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Literature summary extracted from

  • Dubin, G.; Wladyka, B.; Stec-Niemczyk, J.; Chmiel, D.; Zdzalik, M.; Dubin, A.; Potempa, J.
    The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity (2007), Biol. Chem., 388, 227-235.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.22.48 cysteine protease staphopain B of Staphylococcus warneri transformed into Escherichia coli strain BL21(DE3)pLysS, expression failed, mutant C21A used for recombinant protein production, expression in Escherichia coli strain BL21(DE3) Staphylococcus warneri
3.4.22.48 expressed in Escherichia coli Staphylococcus aureus
3.4.22.48 expressed in Escherichia coli Staphylococcus epidermidis

Protein Variants

EC Number Protein Variants Comment Organism
3.4.22.48 C21A purification of native staphopain B unsuccessful since strain SW035 produces only minimally detectable protease activity, active-site mutation generated by site-directed mutagenesis, catalytically inactive mutant StpBwar C21A used for interaction studies Staphylococcus warneri

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.22.48 additional information 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 Staphylococcus aureus
3.4.22.48 additional information 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 Staphylococcus epidermidis
3.4.22.48 staphostatin B 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 Staphylococcus warneri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.22.48 3.3
-
 N-Suc-Gly-Phe-Gly-p-nitroanilide used as substrate for staphopain inhibition studies Staphylococcus aureus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.22.48 extracellular secreted, culture supernatant Staphylococcus aureus
-
-
3.4.22.48 extracellular secreted, culture supernatant Staphylococcus epidermidis
-
-
3.4.22.48 extracellular secreted, culture supernatant Staphylococcus warneri
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.48 Staphylococcus aureus
-
-
-
3.4.22.48 Staphylococcus aureus CH-91
-
-
-
3.4.22.48 Staphylococcus epidermidis
-
-
-
3.4.22.48 Staphylococcus warneri
-
 active-site mutant C21A, derived from strain SW035
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.22.48 cysteine protease StpA2aur CH-91 purified by gel filtration Staphylococcus aureus
3.4.22.48 purified by gel filtration Staphylococcus epidermidis
3.4.22.48 recombinant protein, purified by gel filtration Staphylococcus warneri

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.22.48 culture medium purified from Staphylococcus aureus
-
3.4.22.48 culture medium purified from Staphylococcus epidermidis
-
3.4.22.48 culture medium purified from Staphylococcus warneri
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.22.48 additional information
-
 ability of staphostatins to form a complex with the active site mutant C21A of Staphylococcus warneri staphopain determined by size exclusion chromatography Staphylococcus warneri
3.4.22.48 additional information
-
 cloning and characterization of staphopain A2 and its inhibitor from a novel staphylococcal thiol protease operon (stpAB2CH-91), staphopain/staphostatin interaction and evolution of encoding operons analyzed, evidence of ancestral allelic duplication and parallel evolution of the protease/inhibitor pairs suggested Staphylococcus aureus
3.4.22.48 additional information
-
 staphopain A of Staphylococcus epidermidis used for assessment of staphopain-staphostatin interactions, kinetics shown Staphylococcus epidermidis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.48 additional information inhibitory interactions among staphopains and staphostatins determined and used for interaction analysis Staphylococcus warneri ?
-
 ?
3.4.22.48 additional information inhibitory interactions among staphopains and staphostatins determined, staphopain A of Staphylococcus epidermidis purified and used for interaction analysis Staphylococcus epidermidis ?
-
 ?
3.4.22.48 N-Suc-Gly-Phe-Gly-p-nitroanilide + H2O characterization of a staphopain (StpA2aur CH-91) and its inhibitor (StpinA2aur CH-91) from a novel staphylococcal thiol protease operon (stpAB2CH-91), substrate used for inhibition studies Staphylococcus aureus N-Suc-Gly-Phe-Gly + p-nitroaniline
-
 ?
3.4.22.48 N-Suc-Gly-Phe-Gly-p-nitroanilide + H2O characterization of a staphopain (StpA2aur CH-91) and its inhibitor (StpinA2aur CH-91) from a novel staphylococcal thiol protease operon (stpAB2CH-91), substrate used for inhibition studies Staphylococcus aureus CH-91 N-Suc-Gly-Phe-Gly + p-nitroaniline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.48 staphopain A
-
 Staphylococcus epidermidis
3.4.22.48 staphopain B
-
 Staphylococcus warneri

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.22.48 0.2
-
 N-Suc-Gly-Phe-Gly-p-nitroanilide used for inhibition studies of staphopain identified from a novel staphylococcal thiol protease operon stpAB2CH-91 Staphylococcus aureus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.22.48 additional information
-
 additional information inhibitory interactions among staphopains and staphostatins determined Staphylococcus aureus
3.4.22.48 additional information
-
 additional information inhibitory interactions among staphopains and staphostatins indicated, kinetics shown Staphylococcus epidermidis