3.4.23.48: plasminogen activator Pla
This is an abbreviated version!
For detailed information about plasminogen activator Pla, go to the full flat file.
Word Map on EC 3.4.23.48
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3.4.23.48
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aureus
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staphylococci
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methicillin-resistant
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microbiological
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methicillin
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vancomycin
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nosocomial
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epidermidis
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gentamicin
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mastitis
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catheter
-
enterotoxin
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oxacillin
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swab
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ciprofloxacin
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bacteriological
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cocci
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amikacin
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clindamycin
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enterococci
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saprophyticus
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haemolyticus
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staph
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bacteremia
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methicillin-susceptible
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catheter-related
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viridans
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mupirocin
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tsst-1
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antibiograms
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linezolid
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xylosus
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kirby-bauer
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panton-valentine
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hyicus
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ceftazidime
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thermonuclease
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cefoxitin
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analysis
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medicine
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leukocidin
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teicoplanin
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methicillin-sensitive
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endophthalmitis
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warneri
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fusidic
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sccmec
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toxin-1
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imipenem
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ca-mrsa
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bactec
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capitis
- 3.4.23.48
- aureus
-
staphylococci
-
methicillin-resistant
-
microbiological
- methicillin
- vancomycin
-
nosocomial
- epidermidis
- gentamicin
- mastitis
-
catheter
- enterotoxin
- oxacillin
-
swab
- ciprofloxacin
-
bacteriological
-
cocci
- amikacin
- clindamycin
-
enterococci
- saprophyticus
- haemolyticus
-
staph
- bacteremia
-
methicillin-susceptible
-
catheter-related
- viridans
- mupirocin
-
tsst-1
-
antibiograms
- linezolid
- xylosus
-
kirby-bauer
-
panton-valentine
- hyicus
- ceftazidime
- thermonuclease
- cefoxitin
- analysis
- medicine
-
leukocidin
- teicoplanin
-
methicillin-sensitive
- endophthalmitis
- warneri
-
fusidic
-
sccmec
-
toxin-1
- imipenem
-
ca-mrsa
-
bactec
- capitis
Reaction
Converts human Glu-plasminogen to plasmin by cleaving the Arg560-/-Val peptide bond that is also hydrolysed by the mammalian u-plasminogen activator and t-plasminogen activator. Also cleaves arginyl bonds in other proteins =
Synonyms
beta-Pla, coagulase, fibrinolysin, outer membrane protease, Pla, Pla protease, plasminogen activator, plasminogen activator Pla, plasminogen activator protease Pla, YapE
ECTree
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Activating Compound on EC 3.4.23.48 - plasminogen activator Pla
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
bacterial lipopolysaccharide
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LPS is required for the enzymatic activity of omptins, and in particular, LPS with short O-antigen side chains (rough LPS) is required for omptin activity toward many exogenous macromolecular substrates. It is thought that an extended O-antigen side chain (smooth LPS) sterically interferes with substrate binding
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