaphin, a glycylglycine endopeptidase from the culture liquid of Staphylococcus simulans biovar staphylolyticus
Biochemistry (Moscow)
68
50-53
2003
Staphylococcus simulans
Szweda, P.; Pladzyk, R.; Kotlowski, R.; Kur, J.
Cloning, expression, and purification of the Staphylococcus simulans lysostaphin using the intein-chitin-binding domain (CBD) system
Protein Expr. Purif.
22
467-471
2001
Staphylococcus simulans (P10547), Staphylococcus simulans
Kusuma, C.M.; Kokai-Kun, J.F.
Comparison of four methods for determining lysostaphin susceptibility of various strains of Staphylococcus aureus
Antimicrob. Agents Chemother.
49
3256-3263
2005
Staphylococcus simulans
Surovtsev, V.I.; Fedorov, T.V.; Borozdina, M.A.
Michaelis-Menten kinetics for determining enzymatic activity of lysostaphin
Biochemistry
69
754-756
2004
Staphylococcus simulans
Park, P.W.; Mecham, R.P.
Lysostaphin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) Academic Press
1
1004-1005
2004
Staphylococcus simulans
-
Gruendling, A.; Schneewind, O.
Cross-linked peptidoglycan mediates lysostaphin binding to the cell wall envelope of Staphylococcus aureus
J. Bacteriol.
188
2463-2472
2006
Staphylococcus simulans
Szweda, P.; Kotlowski, R.; Kur, J.
New effective sources of the Staphylococcus simulans lysostaphin
J. Biotechnol.
117
203-213
2005
Staphylococcus simulans (P10547), Staphylococcus simulans
Klein, M.; Kroenke, M.; Krut, O.
Expression of lysostaphin in HeLa cells protects from host cell killing by intracellular Staphylococcus aureus
Med. Microbiol. Immunol.
195
159-163
2006
Staphylococcus simulans
Warfield, R.; Bardelang, P.; Saunders, H.; Chan, W.C.; Penfold, C.; James, R.; Thomas, N.R.
Internally quenched peptides for the study of lysostaphin: An antimicrobial protease that kills Staphylococcus aureus
Org. Biomol. Chem.
4
3626-3638
2006
Staphylococcus simulans
Sharma, R.; Sharma, P.R.; Choudhary, M.L.; Pande, A.; Khatri, G.S.
Cytoplasmic expression of mature glycylglycine endopeptidase lysostaphin with an amino terminal hexa-histidine in a soluble and catalytically active form in Escherichia coli
Protein Expr. Purif.
45
206-215
2006
Staphylococcus simulans
Turner, M.S.; Waldherr, F.; Loessner, M.J.; Giffard, P.M.
Antimicrobial activity of lysostaphin and a Listeria monocytogenes bacteriophage endolysin produced and secreted by lactic acid bacteria
Syst. Appl. Microbiol.
30
58-67
2006
Lactiplantibacillus plantarum, Limosilactobacillus fermentum, Lacticaseibacillus rhamnosus, Staphylococcus simulans, Limosilactobacillus fermentum BR11, Lacticaseibacillus rhamnosus GG
Gruendling, A.; Missiakas, D.M.; Schneewind, O.
Staphylococcus aureus mutants with increased lysostaphin resistance
J. Bacteriol.
188
6286-6297
2006
Staphylococcus simulans, Staphylococcus simulans TNK1
Yang, G.; Gao, Y.; Feng, J.; Huang, Y.; Li, S.; Liu, Y.; Liu, C.; Fan, M.; Shen, B.; Shao, N.
C-terminus of TRAP in Staphylococcus can enhance the activity of lysozyme and lysostaphin
Acta Biochim. Biophys. Sin.
40
452-458
2008
Staphylococcus simulans
Oluola, O.; Kong, L.; Fein, M.; Weisman, L.E.
Lysostaphin in treatment of neonatal Staphylococcus aureus infection
Antimicrob. Agents Chemother.
51
2198-2200
2007
Staphylococcus simulans
Surovtsev, V.I.; Borzenkov, V.M.; Fedorov, T.V.; Smotrov, O.I.
Ionogenic groups in the active site of lysostaphin. Kinetic and thermodynamic data compared with x-ray crystallographic data
Biochemistry (Moscow)
72
989-993
2007
Staphylococcus simulans
LaPlante, K.L.
In vitro activity of lysostaphin, mupirocin, and tea tree oil against clinical methicillin-resistant Staphylococcus aureus
Diagn. Microbiol. Infect. Dis.
57
413-418
2007
Staphylococcus simulans
Graham, S.; Coote, P.J.
Potent, synergistic inhibition of Staphylococcus aureus upon exposure to a combination of the endopeptidase lysostaphin and the cationic peptide ranalexin
J. Antimicrob. Chemother.
59
759-762
2007
Staphylococcus simulans
Kokai-Kun, J.F.; Chanturiya, T.; Mond, J.J.
Lysostaphin as a treatment for systemic Staphylococcus aureus infection in a mouse model
J. Antimicrob. Chemother.
60
1051-1059
2007
Staphylococcus simulans
Yang, X.Y.; Li, C.R.; Lou, R.H.; Wang, Y.M.; Zhang, W.X.; Chen, H.Z.; Huang, Q.S.; Han, Y.X.; Jiang, J.D.; You, X.F.
In vitro activity of recombinant lysostaphin against Staphylococcus aureus isolates from hospitals in Beijing, China
J. Med. Microbiol.
56
71-76
2007
Staphylococcus simulans
Kumar, J.K.
Lysostaphin: an antistaphylococcal agent
Appl. Microbiol. Biotechnol.
80
555-561
2008
Staphylococcus epidermidis, Staphylococcus simulans
Bardelang, P.; Vankemmelbeke, M.; Zhang, Y.; Jarvis, H.; Antoniadou, E.; Rochette, S.; Thomas, N.R.; Penfold, C.N.; James, R.
Design of a polypeptide fluorescence resonance energy transfer substrate that facilitates study of the antimicrobial protease lysostaphin
Biochem. J.
418
615-624
2009
Staphylococcus simulans
Becker, S.C.; Foster-Frey, J.; Donovan, D.M.
The phage K lytic enzyme LysK and lysostaphin act synergistically to kill MRSA
FEMS Microbiol. Lett.
287
185-191
2008
Staphylococcus simulans
Francius, G.; Domenech, O.; Mingeot-Leclercq, M.P.; Dufrene, Y.F.
Direct observation of Staphylococcus aureus cell wall digestion by lysostaphin
J. Bacteriol.
190
7904-7909
2008
Staphylococcus simulans
Placencia, F.X.; Kong, L.; Weisman, L.E.
Treatment of methicillin-resistant Staphylococcus aureus in neonatal mice: lysostaphin versus vancomycin
Pediatr. Res.
65
420-424
2009
Staphylococcus simulans
Desbois, A.P.; Gemmell, C.G.; Coote, P.J.
In vivo efficacy of the antimicrobial peptide ranalexin in combination with the endopeptidase lysostaphin against wound and systemic meticillin-resistant Staphylococcus aureus (MRSA) infections
Int. J. Antimicrob. Agents
35
559-565
2010
Staphylococcus simulans
Kokai-Kun, J.F.; Chanturiya, T.; Mond, J.J.
Lysostaphin eradicates established Staphylococcus aureus biofilms in jugular vein catheterized mice
J. Antimicrob. Chemother.
64
94-100
2009
Staphylococcus simulans
Desbois, A.P.; Lang, S.; Gemmell, C.G.; Coote, P.J.
Surface disinfection properties of the combination of an antimicrobial peptide, ranalexin, with an endopeptidase, lysostaphin, against methicillin-resistant Staphylococcus aureus (MRSA)
J. Appl. Microbiol.
108
723-730
2010
Staphylococcus simulans
Gargis, S.R.; Heath, H.E.; LeBlanc, P.A.; Dekker, L.; Simmonds, R.S.; Sloan, G.L.
Inhibition of the activity of both domains of lysostaphin through peptidoglycan modification by the lysostaphin immunity protein
Appl. Environ. Microbiol.
76
6944-6946
2010
Staphylococcus simulans (P10547)
Schmelcher, M.; Powell, A.M.; Becker, S.C.; Camp, M.J.; Donovan, D.M.
Chimeric phage lysins act synergistically with Lysostaphin to kill mastitis causing Staphylococcus aureus in murine mammary glands
Appl. Environ. Microbiol.
78
2297-22305
2012
Staphylococcus simulans (P10547)
Miao, J.; Pangule, R.C.; Paskaleva, E.E.; Hwang, E.E.; Kane, R.S.; Linhardt, R.J.; Dordick, J.S.
Lysostaphin-functionalized cellulose fibers with antistaphylococcal activity for wound healing applications
Biomaterials
32
9557-9567
2011
Staphylococcus simulans (P10547)
Aguinaga, A.; Francs, M.; Del Pozo, J.; Alonso, M.; Serrera, A.; Lasa, I.; Leiva, J.
Lysostaphin and clarithromycin: A promising combination for the eradication of Staphylococcus aureus biofilms
Int. J. Antimicrob. Agents
37
585-587
2011
Staphylococcus simulans (P10547)
Bastos, M.; Coutinho, B.; Coelho, M.
Lysostaphin: A staphylococcal bacteriolysin with potential clinical applications
Pharmaceuticals
3
1139-1161
2010
Staphylococcus simulans (P10547)
Huang, C.; Hsu, J.; Chung, P.; ChengWINSTON, T.; Jiang, Y.; Ju, Y.
Site-specific N-glycosylation of caprine lysostaphin restricts its bacteriolytic activity toward Staphylococcus aureus
Anim. Biotechnol.
24
129-147
2013
Staphylococcus simulans (P10547)
Lu, H.; Gu, M.; Huang, Q.; Huang, J.; Lu, W.; Lu, H.; Huang, Q.
Hydrogen/deuterium exchange mass spectrometry and site-directed disulfide cross-linking suggest an important dynamic interface between the two lysostaphin domains
Antimicrob. Agents Chemother.
57
1872-1881
2013
Staphylococcus simulans (P10547), Staphylococcus simulans
Hertlein, T.; Sturm, V.; Lorenz, U.; Sumathy, K.; Jakob, P.; Ohlsen, K.
Bioluminescence and 19F magnetic resonance imaging visualize the efficacy of lysostaphin alone and in combination with oxacillin against Staphylococcus aureus in murine thigh and catheter-associated infection models
Antimicrob. Agents Chemother.
58
1630-1638
2014
Staphylococcus simulans (P10547)
Chen, C.; Fan, H.; Huang, Y.; Peng, F.; Fan, H.; Yuan, S.; Tong, Y.
Recombinant lysostaphin protects mice from methicillin-resistant Staphylococcus aureus pneumonia
BioMed Res. Int.
2014
2014
2014
Staphylococcus simulans (P10547)
Sabala, I.; Jonsson, I.; Tarkowski, A.; Bochtler, M.
Anti-staphylococcal activities of lysostaphin and LytM catalytic domain
BMC Microbiol.
12
97
2012
Staphylococcus simulans (P10547)
Sabala, I.; Jagielska, E.; Bardelang, P.; Czapinska, H.; Dahms, S.; Sharpe, J.; James, R.; Than, M.; Thomas, N.; Bochtler, M.
Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans
FEBS J.
281
4112-4122
2014
Staphylococcus simulans (P10547)
Kumar, A.; Khan, I.; Sharma, P.; Sumathy, K.; Ella, K.
Evaluation of activity of recombinant lysostaphin against isolates of meticillin-resistant Staphylococcus aureus from Indian hospitals
J. Med. Microbiol.
63
763-766
2014
Staphylococcus simulans
Filatova, L.Y.; Donovan, D.M.; Ishnazarova, N.T.; Foster-Frey, J.A.; Becker, S.C.; Pugachev, V.G.; Balabushevich, N.G.; Dmitrieva, N.F.; Klyachko, N.L.
A chimeric LysK-lysostaphin fusion enzyme lysing Staphylococcus aureus cells a study of both kinetics of inactivation and specifics of interaction with anionic polymers
Appl. Biochem. Biotechnol.
180
544-557
2016
Staphylococcus simulans
Wu, X.; Kwon, S.J.; Kim, D.; Zha, J.; Mora-Pale, M.; Dordick, J.S.
Unprotonated short-chain alkylamines inhibit staphylolytic activity of lysostaphin in a wall teichoic acid-dependent manner
Appl. Environ. Microbiol.
84
e00693-18
2018
Staphylococcus simulans
Boksha, I.S.; Lavrova, N.V.; Grishin, A.V.; Demidenko, A.V.; Lyashchuk, A.M.; Galushkina, Z.M.; Ovchinnikov, R.S.; Umyarov, A.M.; Avetisian, L.R.; Chernukha, M.I.u.; Shaginian, I.A.; Lunin, V.G.; Karyagina, A.S.
Staphylococcus simulans recombinant lysostaphin production, purification, and determination of antistaphylococcal activity
Biochemistry
81
502-510
2016
Staphylococcus simulans
Tossavainen, H.; Raulinaitis, V.; Kauppinen, L.; Pentikaeinen, U.; Maaheimo, H.; Permi, P.
Structural and functional insights into lysostaphin-substrate interaction
Front. Mol. Biosci.
5
60
2018
Staphylococcus simulans (P10547), Staphylococcus simulans
Sadoogh Abbasian, S.; Soufian, S.; Ghaznavi-Rad, E.; Abtahi, H.
High level activity of recombinant lysostaphin after computer simulation and additive-based refolding
Int. J. Pept. Res. Ther.
25
1241-1249
2019
Staphylococcus simulans
-
Narasimhaswamy, N.; Bairy, I.; Shenoy, G.; Bairy, L.
In vitro activity of recombinant lysostaphin in combination with linezolid, vancomycin and oxacillin against methicillin-resistant Staphylococcus aureus
Iran. J. Microbiol.
9
208-212
2017
Staphylococcus simulans
Ceotto-Vigoder, H.; Marques, S.L.; Santos, I.N.; Alves, M.D.; Barrias, E.S.; Potter, A.; Alviano, D.S.; Bastos, M.C.
Nisin and lysostaphin activity against preformed biofilm of Staphylococcus aureus involved in bovine mastitis
J. Appl. Microbiol.
121
101-114
2016
Staphylococcus simulans
Blazanovic, K.; Zhao, H.; Choi, Y.; Li, W.; Salvat, R.S.; Osipovitch, D.C.; Fields, J.; Moise, L.; Berwin, B.L.; Fiering, S.N.; Bailey-Kellogg, C.; Griswold, K.E.
Structure-based redesign of lysostaphin yields potent antistaphylococcal enzymes that evade immune cell surveillance
Mol. Ther. Methods Clin. Dev.
2
15021
2015
Staphylococcus simulans
Grishin, A.V.; Lavrova, N.V.; Lyashchuk, A.M.; Strukova, N.V.; Generalova, M.S.; Ryazanova, A.V.; Shestak, N.V.; Boksha, I.S.; Polyakov, N.B.; Galushkina, Z.M.; Soboleva, L.A.; Vetchinin, S.S.; Pavlov, V.M.; Karyagina, A.S.; Lunin, V.G.
The influence of dimerization on the pharmacokinetics and activity of an antibacterial enzyme lysostaphin
Molecules
24
1879
2019
Staphylococcus simulans (P10547)
Jun, S.; Cho, S.; Park, Y.
Functionalization of lysostaphin on gold and silver nanoparticles and their in vitro antibacterial activities against methicillin-resistant Staphylococcus aureus
Nanosci. Nanotechnol. Lett.
7
433-440
2015
Staphylococcus simulans
-
Duman, Z.E.; Uenlue, A.; Cakar, M.M.; Uenal, H.; Binay, B.
Enhanced production of recombinant Staphylococcus simulans lysostaphin using medium engineering
Prep. Biochem. Biotechnol.
49
521-528
2019
Staphylococcus simulans (P10547), Staphylococcus simulans, Staphylococcus simulans NRRLB-2628 (P10547)
Chandra Ojha, S.; Imtong, C.; Meetum, K.; Sakdee, S.; Katzenmeier, G.; Angsuthanasombat, C.
Purification and characterization of the antibacterial peptidase lysostaphin from Staphylococcus simulans Adverse influence of Zn2+ on bacteriolytic activity
Protein Expr. Purif.
151
106-112
2018
Staphylococcus simulans (P10547), Staphylococcus simulans
Johnson, C.T.; Sok, M.C.P.; Martin, K.E.; Kalelkar, P.P.; Caplin, J.D.; Botchwey, E.A.; Garcia, A.J.
Lysostaphin and BMP-2 co-delivery reduces S. aureus infection and regenerates critical-sized segmental bone defects
Sci. Adv.
5
eaaw1228
2019
Staphylococcus simulans
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