3.4.22.48: staphopain
This is an abbreviated version!
For detailed information about staphopain, go to the full flat file.
Word Map on EC 3.4.22.48
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3.4.22.48
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aureus
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staphylococcal
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streptococcal
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pyogenes
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staphostatins
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speb
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exotoxin
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pyrogenic
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aureolysin
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sspc
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gordonii
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pharmacology
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medicine
- 3.4.22.48
- aureus
-
staphylococcal
- streptococcal
- pyogenes
- staphostatins
- speb
-
exotoxin
-
pyrogenic
- aureolysin
- sspc
- gordonii
- pharmacology
- medicine
Reaction
broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate =
Synonyms
Ecp, extracellular cysteine protease, SCPA, Sscp A, Sscp B, SspB, SspB protein, staphopain, staphopain A, staphopain B, staphopain C, staphylopain
ECTree
3.4.22.48 staphopainAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.4.22.48 - staphopain
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
L-trans-epoxysuccinyl-leucylamide-(4-guanido)-butane
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E-64, irreversible inhibitor
squamous cell carcinoma antigen 1
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the high association rate constant (kass) for inhibitory complex formation (19000 M/s for staphopain A interaction with SCCA1) suggests that squamous cell carcinoma antigen 1 (SCCA1) can regulate staphopain activity in vivo at epithelial surfaces infected/colonized by Staphylococcu aureus; the high association rate constant (kass) for inhibitory complex formation (58000 M/s for staphopain A interaction with SCCA1) suggests that squamous cell carcinoma antigen 1 (SCCA1) can regulate staphopain activity in vivo at epithelial surfaces infected/colonized by Staphylococcu aureus
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staphostatins
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co-expression of staphopain and inhibitor staphostatin from the same operon, regulatory effect; endogenous proteins that specifically inhibit staphopain; formation of tight and stable non-covalent complexes
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staphostatin A
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absolute specific for staphopain A; encoded by the gene scpB
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staphostatin A
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i.e. ScpB, intracellular, endogenous specific inhibitor of ScpA forming noncovalent complexes, structure determination, slight cleaving of the inhibitor by the enzyme
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staphostatin B
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endogenous inhibitor of cysteine proteases, recombinantly expressed in Escherichia coli as wild-type protein and mutant and purified; forms a mixed eight-stranded beta-barrel; structural interactions between inhibitor and enzyme are resolved from crystal structure of the enzyme-inhibitor complex
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staphostatin B
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absolute specific for staphopain B; encoded by the gene scpC
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staphostatin B
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i.e. SspC, intracellular, endogenous specific inhibitor of SspB forming noncovalent complexes, structure determination, slight cleaving of the inhibitor by the enzyme
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staphostatin B
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characterization of an endogenous staphostatin from Staphylococcus warneri and its target protease, in vivo assessment of inhibitory activities tested, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, inhibition only observed if both proteins belong to the same subgroup of either staphopain A/staphostatin A or staphopain B/staphostatin B orthologs
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additional information
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no inhibition by human kininogens and cystatin C
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additional information
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the proregion of the zymogen is inhibitory for the mature enzyme
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additional information
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inhibitory interactions among staphopains and staphostatins analyzed, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, in vivo assessment of inhibitory activities, inhibitory activities and stoichiometry presented
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additional information
no inhibition of the cysteine proteases staphopain A by cystatin A, C, D and cystatin E/M, inhibitors shown to be hydrolyzed by staphopain A, inhibitory activity of native and staphopain-generated modified forms of cystatins presented; no inhibition of the cysteine proteases staphopain B by cystatin A, C, D and cystatin E/M, inhibitory activity of native and staphopain-generated modified forms of cystatins presented
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additional information
no inhibition of the cysteine proteases staphopain A by cystatin A, C, D and cystatin E/M, inhibitors shown to be hydrolyzed by staphopain A, inhibitory activity of native and staphopain-generated modified forms of cystatins presented; no inhibition of the cysteine proteases staphopain B by cystatin A, C, D and cystatin E/M, inhibitory activity of native and staphopain-generated modified forms of cystatins presented
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additional information
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no inhibition of the cysteine proteases staphopain A by cystatin A, C, D and cystatin E/M, inhibitors shown to be hydrolyzed by staphopain A, inhibitory activity of native and staphopain-generated modified forms of cystatins presented; no inhibition of the cysteine proteases staphopain B by cystatin A, C, D and cystatin E/M, inhibitory activity of native and staphopain-generated modified forms of cystatins presented
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additional information
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immunglobulin G and immunglobulin G's Fc fragment reduce the effect of SspB
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additional information
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no inhibition by O-phenanthroline, diisofluorophosphate, phenylmethanesulfonyl fluoride, human kininogens and cystatins A,C, and D
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additional information
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staphostin homologue genes are probably encoding enzyme inhibitors
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additional information
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in vivo assessment of inhibitory activities determined, inhibitor derived from one species of Staphylococcus can inhibit the staphopain from another species, inhibition only observed if both proteins belong to the same subgroup of either staphopain A/staphostatin A or staphopain B/staphostatin B orthologs
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additional information
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staphostin homologue genes are probably encoding enzyme inhibitors
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