Information on EC 3.4.24.40 - serralysin

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
3.4.24.40
-
RECOMMENDED NAME
GeneOntology No.
serralysin
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Preferential cleavage of bonds with hydrophobic residues in P1'
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aeruginolysin
-
-
Alkaline protease
-
-
Alkaline protease
Pseudomonas aeruginosa MTCC 7926
-
-
-
calcium-regulated alkaline protease
-
-
DR2310 protease
-
-
Escherichia freundii proteinase
-
-
-
-
Extracellular metalloproteinase
-
-
-
-
protease B
-
-
protease B
Xenorhabdus kozodoii Morocco strain
-
-
-
protease C
-
-
protease I
Pseudomonas aeruginosa PA
-
-
-
Proteinase, Serratia marcescens metallo-
-
-
-
-
PrtA metalloprotease
-
-
PrtA metalloprotease
Erwinia chrysanthemi B374
-
-
-
pseudomonal serralysin
-
-
Pseudomonas aeruginosa alk. protease
-
-
-
-
Pseudomonas aeruginosa alkaline protease
-
-
Pseudomonas aeruginosa alkaline proteinase
-
-
-
-
Pseudomonas alkaline protease
-
-
psychrophilic alkaline metalloprotease
-
PAP
psychrophilic alkaline metalloprotease
Pseudomonas sp. TAC-II-18
-
PAP
-
serralysin-like metalloprotease
-
-
serralysin-like metalloprotease
Xenorhabdus kozodoii Morocco strain
-
-
-
Serratia marcescens extracellular proteinase
-
-
-
-
Serratia marcescens metalloprotease
-
-
-
-
Serratia marcescens metalloprotease
-
-
Serratia marcescens metalloproteinase
-
-
-
-
thermoalkaline protease
-
-
thermoalkaline protease
Pseudomonas putida SKG-1
-
-
-
thermostable alkaline protease
-
-
Zinc proteinase
-
-
-
-
LupA
D0VMS8
sequence alignment reveals that the protein belongs to the serralysin-type metalloproteases
additional information
-
belongs to serralysin subfamily M12
additional information
-
subfamily serralysins together with astacins, snake venom and matrix metalloproteinases should be grouped into a common family, the metzincins (closely related to the thermolysin family)
additional information
-
belongs to serralysin subfamily M12
additional information
-
subfamily serralysins together with astacins, snake venom and matrix metalloproteinases should be grouped into a common family, the metzincins (closely related to the thermolysin family)
additional information
-
belongs to serralysin subfamily M12
additional information
-
subfamily serralysins together with astacins, snake venom and matrix metalloproteinases should be grouped into a common family, the metzincins (closely related to the thermolysin family)
additional information
-
belongs to serralysin subfamily M12
CAS REGISTRY NUMBER
COMMENTARY
70851-98-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
psychrophilic strain B-3038
-
-
Manually annotated by BRENDA team
Erwinia chrysanthemi B374
B374
-
-
Manually annotated by BRENDA team
i.e. strain UH-5
-
-
Manually annotated by BRENDA team
native and recombinant protein
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa MTCC 7926
i.e. strain UH-5
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PA
PA
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens KT1
KT1
-
-
Manually annotated by BRENDA team
MTCC 10510
-
-
Manually annotated by BRENDA team
Pseudomonas putida SKG-1
MTCC 10510
-
-
Manually annotated by BRENDA team
Pseudomonas sp. TAC-II-18
-
-
-
Manually annotated by BRENDA team
derepressed strain
-
-
Manually annotated by BRENDA team
strain BG
-
-
Manually annotated by BRENDA team
strain kums 3958 (clinical isolate)
-
-
Manually annotated by BRENDA team
strains SF 178, SH 186 (both serotype 06/014:H12 and bacitrocin type 18)
-
-
Manually annotated by BRENDA team
wild-type
-
-
Manually annotated by BRENDA team
Serratia marcescens BG
strain BG
-
-
Manually annotated by BRENDA team
formerly Aranicola proteolyticus, symbiotic bacterium of spider Nephila clavata
-
-
Manually annotated by BRENDA team
strain E-15
-
-
Manually annotated by BRENDA team
Xenorhabdus kozodoii Morocco strain
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the calcium-regulated alkaline protease is implicated in multiple modes of infection
physiological function
-
the alkaline protease AprA is associated with bacterial virulence and interferes with complement-mediated lysis of erythrocytes and complement activation. AprA potently blocks phagocytosis and killing of Pseudomonas by human neutrophils. AprA inhibits opsonization of bacteria with C3b and the formation of the chemotactic agent C5a. AprA specifically blocks C3b deposition via the classical and lectin pathways, whereas the alternative pathway is not affected. AprA degrades both human C1s and C2, and the mechanism of action for complement inhibition is cleavage of C2, overview
evolution
-
the calcium-regulated alkaline protease is a member of the repeats in toxin, RTX, family of proteins
additional information
-
the enzyme is compatible at 60C with commercial detergents
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
125I-insulin + H2O
?
show the reaction diagram
-
-
-
-
?
2-Aminobenzoyl-Gly-Phe-Arg-Leu-Leu 4-nitrobenzyl amide + H2O
?
show the reaction diagram
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
-
-
2-Aminobenzoyl-Gly-Phe-Arg-Xaa 4-nitrobenzyl amide + H2O
?
show the reaction diagram
-
Xaa is Gly, Ala, Val, Leu or Phe, Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
-
-
Abz-LGMISLMKRPPGFSPFRSSRI-NH2 + H2O
?
show the reaction diagram
-
peptide corresponds to fragment L373-I393 of human kininogen, cleavage of Arg-Ser, Gly-Phe and Lys-Arg bond
-
-
?
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt + H2O
?
show the reaction diagram
-
-
-
-
?
Aminoethylated lysozyme + H2O
?
show the reaction diagram
-
-
-
-
-
angiotensin I + H2O
DRVY + IHPFLHL + DRVYI + HPFHL
show the reaction diagram
-
-
-
?
Angiotensin II + H2O
?
show the reaction diagram
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
-
-
-
?
azocasein + H2O
?
show the reaction diagram
Serratia marcescens BG
-
-
-
-
-
azocasein + H2O
?
show the reaction diagram
Pseudomonas sp. TAC-II-18
-
-
-
-
?
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl tripeptides + H2O
?
show the reaction diagram
-
overview
-
-
-
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
cleavage site: Ala+Ala-Ala
-
-
-
Benzyloxycarbonyl-Ala-Gly-Gly-Leu + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Ala-Gly-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Ala-Gly-Gly-Leu-Xaa + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P3' results in marked increase in hydrolysis
-
-
-
Benzyloxycarbonyl-Ala-Phe-Gly-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Ala-Phe-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Ala-Ala + H2O
?
show the reaction diagram
-
cleavage site: Gly-Ala
-
-
-
Benzyloxycarbonyl-Gly-Gly-Gly-Leu + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
Benzyloxycarbonyl-Gly-Gly-Leu amide + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
Benzyloxycarbonyl-Gly-Leu-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Leu-Gly-Gly-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Gly-Leu-Gly-Gly-Xaa + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P3' results in marked increase in hydrolysis
-
-
-
Benzyloxycarbonyl-Gly-Leu-Xaa + H2O
?
show the reaction diagram
-
at position Xaa with decreasing susceptibility to the enzyme: Leu, Phe or Ala, poor substrates: Gly or NH2, D-Ala
-
-
-
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Phe-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Phe-Ala-Ala + H2O
?
show the reaction diagram
-
cleavage site: Phe-Ala
-
-
-
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
-
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
?
show the reaction diagram
-
best substrate
-
-
-
Benzyloxycarbonyl-Phe-Xaa-Ala + H2O
Benzyloxycarbonyl-Phe + Xaa-Ala
show the reaction diagram
-
susceptibility to the enzyme is Xaa-dependent, in decreasing order of efficiency: Ala, Phe, Leu, Trp or Ser or Gly
-
-
Benzyloxycarbonyl-Xaa-Ala-Ala + H2O
Benzyloxycarbonyl-Xaa + Ala-Ala
show the reaction diagram
-
susceptibility to the enzyme is Xaa-dependent, in decreasing order of efficiency: L-Phe, Leu or Ala, Val, Gly, D-Ala
-
-
Benzyloxycarbonyl-Xaa-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
-
-
-
Benzyloxycarbonyl-Xaa-Leu-Ala + H2O
Benzyloxycarbonyl-Xaa + Leu-Ala
show the reaction diagram
-
susceptibility to the enzyme is Xaa-dependent, in decreasing order of efficiency: L-Phe, Leu or Ala, Val, Gly, D-Ala
-
-
Benzyloxycarbonyl-Xaa-Phe-Gly-Ala + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
-
-
-
Benzyloxycarbonyl-Xaa-Phe-Leu-Ala + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
-
-
-
beta-1,3 glucan recognition protein 2 + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Xenorhabdus kozodoii, Xenorhabdus kozodoii Morocco strain
-
-
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Xenorhabdus kozodoii, Xenorhabdus kozodoii Morocco strain
-
-
-
-
?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Xenorhabdus kozodoii, Xenorhabdus kozodoii Morocco strain
-
-
-
-
?
C-terminal octapeptide of glucagon + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
Carboxymethyl-beta-insulin + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
casein + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
?
show the reaction diagram
-
-
-
-
-
casein + H2O
?
show the reaction diagram
Pseudomonas aeruginosa PA
-
-
-
-
?
D-Ala-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Dabcyl-Glu-Val-Tyr-Ala-Val-Glu-Ser-Edans + H2O
?
show the reaction diagram
-
-
-
-
?
DL-Val-Leu-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Egg albumin + H2O
?
show the reaction diagram
-
-
-
-
-
Fibrin + H2O
?
show the reaction diagram
-
-
-
-
?
Fibrinogen + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
?
furylacryloyl-Ala-Leu-Val-Tyr + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Leu-Gly-Pro-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
-
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
gelatine + H2O
?
show the reaction diagram
Pseudomonas aeruginosa, Pseudomonas aeruginosa PA
-
-
-
-
?
Glucagon + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
Glycoprotein G + H2O
?
show the reaction diagram
-
i.e. thrombin-sensitive protein, thrombospondin, MW 190000
-
-
-
hemocyte aggregation inhibitor protein (HAIP) + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
-
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
-
hide powder azure + H2O
?
show the reaction diagram
-
-
-
-
-
His-Ser-4-methoxy-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
His-Ser-4-methoxynaphthylamide + H2O
His-Ser + 4-methoxynaphthylamide
show the reaction diagram
-
-
-
-
?
Human alpha1-proteinase inhibitor + H2O
?
show the reaction diagram
-
MW 52000
-
-
-
human complement component C1 + H2O
?
show the reaction diagram
-
-
-
-
?
human complement component C2 + H2O
?
show the reaction diagram
-
-
-
-
?
Human platelet surface glycoprotein Ib + H2O
?
show the reaction diagram
-
-
-
-
-
Immunoglobulin A1 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin A2 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin G1 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin G2 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin G3 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin G4 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
including serpin-1I + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
interleukin-6 + H2O
?
show the reaction diagram
-
complete digestion
-
-
?
interleukin-8 + H2O
?
show the reaction diagram
-
rapid processing to a 72 amino acid form, further degradation is slow
-
-
?
L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala + L-Ala-L-Ala
show the reaction diagram
-
-
-
-
L-Ala-L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala + L-Ala-L-Ala-L-Ala
show the reaction diagram
-
-
-
-
L-Ala-L-Ala-L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala-L-Ala + L-Ala-L-Ala-L-Ala
show the reaction diagram
-
-
-
-
L-Ala-oligopeptides + H2O
?
show the reaction diagram
-
proteolytic activity increases drastically with increasing chain length from tetramer to hexamer, no substrate: dipeptide or tripeptide
-
-
-
N-alpha-benzoyl-DL-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
artificial substrate BAPNA
-
?
N-benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-terminal hexapeptide of glucagon + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KDR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KFR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KGRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KGR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KHRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KHR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLAFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLA + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLDFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLD + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLEFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLE + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLFFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLF + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLGFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLG + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLHFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLH + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLKFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLK + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLLFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLL + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLMFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLM + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLNFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLN + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLPFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLP + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLQFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLQ + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRASKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + ASKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRDSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + DSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRLSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + LSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + NSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRRSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + RSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + SSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLSFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLS + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLTFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLT + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLXWFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLXW + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLYFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLY + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KNRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KNR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KQRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KQR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KRRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KRR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KSR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
Oxidized insulin B-chain + H2O
?
show the reaction diagram
-
cleavage specificity of Pseudomonas aeruginosa, Pseudomonas fragi, Serratia sp. and Proteus mirabilis enzyme
-
-
-
peptide 6A + H2O
?
show the reaction diagram
-
-
-
?
Plasma fibronectin + H2O
?
show the reaction diagram
-
Serratia marcescens MW 52000 enzyme, cleavage sites
-
-
-
Plasma fibronectin + H2O
?
show the reaction diagram
-
from pig
-
-
-
Pro-Phe-Arg 4-methylcoumarin 7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
-
Pro-Phe-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Ribonuclease + H2O
?
show the reaction diagram
-
-
-
-
-
scolexins A + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
scolexins B + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
serine proteinase homolog 3 + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
serpin-1 variants + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA, six serpin-1 variants differing in their 40- to 50-amino-acid-long C-terminal sequences are identified
-
-
?
substance P + H2O
RPKPQQFFG + LM-NH2 + RPKPQQFF + GLM-NH2 + RPKQQF + FGLM-NH2
show the reaction diagram
-
-
-
?
substance P 1-7 + H2O
?
show the reaction diagram
-
-
-
?
substance P 1-9 + H2O
RPKP + QQFFG + RPKQQ + FFG
show the reaction diagram
-
-
-
?
substance P 7-11 + H2O
?
show the reaction diagram
-
-
-
?
substance P 8-11 + H2O
?
show the reaction diagram
-
-
-
?
substance P(free acid) + H2O
RPKPQQFFG + LM + RPKPQQFF + GLM + RPKQQF + FGLM
show the reaction diagram
-
-
-
?
Suc-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Succ-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Succ-Ala-Ala-Pro-Xaa-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
Pseudomonas fluorescens, Pseudomonas fluorescens KT1
-
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
Pseudomonas fluorescens, Pseudomonas fluorescens KT1
-
-
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
Pseudomonas fluorescens, Pseudomonas fluorescens KT1
-
-
-
-
?
t-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Gly-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Gly-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Leu-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
Pseudomonas fluorescens KT1
-
-
-
-
?
t-butyloxycarbonyl-Met-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
Pseudomonas fluorescens KT1
-
-
-
-
?
t-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Tryptic insulin heptapeptide + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
show the reaction diagram
Xenorhabdus kozodoii, Xenorhabdus kozodoii Morocco strain
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
elastin
-
-
-
additional information
?
-
-
no substrates are small peptides
-
-
-
additional information
?
-
-
broad substrate side-chain specificity: hydrophobic amino acid residues at P2 and P2' are favorable
-
-
-
additional information
?
-
-
benzoyl-L-Arg amide, acetyl-L-Tyr ethyl ester, carbobenzoxy-Glu-Tyr, carbobenzoxy-Gly-Phe, L-Leu amide
-
-
-
additional information
?
-
-
human platelet surface glycoprotein V
-
-
-
additional information
?
-
-
minimum peptide size: hexapeptide
-
-
-
additional information
?
-
-
collagen
-
-
-
additional information
?
-
-
trypsin-alpha1-proteinase inhibitor complex
-
-
-
additional information
?
-
-
no esterase activity: no substrates are N-benzoyl-L-Arg ethyl ester or N-benzoyl-L-Tyr ethyl esters
-
-
-
additional information
?
-
-
tetrapeptides are poorer substrates than benzyloxycarbonyl tetrapeptides, benzyloxycarbonyl dipeptides, N-acetylated amino acid esters or amides, dipeptide amides, tripeptides, benzyloxycarbonyl-(Gly)4, benzyloxycarbonyl-(Gly)5, benzyloxycarbonyl-Gly-Leu-Gly-Gly-D-Ala
-
-
-
additional information
?
-
-
important factor in virulence seen in several microbial diseases caused by Pseudomonas aeruginosa and Serratia marcescens, e.g. corneal ulcers and pneumonia, inducible enzyme
-
-
-
additional information
?
-
-
inhibits cytokine-induced signaling in A549 pulmonary epithelial cells
-
-
-
additional information
?
-
-
inhibits IFN-gamma antiviral and immunomodulatory activity
-
-
-
additional information
?
-
-
S1 subsite has a broad specificity, being Gly the preferred amino acid followed by positively charged residues Arg and His. S2 and S1 subsites accomodate better hydrophilic residues with aliphatic or aromatic side chains like Leu or Phe
-
-
-
additional information
?
-
-
no substrate: casein, bovine serum albumin, lysozyme, lactalbumin, lactoglobulin and thyroglobulin
-
-
-
additional information
?
-
Xenorhabdus kozodoii, Xenorhabdus kozodoii Morocco strain
-
substrate specificity, and reaction product analysis by electron-spray ionization mass spectrometry, overview. Protease B requires at least three amino acids N-terminal to the scissile bond for detectable hydrolysis. On such substrate protease B is clearly specific for positively charged residues, Arg and Lys, at the P1 substrate position and is rather permissive in the others, but Ser at P1 is preferred in the oligopeptide substrate which contained amino acids also C-terminal to the scissile bond
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
human complement component C1 + H2O
?
show the reaction diagram
-
-
-
-
?
human complement component C2 + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
important factor in virulence seen in several microbial diseases caused by Pseudomonas aeruginosa and Serratia marcescens, e.g. corneal ulcers and pneumonia, inducible enzyme
-
-
-
additional information
?
-
-
inhibits cytokine-induced signaling in A549 pulmonary epithelial cells
-
-
-
additional information
?
-
-
inhibits IFN-gamma antiviral and immunomodulatory activity
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
1-2 gatom/mol enzyme; no activation by added Ca2+
Ca2+
-
requirement
Ca2+
-
7 gatom/mol enzyme; requirement
Ca2+
-
weakly restores activity after EDTA treatment, Serratia marcescens MW 56000 and MW 60000 enzymes
Ca2+
-
activation
Ca2+
-
stabilizing
Ca2+
-
in presence of Ca2+, Zn2+ or Co2+ may recativate EDTA-inactivated protease. Ca2+ concentrations required are between 0.01 mM and 0.1 mM, inhibitory above 0.1 mM
Ca2+
Q3YAW3
required
Ca2+
-
activates
Ca2+
-
calcium-regulated alkaline protease, role of Ca2+ in enzyme folding and activation: Ca2+binding induces RTX folding, which serves to chaperone the folding of the protease domain. Subsequent association of the RTX domain with an N-terminal alpha-helix stabilizes AP, Ca2+ regulates the RTX family of virulence factors, overview
Co2+
-
above 5 mM, benzoxycarbonyl-Ala-Phe-Gly-Ala as substrate; activation
Co2+
-
1 mM, at pH 10, not at pH 7; activation
Co2+
-
in the presence of Ca2+, restoration of EDTA-inactivied protease. No reactivation in absence of Ca2+
Co2+
-
slightly activating
Cu2+
-
slightly activating
Cu2+
-
activates
Fe2+
-
restores activity after EDTA treatment, Serratia marcescens MW 56000 enzyme, not MW 60000 enzyme
Mg2+
-
activation
Zn2+
-
zinc-containing metalloproteinase (not)
Zn2+
-
zinc-binding motif: His-Glu-Xaa-Xaa-His
Zn2+
-
active site ion; zinc-containing metalloproteinase
Zn2+
-
added Zn2+ inhibits; zinc-containing metalloproteinase
Zn2+
-
zinc-containing metalloproteinase
Zn2+
-
zinc-binding motif: His-Glu-Xaa-Xaa-His; zinc-binding motif: His-Glu-Xaa-Xaa-His (Pseudomonas aeruginosa, Erwinia chrysanthemi, Serratia sp. E-15); zinc-containing metalloproteinase
Zn2+
-
1 gatom/mol enzyme (Serratia marcescens, Serratia sp., Serratia piscatrum); 1 mol/mol enzyme; restores activity after EDTA treatment (Serratia marcescens MW 56000 and MW 60000 enzymes); zinc-binding motif: His-Glu-Xaa-Xaa-His; zinc-containing metalloproteinase
Zn2+
-
1 gatom/mol enzyme (Serratia marcescens, Serratia sp., Serratia piscatrum); 1 mol/mol enzyme; zinc-binding motif: His-Glu-Xaa-Xaa-His; zinc-binding motif: His-Glu-Xaa-Xaa-His (Pseudomonas aeruginosa, Erwinia chrysanthemi, Serratia sp. E-15); zinc-containing metalloproteinase
Zn2+
-
zinc-containing metalloproteinase
Zn2+
-
zinc-containing metalloproteinase (not)
Zn2+
-
zinc-binding consensus sequence in comparison to astacins, snake venom, matrix metalloproteinases; zinc-containing metalloproteinase
Zn2+
-
zinc-containing metalloproteinase
Zn2+
-
Zn2+ is bound at the active site
Zn2+
-
zinc-dependent metalloprotease
Zn2+
-
one Zn2+ per protein molecule
Zn2+
-
in the presence of Ca2+, restoration of EDTA-inactivied protease. No reactivation in absence of Ca2+. Inhibitory above 0.025 mM
Mn2+
-
activates
additional information
-
contains no significant amount of any metal except Ca2+; no activation by Mn2+; no activation by Ni2+
additional information
-
atomic absorption spectroscopy; magnesium, manganese, cobalt, copper or iron
additional information
-
no activation by Fe3+, Mg2+; no activation by Mn2+
additional information
-
no activation by Rb2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
1 mM
1,10-phenanthroline
-
reversible by dialysis, Mg2+ or Co2+ partially restores; strong
1,10-phenanthroline
-
neither Ca2+, Zn2+ nor Fe2+ restores
1,10-phenanthroline
-
Serratia marcescens enzyme
1,10-phenanthroline
-
10 mM; strong
1,10-phenanthroline
-
30 min, room temperature, pH 7.5, complete and irreversible inhibition in a concentration range below 1 mM
1,10-phenanthroline
-
pH 7.8, 37C, 1 mM 66% inhibition, 3mM 90% inhibition
1,10-phenanthroline
-
10 mM, strong inhibition at pH 5.5 and pH 8.0 with and without addition of 1 mM Co2+
1,10-phenanthroline
-
complete inhibition
1,10-phenanthroline
-
activity can be restored with the addition of Mn2+, Cu2+ and Co2+ up to 90-200% of its original value, while Zn2+ is inefficient
1,10-phenantroline
-
-
2,2'-Bipyridyl
-
5 mM
2,2'-Bipyridyl
-
weak
2,2'-Bipyridyl
-
not
8-hydroxyquinoline
-
0.1 mM at pH 10, 5 mM at pH 7
Ac-Val-Leu-Lys-4-mercaptoanilide
-
pH 7.8, 37C, 0.2 mM 69% inhibition, 0.3 mM complete inhibition
antipain
-
only Serratia marcescens MW 56000 enzyme
APRin protein
-
slow binding inhibition, reversible inhibition. and truncated mutants
-
benzalkonium chloride
-
-
Benzyloxycarbonyl-D-Ala-Leu-Ala
-
competitive to benzyloxycarbonyl-Ala-Phe-Gly-Ala
Benzyloxycarbonyl-Gly-Leu-D-Ala
-
benzyloxycarbonyl-Ala-Phe-Gly-Ala as substrate
Benzyloxycarbonyl-Gly-Leu-Gly
-
benzyloxycarbonyl-Ala-Phe-Gly-Ala as substrate
Benzyloxycarbonyl-Gly-Leu-NH2
-
benzyloxycarbonyl-Ala-Phe-Gly-Ala as substrate
Benzyloxycarbonyl-Phe-D-Leu-Ala
-
competitive to benzyloxycarbonyl-Ala-Phe-Gly-Ala
Bovine pancreatic trypsin inhibitor
-
0.01 mM, 5% inhibition at pH 5.5
-
Ca2+
-
inhibitory above 0.1 mM
Cd2+
-
at pH 10, not at pH 7
chymostatin
-
0.1 mM, 18% inhibition at pH 8.0
Co2+
-
inhibitory above 5 mM
Cysteine hydrochloride
-
weak
diisopropylfluorophosphate
-
1 mM, weak inhibition at pH 5.5 and pH 8.0 with and without addition of 1 mM Co2+
dithiothreitol
Q3YAW3
5 mM, 5% residual activity
DTNB
-
reversible, synergism with pyridoxal 5'-phosphate or phenylglyoxal
EDTA
-
0.1 mM at pH 10, 5 mM at pH 7
EDTA
-
Ca2+ (partially); Cu2+ restores partially; more effective at acidic pH; partially reversible by dialysis
EDTA
-
Ca2+ (not) restores; Fe2+ (not); Zn2+ (not)
EDTA
-
Ca2+ (MW 56000 and MW 60000 enzyme); Ca2+ (partially); Co2+ (Serratia sp. E-16 enzyme); Cu2+ (not); Fe2+ (only MW 56000 enzyme); Mg2+ (not); Serratia enzymes; Zn2+ (MW 56000 and MW 60000 enzyme)
EDTA
-
Co2+; Mn2+; strong, 5 mM
EDTA
-
Ca2+ (restored activity higher than native activity); enhances inhibition by guanidine-HCl; Fe2+ (partially); Mg2+; Mn2+ (restored activity higher than native activity); no reactivation by K+; Zn2+ (restored activity higher than native activity)
EDTA
-
30 min, room temperature, pH 7.5, complete inhibition in a concentration range below 1 mM
EDTA
-
10 mM, pH 8, strong inhibition
EDTA
-
10 mM, almost complete inactivation at pH 5.5 and pH 8.0 with and without addition of 1 mM Co2+
EDTA
-
1 mmol, pH 8.1, no inactivation by 0.1 M EDTA
EDTA
-
10 mM, 42% residual activity
EDTA
-
complete inhibition
EDTA
Q3YAW3
5 mM, 23% residual activity
EDTA
-
inhibits the activity only partially even either after long incubation or in excess amount
EGTA
-
10 mM, pH 8, strong inhibition
EGTA
-
complete inhibition
EGTA
Q3YAW3
5 mM, 33% residual activity
Elastatinal
-
0.1 mM, 11% inhibition at pH 8.0 and without 1 mM Co2+ addition
Fe2+
-
strong
-
Guanidine-HCl
-
enhanced by EDTA
HgCl2
-
complete inhibition
KCN
-
at pH 10, no inhibition at pH 7.5
L-trans-epoxysuccinyl-leucyl-amido-(4-guanido)butane
-
0.1 mM, 26% inhibition at pH 8.0 and 1 mM Co2+ addition, 26% inhibition at pH 5.5 without addition of 1 mM Co2+
L3A SmaPI
-
mutant inhibitor
-
L3D SmaPI
-
mutant inhibitor
-
L3F SmaPI
-
mutant inhibitor
-
L3G SmaPI
-
mutant inhibitor
-
L3I SmaPI
-
mutant inhibitor
-
L3K SmaPI
-
mutant inhibitor
-
L3P SmaPI
-
mutant inhibitor
-
Leupeptin
-
weak, only Serratia marcescens MW 56000 enzyme
N-bromosuccinimide
-
strong
N-bromosuccinimide
-
strong
N-bromosuccinimide
-
-
N-ethylmaleimide
-
weak
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
N-ethylmaleimide
-
0.1 mM, 14% inhibition at pH 8.0 and 1 mM Co2+ addition
N-tosyl-L-phenylalanine chloromethyl ketone
-
0.1 mM, 18% inhibition at pH 8.0
NaCl
-
inhibitory effect depends on substrate
NaCl
Q3YAW3
1 M, 56% residual activity
Ni2+
-
at pH 10, not at pH 7
Nitrilotriacetate
-
weak
o-phenanthroline
-
2 mM, no residual activity
o-phenanthroline
Q3YAW3
0.5 mM, 10% residual activity
p-hydroxymercuribenzoate
-
0.002 mM, 71% residual activity
Periplasmic endogen inhibitor peptide of Serratia marcescens
-
recombinant and native form, pH- and heat-stable protein, inhibition at 1:1 molar ratio, highly specific for Serratia marcescens proteinase, mechanism
-
Periplasmic endogen inhibitor peptide of Serratia marcescens
-
-
-
phenyl-methanesulfonyl fluoride
-
1 mM, 14-17% inhibition at pH 5.5 and pH 8.0 with and without addition of 1 mM Co2+
Phenylglyoxal
-
synergism with DTNB
phosphoramidon
-
0.1 mM, no inhibition at pH 8.0 and 1 mM Co2+ addition, 25% inhibition at pH 8.0 and 5.5 without addition of 1 mM Co2+
PMSF
-
weak, Serratia marcescens
pyridoxal 5'-phosphate
-
synergism with DTNB
SmaPI
-
Serratia marcescens metalloprotease inhibitor, wild-type
-
SmaPIAddA
-
mutant inhibitor
-
SmaPIDelG
-
mutant inhibitor
-
SmaPIDelG1-L3
-
mutant inhibitor
-
SmaPIDelG1-S2
-
mutant inhibitor
-
Sodium thioglycolate
-
1 mM, at pH 10, no inhibition at pH 7.5
Sodium thioglycolate
-
weak
Sodium thioglycolate
-
not
Soybean trypsin inhibitor
-
0.01 mM, 9% inhibition at pH 5.5
-
Tetraethylenepentamine
-
zinc-specific chelator
Tetramethylenepentamine
-
Serratia marcescens
Zn2+
-
inhibitory above 0.025 mM
Zn2+
-
both the Zn2+ inhibition of protease B activity and its resistance to EDTA inhibition might be caused by an Asp in position 191 where most of the serralysins contain Asn
Leupeptin
-
0.1 mM, 10% inhibition at pH 8.0 and 1 mM Co2+ addition, 7% inhibition at pH 8.0 without 1 mM Co2+ addition
additional information
-
diisopropyl phosphofluoridate; PCMB; potato inhibitor; soybean trypsin inhibitor; tosyl-L-Phe chloromethyl ketone or tosyl-L-Lys chloromethyl ketone
-
additional information
-
2-mercaptoethanol; diisopropyl phosphofluoridate; iodine, ovomucoid; monoiodoacetic acid; PCMB; potato inhibitor; soybean trypsin inhibitor
-
additional information
-
Lima bean, human pancreatic or egg white trypsin inhibitor, human alpha1-antitrypsin; no inhibition by Mg2+, Mn2+, Ca2+, Ba2+, NaCN, NaN3, sodium arsenite, p-hydroxymercuribenzoate; soybean trypsin inhibitor
-
additional information
-
-
-
additional information
-
-
-
additional information
-
2-mercaptoethanol (Serratia marcescens); diisopropyl phosphofluoridate (Serratia marcescens); GSH, EGTA (Serratia marcescens), phosphoramidon, zincov (i.e. 2-(N-hydroxycarboxamido)-4-methylpentanoyl-L-Ala-glycinamide, thermolysin inhibitor); monoiodoacetic acid (Serratia marcescens)
-
additional information
-
citrate, NaF, oxalate; diisopropyl phosphofluoridate; monoiodoacetic acid; PCMB; potato inhibitor; soybean trypsin inhibitor
-
additional information
-
IAA; PCMB
-
additional information
-
PCMB
-
additional information
-
not inhibited by chloromethylketone or hydroxamate
-
additional information
-
not inhibited by dithiothreitol, PMSF and DFP
-
additional information
-
not inhibitory: triton X-100, tween up to 0.1%
-
additional information
-
not inhibitory: PMSF, E-64 and pepstatin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
8.7
-
Ala-Ala-Ala-Ala
-
-
1.2
-
Ala-Ala-Ala-Ala-Ala
-
-
0.5
-
Ala-Ala-Ala-Ala-Ala-Ala
-
benzyloxycarbonyl-Phe-L-Ala-Ala
2.7
-
Benzyloxycarbonyl-Ala-Ala-Ala
-
-
4.8
-
benzyloxycarbonyl-Ala-Gly-Leu-Ala
-
-
1.5
-
benzyloxycarbonyl-Ala-Leu-Ala
-
-
20
-
benzyloxycarbonyl-D-Ala-Gly-Leu-Ala
-
-
7.7
-
Benzyloxycarbonyl-Gly-Ala-Ala
-
-
5.4
-
benzyloxycarbonyl-Gly-Gly-Leu-Ala
-
benzyloxycarbonyl-Ala-Gly-Gly-Leu
2.9
-
Benzyloxycarbonyl-Gly-Leu-Ala
-
-
2.4
-
benzyloxycarbonyl-Gly-Leu-Gly-Ala
-
-
11
-
Benzyloxycarbonyl-Gly-Leu-Gly-Gly
-
-
4.3
-
Benzyloxycarbonyl-Gly-Leu-Gly-Gly-Ala
-
-
0.9
-
Benzyloxycarbonyl-Gly-Leu-Leu
-
benzyloxycarbonyl-Gly-Phe-Leu-Ala
0.6
-
benzyloxycarbonyl-Gly-Leu-Phe
-
benzyloxycarbonyl-Ala-Phe-Leu-Ala
5.3
-
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala
-
-
0.006
-
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
-
recombinant enzyme, pH 7.8
0.0126
-
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
-
native enzyme, pH 7.8
0.014
-
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
-
recombinant enzyme labeled with L-difluoromethionine, pH 7.8
0.4
-
Benzyloxycarbonyl-Phe-Ala-Ala
-
benzyloxycarbonyl-Phe-Leu-Ala
0.4
-
Benzyloxycarbonyl-Phe-Ala-Ala
-
-
1.8
-
benzyloxycarbonyl-Phe-Gly-Ala
-
benzyloxycarbonyl-Phe-Ser-Ala, benzyloxycarbonyl-Leu-Ala-Ala
2.3
-
benzyloxycarbonyl-Phe-Gly-Leu-Ala
-
benzyloxycarbonyl-Ala-Leu-Gly-Gly
0.2
-
benzyloxycarbonyl-Phe-Phe-Ala
-
-
2.5
-
benzyloxycarbonyl-Val-Ala-Ala
-
benzyloxycarbonyl-Ala-Phe-Gly-Ala
0.00308
-
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.00096
-
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.0027
-
o-aminobenzoyl-KGRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.0007
-
o-aminobenzoyl-KHRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.002
-
o-aminobenzoyl-KLFFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.00582
-
o-aminobenzoyl-KLRDSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00292
-
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00137
-
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00056
-
o-aminobenzoyl-KLWFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.00198
-
o-aminobenzoyl-KNRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00115
-
o-aminobenzoyl-KQRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00157
-
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
17.3
-
Phe-Gly-Leu-Ala
-
-
0.015
-
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
-
without Co2+, pH 8.0
0.023
-
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
-
1 mM Co2+, pH 5.5; without Co2+, pH 5.5
0.035
-
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
-
1 mM Co2+, pH 8.0
0.016
-
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide
-
without Co2+, pH 8.0
-
0.021
-
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide
-
pH 7.8, 37C
-
0.023
-
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide
-
1 mM Co2+, pH 8.0
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.52
-
angiotensin I
-
pH 8.6, 30C
2.94
-
angiotensin I
-
pH 8.6, 30C
0.53
-
angiotensin II
-
pH 8.6, 30C
6.08
-
angiotensin II
-
pH 8.6, 30C
0.0073
-
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
-
recombinant enzyme labeled with L-difluoromethionine, pH 7.8
0.01
-
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
-
recombinant enzyme, pH 7.8
0.026
-
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
-
native enzyme, pH 7.8
1.3
-
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
3.8
-
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
20.67
-
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
9.5
-
o-aminobenzoyl-KGRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
32.5
-
o-aminobenzoyl-KHRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
44.2
-
o-aminobenzoyl-KLFFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.57
-
o-aminobenzoyl-KLRDSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.26
-
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
52.17
-
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.3
-
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
35.07
-
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
6.7
-
o-aminobenzoyl-KLWFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
28.19
-
o-aminobenzoyl-KNRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
40.41
-
o-aminobenzoyl-KQRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.52
-
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
14.43
-
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.038
-
peptide 6A
-
pH 8.6, 30C
-
33
-
substance P 1-7
-
pH 8.6, 30C
56
-
substance P 1-9
-
pH 8.6, 30C
0.08
-
substance P 7-11
-
pH 8.6, 30C
0.02
-
substance P 8-11
-
pH 8.6, 30C
160
-
substance P(free acid)
-
pH 8.6, 30C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00217
-
L3D SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000903
-
L3DSmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000791
-
L3F SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.00107
-
L3G SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000723
-
L3I SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.00184
-
L3K SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000958
-
L3P SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000713
-
SmaPI
-
pH 7.0, 25C, wild-type inhibitor
-
0.000728
-
SmaPIAddA
-
pH 7.0, 25C, mutant inhibitor
-
0.000725
-
SmaPIDelG1
-
pH 7.0, 25C, mutant inhibitor
-
0.00274
-
SmaPIDelG1-L3
-
pH 7.0, 25C, mutant inhibitor
-
0.000736
-
SmaPIDelG1-S2
-
pH 7.0, 25C, mutant inhibitor
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.98
-
-
7-amino-4-methyl-coumarin, 37C, pH 8.0
additional information
-
-
-
additional information
-
-
-
additional information
-
-
113 U/mg, one unit gives an increase of 0.01 absorbance at 366 nm, excess of azocasein in 20 mM Tris, 1 mM CaCl2, pH 8
additional information
-
-
enzyme activity in cell cultures grown at different culture conditions, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7.5
-
azocasein as substrate
5.5
-
-
with substrate t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide in absence and presence of Co2+
6
7
-
two optima: 6-7 and 8-10, strain SF 178
7
9
-
egg white albumin, hemoglobin as substrates
7
-
-
benzyloxycarbonyl-Phe-Ala-Ala or benzyloxycarbonyl-Ala-Phe-Gly-Ala as substrate
7
-
-
2 optima: 7 and 9, strain SH 186
8
10
-
two optima: 6-7 and 8-10, strain SF 178
8
9
-
casein as substrate
9
-
-
2 optima: 7 and 9, strain SH 186
additional information
-
-
pI: 4
additional information
-
-
pI: 5.2
additional information
-
-
pI: 5.3-5.4
additional information
-
-
pI: 8.2
additional information
-
-
pI: 4
additional information
-
-
pI: 5.4 and 5.5 (microheterogeneity in isoelectric focusing)
additional information
-
-
pI: 5.25 (calculated value)
additional information
-
-
alkaline pH
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
10
-
about half-maximal activity at pH 6 and about 80% of maximal activity at pH 10, casein as substrate, about 75% of maximal activity at pH 6 and about 60% of maximal activity at pH 10, egg white albumin as substrate
6
8
-
in absence and presence of Co2+
6.5
10
-
about half-maximal activity at pH 6.5 and about 65% of maximal activity at pH 10, hemoglobin as substrate
7.2
10.8
-
about half-maximal activity at pH 7.2 and 10.8
7.5
10.6
-
-
8
9
-
with substrate t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide in the presence of Co2+
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
-
highest acitivity after 4 days of culture
25
-
-
at pH 10, in sodium carbonate buffer
30
-
-
azocasein as substrate
30
-
-
assay at
40
-
-
at pH 8, in phosphate buffer
additional information
-
-
assay carried out at room temperature
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42
62
-
about half-maximal activity at 42C and 62C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
Q3YAW3
isoelectric focusing
8.5
-
-
isoelectric focusing
8.7
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
optimization of protease production, optimal at pH 8.0, 27C, with casein
Manually annotated by BRENDA team
-
optimization of cell culture medium ingredients for protease production, and of conditions: optimal at pH 8.0-9.0, 40C, 0.2-0.4% Na2CO3, 0.1% phosphate, and under static conditions without agitating, overview
Manually annotated by BRENDA team
-
optimization of fermentation production of a solvent stable thermoalkaline protease by a psychrotrophic Pseudomonas putida isolate, overview. Optimized to 1.0% glucose w/v, 2.0% gelatin, 0.5% yeast extract, and 0.01% w/v Mg2+ at pH 9.0, 25C and 200 rpm, agitation and aeration processes are important variables, detailed overview
Manually annotated by BRENDA team
Pseudomonas aeruginosa MTCC 7926
-
optimization of cell culture medium ingredients for protease production, and of conditions: optimal at pH 8.0-9.0, 40C, 0.2-0.4% Na2CO3, 0.1% phosphate, and under static conditions without agitating, overview
-
Manually annotated by BRENDA team
Pseudomonas putida SKG-1
-
optimization of fermentation production of a solvent stable thermoalkaline protease by a psychrotrophic Pseudomonas putida isolate, overview. Optimized to 1.0% glucose w/v, 2.0% gelatin, 0.5% yeast extract, and 0.01% w/v Mg2+ at pH 9.0, 25C and 200 rpm, agitation and aeration processes are important variables, detailed overview
-
Manually annotated by BRENDA team
-
recombinant enzyme of Serratia piscatrum expressed in Serratia marcescens
Manually annotated by BRENDA team
Serratia marcescens BG
-
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme from Serratia sp., expressed in Escherichia coli
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
-
the enzyme is secreted
-
Manually annotated by BRENDA team
Erwinia chrysanthemi B374
-
-
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa MTCC 7926
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PA, Pseudomonas fluorescens KT1
-
-
-
-
Manually annotated by BRENDA team
Pseudomonas putida SKG-1
-
the enzyme is secreted
-
-
Manually annotated by BRENDA team
Pseudomonas sp. TAC-II-18, Serratia marcescens BG
-
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Serratia marcescens (strain ATCC 21074 / E-15)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
44000
-
-
Serratia marcescens, gel filtration
45000
-
-
Escherichia freundii, gel filtration
45400
-
-
Escherichia freundii, minimum MW calculated on the basis of zinc content
45800
-
-
Escherichia freundii, sedimentation equilibrium studies
46000
-
-
gel filtration
47000
-
-
SDS-PAGE
48400
-
-
Pseudomonas aeruginosa, sedimentation velocity centrifugation
48690
-
-
calculated; electrospray mass spectrometry
48730
-
-
electrospray mass spectrometry
48770
-
-
electrospray mass spectrometry
49000
-
D0VMS8
SDS-PAGE
49500
-
-
Pseudomonas aeruginosa, deduced from nucleotide sequence
49500
-
-
commercial preparation, SDS-PAGE
50000
-
-
Serratia marcescens, SDS-PAGE
50000
-
-
Erwinia chrysanthemi, wild-type enzyme or recombinant protease C, SDS-PAGE
50000
-
-
SDS-PAGE
50600
-
-
Serratia piscatrum, deduced from nucleotide sequence
50630
-
-
Serratia piscatrum, deduced from nucleotide sequence
51100
-
-
Erwinia chrysanthemi, recombinant protease C, calculated from nucleotide sequence
51900
-
-
Serratia marcescens, sedimentation equilibrium centrifugation
56000
-
-
Serratia marcescens, strain kums, two enzymes: MW 56000 and MW 60000
57000
-
-
SDS-PAGE
57000
-
-
estimated
60000
-
-
Serratia marcescens, two enzymes: MW 56000 and MW 60000
additional information
-
-
amino acid composition
additional information
-
-
amino acid composition
additional information
-
-
primary structure of Serratia sp., Erwinia chrysanthemi and Pseudomonas aeruginosa enzyme, tertiary structure of Serratia sp. and Pseudomonas aeruginosa enzyme
additional information
-
-
amino acid sequences
additional information
-
-
amino acid composition
additional information
-
-
amino acid sequence alignment
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 50000, Erwinia chrysanthemi, wild-type enzyme or recombinant protease C, SDS-PAGE, x * 50000-52500, Erwinia chrysanthemi, 3 recombinant proteases A-C, SDS-PAGE
?
-
x * 49500, full length mature enzyme, mass spectrometry
?
-
x * 51500, SDS-PAGE
?
-
x * 85000, SDS-PAGE
?
Q3YAW3
x * 45000, SDS-PAGE
monomer
-
1 * 51000, Escherichia freundii, SDS-PAGE
monomer
-
1 * 52500, Serratia marcescens, SDS-PAGE
monomer
-
1 * 47500, Serratia marcescens, SDS-PAGE
monomer
-
1 * 50000, Serratia marcescens, SDS-PAGE
monomer
-
1 * 54400, Serratia marcescens, SDS-PAGE
monomer
-
1 * 52000, Serratia marcescens, SDS-PAGE
monomer
Pseudomonas fluorescens KT1
-
-
-
monomer
Serratia marcescens BG
-
1 * 52500, Serratia marcescens, SDS-PAGE
-
additional information
-
enzyme activity is resistant to treatment by pepsin, trypsin and chymotrypsin
additional information
Q3YAW3
the N-terminal amino acid sequence shares 100% identity with the domain 14-34 of extracellular alkaline endoprotease sequences called AprX
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
0.69 mol sugar/mol enzyme
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
complex with cognate inhibitor AprIn, crystals from vapour diffusion method with sitting or hanging drops, complex with recombinant inhibitor, structure solution using APR coordinates as a search model
Q03023
two-domain protein with a calcium binding parallel beta roll motif, 1.64A by multiple isomorphous replacement and non-crystallographic symmetry averaging between different crystal forms, crystallization at 4 and 18 C, spanning pH range of 3-9
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
4
-
inactivation
3.5
11
-
stable in this range
5
10
-
3 h, stable at 30C
5
10
-
1 h, at room temperature
5
9
-
10 min, fairly stable at 30C
6
8.5
-
1 h, stable at 30C
6
9
-
room temperature
6.5
-
-
10 min, stable below 45C
7
10
-
stable within this range, maximum stability at pH 10.0 after 2 h
7.5
-
-
15 min, stable at 25-45C
10
-
-
10 min, stable below 25C, inactivation at 35C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
45
-
stable within this range, sharp decrease in stability above
20
-
-
3 h, stable at pH 5-10
20
-
-
1 h, pH 5-10
25
40
-
stable at 25C, but declining activity above 40C
25
45
-
15 min, stable at pH 7.5
25
-
-
and below, 10 min stable at pH 10
30
-
-
1 h, stable at pH 6-8.5
30
-
-
pH 5-9, fairly stable
35
-
-
10 min, pH 10, inactivation
45
-
-
and below, 10 min stable at pH 6.5
45
-
-
50% activity after 20 min
50
-
-
below, 10 min, fairly stable at neutral pH-values
55
-
-
10 min, inactivation, CaCl2 does not stabilize
55
-
-
10 min, partly unstable in distilled water, 100 mM phosphate or 10 mM CaCl2 stabilizes
55
-
-
the selective substitution of Ca2+ for functional zinc does not change stability below 55C
60
-
-
15 min, inactivation
60
-
-
inactivation in 20 mM Tris-HCl buffer, pH 7, stable in the presence of tetraethylenepentamine or CaCl2
63
-
-
10 min, inactivation in the presence of stabilizing agents
additional information
-
-
thermal unfolding profiles
additional information
-
-
inhibitory activity to IFN-gamma is heat sensitive
additional information
-
-
comparison of full-length and truncation mutants, DELTAN-AP shows increased thermal sensitivity compared with the wild-type enzyme. At 42C, protease activity decreases by 50%, and at 55C, protease activity decreases by 90% when compared with the full-length AP in 2 mM Ca2+
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Unstable in the presence of 10 mM CaCl2
-
sensitive to trypsin degradation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, pH 4.5-11.5, 1 day
-
-70C, lyophilized Serratia marcescens enzyme, several months
-
4C, 5 mg enzyme/ml deionized glass-distilled water, 1 day
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified to homogeneity by precipitation with ammonium sulfate (65%). After dialysis, the crude enzyme is further purified by FPLC using Superdex 200 column
D0VMS8
ammonium sulfate precipitation, gel filtration, chromatography
-
gel filtration
-
metal chelate chromatography with copper and hydrophobic interaction chromatography, dialysis
-
precipitation with ammonium sulfate and acetone, gel filtration and chromatography
-
recombinant refolded His-tagged wild-type and mutant AP proteins and domains from inclusion bodies by nickel affinity chromatography
-
dialysis against 10 mM N-methyldiethanolamine, DE-52 gel filtration, chelating Sepharose 6B gel filtration, dialysis against 0.02M triethanolamine-HCl buffer
-
2 immunologically not related enzymes: MW 56000 and MW 60000
-
to near homogeneity
-
purification from culture fluid
-
native enzyme by two different steps of anion exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Erwinia chrysanthemi; expressed in Escherichia coli
-
expressed in Escherichia coli
-
expression in Escherichia coli C600, synthesized as a zymogen ProA
-
recombinantly expressed in Escherichia coli
D0VMS8
recombinantly expressed in Escherichia coli
-
apr gene requires the lasR gene for transcription
-
expression of wild-type and mutant AP proteins and domains at high levels in inclusion bodies
-
expressed in Escherichia coli; expressed in Serratia marcescens strain pSP2; Serratia marcescens (wild-type)
-
expressed in Escherichia coli; expressed in Serratia marcescens; Serratia piscatrum
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
M226A
-
using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants
M226A/E189A
-
introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
M226H
-
mutant could not be purified, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants
M226H/E189A
-
introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
M226I
-
M226I possesses 50% of wild-type activity, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants
M226I/E189A
-
introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
M226L
-
M226L possesses 85% of wild-type activity, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants
M226L/E189A
-
introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
M226N
-
mutant could not be purified
M226N/E189A
-
introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
additional information
-
enzyme form bearing residues Leu-Lys at the N-terminus, in the absence of calcium far more efficient degradation of interleukins IL-6 and IL-8 than wild-type
additional information
-
recombinant protein labeled with L-difluoromethionine in invariant position of M214 shows little effect on protein structure or function
additional information
-
generation of a series of full-length and truncation mutants for structural and functional studies, overview. DELTAN-AP shows increased thermal sensitivity compared with the wild-type enzyme. At 42C, protease activity decreases by 50%, and at 55C, protease activity decreases by 90% when compared with the full-length AP in 2 mM Ca2+
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged wild-type and mutant AP proteins and domains under denaturing conditions are refolded from inclusion bodies using either urea for RTX, or guanidine HCl for full-length and truncation mutants
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
enzyme is one of the virulence factors of the opportunistic pathogen which causes severe and lethal infections in patients with underlying diseases, implicated in the hydrolysis of many biologically active proteins
medicine
-
inhibition of tumor necrosis factor-alpha-induced RANTES secretion
medicine
-
anti-coagulant activity in human plasma
medicine
-
inhibits IFN-gamma antiviral and immunomodulatory activity