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Literature summary for 3.4.22.48 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
Search for more literature for 3.4.22.48

Cloned(Commentary)

Cloned (Comment) Organism
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
expressed in Escherichia coli Staphylococcus aureus
expressed in Escherichia coli Staphylococcus epidermidis

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
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
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
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]

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

Localization

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

Organism

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

Purification (Commentary)

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

Source Tissue

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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
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
additional information
-
 staphopain A of Staphylococcus epidermidis used for assessment of staphopain-staphostatin interactions, kinetics shown Staphylococcus epidermidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information inhibitory interactions among staphopains and staphostatins determined and used for interaction analysis Staphylococcus warneri ?
-
 ?
additional information inhibitory interactions among staphopains and staphostatins determined, staphopain A of Staphylococcus epidermidis purified and used for interaction analysis Staphylococcus epidermidis ?
-
 ?
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
-
 ?
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

Synonyms Comment Organism
staphopain A
-
 Staphylococcus epidermidis
staphopain B
-
 Staphylococcus warneri

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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]

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