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125I-insulin + H2O
?
-
-
-
-
?
2-Aminobenzoyl-Gly-Phe-Arg-Leu-Leu 4-nitrobenzyl amide + H2O
?
2-Aminobenzoyl-Gly-Phe-Arg-Xaa 4-nitrobenzyl amide + H2O
?
2-aminobenzoyl-KLCSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLC + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-KLKSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLK + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-KLR + SSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
-
-
-
?
Abz-LGMISLMKRPPGFSPFRSSRI-NH2 + H2O
?
-
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
?
-
-
-
-
?
Aminoethylated lysozyme + H2O
?
-
-
-
-
?
angiotensin I + H2O
DRVY + IHPFLHL + DRVYI + HPFHL
-
-
-
?
angiotensin II + H2O
?
-
-
-
?
Azocoll + H2O
?
-
-
-
-
?
Benzyloxycarbonyl tripeptides + H2O
?
-
overview
-
-
?
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
?
Benzyloxycarbonyl-Ala-Gly-Gly-Leu + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Gly-Gly-Leu-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Gly-Gly-Leu-Xaa + H2O
?
-
a hydrophobic or bulky residue at P3' results in marked increase in hydrolysis
-
-
?
benzyloxycarbonyl-Ala-Gly-Leu-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala-Leu-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Phe-Gly-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Phe-Leu-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-D-Ala-Gly-Leu-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Ala-Ala + H2O
?
Benzyloxycarbonyl-Gly-Gly-Gly-Leu + H2O
?
-
poor substrate
-
-
?
Benzyloxycarbonyl-Gly-Gly-Leu amide + H2O
?
-
poor substrate
-
-
?
benzyloxycarbonyl-Gly-Gly-Leu-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Leu-Gly-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Gly-Gly + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Gly-Gly-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Gly-Gly-Xaa + H2O
?
-
a hydrophobic or bulky residue at P3' results in marked increase in hydrolysis
-
-
?
Benzyloxycarbonyl-Gly-Leu-Leu + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Phe + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Xaa + H2O
?
-
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
?
-
-
-
-
?
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Phe-Ala-Ala + H2O
?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Phe-Gly-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Gly-Leu-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
?
-
best substrate
-
-
?
benzyloxycarbonyl-Phe-Phe-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Phe-Xaa-Ala + H2O
Benzyloxycarbonyl-Phe + Xaa-Ala
-
susceptibility to the enzyme is Xaa-dependent, in decreasing order of efficiency: Ala, Phe, Leu, Trp or Ser or Gly
-
?
benzyloxycarbonyl-Val-Ala-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Xaa-Ala-Ala + H2O
Benzyloxycarbonyl-Xaa + Ala-Ala
-
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
?
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
-
-
?
Benzyloxycarbonyl-Xaa-Leu-Ala + H2O
Benzyloxycarbonyl-Xaa + Leu-Ala
-
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
?
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
-
-
?
Benzyloxycarbonyl-Xaa-Phe-Leu-Ala + H2O
?
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
-
-
?
beta-1,3 glucan recognition protein 2 + H2O
?
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
Bovine serum albumin + H2O
?
C-terminal octapeptide of glucagon + H2O
?
-
cleavage sites
-
-
?
Carboxymethyl-beta-insulin + H2O
?
-
cleavage sites
-
-
?
D-Ala-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Dabcyl-Glu-Val-Tyr-Ala-Val-Glu-Ser-EDANS + H2O
?
-
-
-
-
?
DL-Val-Leu-Arg-4-nitroanilide + H2O
?
-
-
-
-
?
Egg albumin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
furylacryloyl-Ala-Leu-Val-Tyr + H2O
?
-
-
-
-
?
furylacryloyl-Leu-Gly-Pro-Ala + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
cleavage sites
-
-
?
Glycoprotein G + H2O
?
-
i.e. thrombin-sensitive protein, thrombospondin, MW 190000
-
-
?
hemocyte aggregation inhibitor protein (HAIP) + H2O
?
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
hide powder azure + H2O
?
-
-
-
-
?
His-Ser-4-methoxy-2-naphthylamide + H2O
?
-
-
-
-
?
His-Ser-4-methoxy-2-naphthylamide + H2O
His-Ser + 4-methoxy-2-naphthylamine
-
-
-
-
?
Human alpha1-proteinase inhibitor + H2O
?
-
MW 52000
-
-
?
human complement component C1 + H2O
?
-
-
-
-
?
human complement component C2 + H2O
?
-
-
-
-
?
Human platelet surface glycoprotein Ib + H2O
?
-
-
-
-
?
Immunoglobulin A1 + H2O
?
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
?
Immunoglobulin A2 + H2O
?
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
?
Immunoglobulin G1 + H2O
?
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
?
Immunoglobulin G2 + H2O
?
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
?
Immunoglobulin G3 + H2O
?
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
?
Immunoglobulin G4 + H2O
?
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
?
including serpin-1I + H2O
?
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
interleukin-6 + H2O
?
-
complete digestion
-
-
?
interleukin-8 + H2O
?
-
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
-
-
-
?
L-Ala-L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala + L-Ala-L-Ala-L-Ala
-
-
-
?
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
-
-
-
?
L-Ala-oligopeptides + H2O
?
-
proteolytic activity increases drastically with increasing chain length from tetramer to hexamer, no substrate: dipeptide or tripeptide
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
N-alpha-benzoyl-DL-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
artificial substrate BAPNA
-
?
N-benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-terminal hexapeptide of glucagon + H2O
?
-
cleavage sites
-
-
?
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KDR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KDR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KFR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KGRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KGR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KHRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KHR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLAFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLA + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLDFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLD + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLEFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLE + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLFFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLF + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLGFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLG + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLHFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLH + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLKFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLK + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLLFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLL + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLMFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLM + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLNFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLN + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLPFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLP + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLQFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLQ + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLRASKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + ASKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLRDSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + DSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLRLSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + LSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + NSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLRRSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + RSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + SSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-KLSFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLS + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLTFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLT + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLWFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLW + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KLYFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLY + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KNRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KNR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KQRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KQR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KRRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KRR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KSR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
peptide 6A + H2O
?
-
-
-
?
Phe-Gly-Leu-Ala + H2O
?
-
-
-
-
?
Plasma fibronectin + H2O
?
Pro-Phe-Arg 4-methylcoumarin 7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
Pro-Phe-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Ribonuclease + H2O
?
-
-
-
-
?
scolexins A + H2O
?
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
scolexins B + H2O
?
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
serine proteinase homolog 3 + H2O
?
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
serpin-1 variants + H2O
?
-
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
-
-
-
?
substance P 1-7 + H2O
?
-
-
-
?
substance P 1-9 + H2O
RPKP + QQFFG + RPKQQ + FFG
-
-
-
?
substance P 7-11 + H2O
?
-
-
-
?
substance P 8-11 + H2O
?
-
-
-
?
substance P(free acid) + H2O
RPKPQQFFG + LM + RPKPQQFF + GLM + RPKQQF + FGLM
-
-
-
?
Suc-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Succ-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
?
-
-
-
-
?
Succ-Ala-Ala-Pro-Xaa-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
t-butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
t-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Gly-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Gly-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
t-butyloxycarbonyl-Met-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
?
t-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Tryptic insulin heptapeptide + H2O
?
-
cleavage sites
-
-
?
additional information
?
-
2-Aminobenzoyl-Gly-Phe-Arg-Leu-Leu 4-nitrobenzyl amide + H2O
?
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
-
?
2-Aminobenzoyl-Gly-Phe-Arg-Leu-Leu 4-nitrobenzyl amide + H2O
?
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
-
?
2-Aminobenzoyl-Gly-Phe-Arg-Xaa 4-nitrobenzyl amide + H2O
?
-
Xaa is Gly, Ala, Val, Leu or Phe, Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
-
?
2-Aminobenzoyl-Gly-Phe-Arg-Xaa 4-nitrobenzyl amide + H2O
?
-
Xaa is Gly, Ala, Val, Leu or Phe, Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
?
-
cleavage site: AlaÄ+ÄAla-Ala
-
-
?
Benzyloxycarbonyl-Gly-Ala-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Gly-Ala-Ala + H2O
?
-
cleavage site: Gly-Ala
-
-
?
Benzyloxycarbonyl-Phe-Ala-Ala + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Phe-Ala-Ala + H2O
?
-
cleavage site: Phe-Ala
-
-
?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
the enzyme cleaves 61 unique sequence pairs of bovine serum albumin involving all 20 amino acids
-
-
?
Bovine serum albumin + H2O
?
-
the enzyme cleaves 61 unique sequence pairs of bovine serum albumin involving all 20 amino acids
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
Km of 1.261 mg/ml for casein
-
-
?
casein + H2O
?
-
Km of 1.261 mg/ml for casein
-
-
?
Fibrin + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
the enzyme hydrolyzes the Aalpha chain in 1 min, the Bbeta chain in 5 min, and the gamma chain in more than 1 h
-
-
?
Fibrinogen + H2O
?
-
the enzyme hydrolyzes the Aalpha chain in 1 min, the Bbeta chain in 5 min, and the gamma chain in more than 1 h
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage specificity of Pseudomonas aeruginosa, Pseudomonas fragi, Serratia sp. and Proteus mirabilis enzyme
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage sites
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage specificity of Pseudomonas aeruginosa, Pseudomonas fragi, Serratia sp. and Proteus mirabilis enzyme
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage specificity of Pseudomonas aeruginosa, Pseudomonas fragi, Serratia sp. and Proteus mirabilis enzyme
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage specificity of Pseudomonas aeruginosa, Pseudomonas fragi, Serratia sp. and Proteus mirabilis enzyme
-
-
?
Plasma fibronectin + H2O
?
-
Serratia marcescens MW 52000 enzyme, cleavage sites
-
-
?
Plasma fibronectin + H2O
?
-
from pig
-
-
?
Pro-Phe-Arg 4-methylcoumarin 7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
?
Pro-Phe-Arg 4-methylcoumarin 7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
?
t-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
additional information
?
-
-
no substrate: casein, bovine serum albumin, lysozyme, lactalbumin, lactoglobulin and thyroglobulin
-
-
?
additional information
?
-
-
elastin
-
-
?
additional information
?
-
-
elastin
-
-
?
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
?
-
-
collagen
-
-
?
additional information
?
-
-
tetrapeptides are poorer substrates than benzyloxycarbonyl tetrapeptides
-
-
?
additional information
?
-
-
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
?
-
-
inhibits cytokine-induced signaling in A549 pulmonary epithelial cells
-
-
?
additional information
?
-
-
inhibits IFN-gamma antiviral and immunomodulatory activity
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no substrates are small peptides
-
-
?
additional information
?
-
-
human platelet surface glycoprotein V
-
-
?
additional information
?
-
-
minimum peptide size: hexapeptide
-
-
?
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
?
-
-
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
?
-
-
the enzyme does not degrade urokinase, streptokinase, and tissue plasminogen activator
-
-
?
additional information
?
-
-
the enzyme does not degrade urokinase, streptokinase, and tissue plasminogen activator
-
-
?
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
?
-
-
enzyme prefers Arg in subsite P1
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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8-hydroxyquinoline
-
0.1 mM at pH 10, 5 mM at pH 7
Ac-Val-Leu-Lys-4-mercaptoanilide
-
pH 7.8, 37°C, 0.2 mM 69% inhibition, 0.3 mM complete inhibition
alkaline protease inhibitor
-
-
-
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
-
captopril
-
0.001 mM, 82% residual activity
Cd2+
-
at pH 10, not at pH 7
chymostatin
-
0.1 mM, 18% inhibition at pH 8.0
diisopropylfluorophosphate
-
1 mM, weak inhibition at pH 5.5 and pH 8.0 with and without addition of 1 mM Co2+
dithiothreitol
5 mM, 5% residual activity
DTNB
-
reversible, synergism with pyridoxal 5'-phosphate or phenylglyoxal
E-64
-
0.0056 mM, 91% residual activity
Elastatinal
-
0.1 mM, 11% inhibition at pH 8.0 and without 1 mM Co2+ addition
Guanidine-HCl
-
enhanced by EDTA
HgCl2
-
complete inhibition
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
-
Mg2+
-
10 mM, 93% residual activity
N-tosyl-L-phenylalanine chloromethyl ketone
-
0.1 mM, 18% inhibition at pH 8.0
Ni2+
-
at pH 10, not at pH 7
p-hydroxymercuribenzoate
-
0.002 mM, 71% residual activity
Periplasmic endogen inhibitor peptide of Serratia marcescens
-
Phenanthroline
-
strong inhibition with 4.65% residual activity at 10 mM
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
phenylmethylsulfonyl fluoride
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+
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
-
Sn2+
-
59.07% residual activity at 5 mM
Soybean trypsin inhibitor
-
0.01 mM, 9% inhibition at pH 5.5
-
Tetraethylenepentamine
-
zinc-specific chelator
Tetramethylenepentamine
-
Serratia marcescens
1,10-phenanthroline
-
1 mM
1,10-phenanthroline
-
complete inhibition
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, 37°C, 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
-
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
-
activity can be restored with the addition of Mn2+, Cu2+ and Co2+ up to 90-200% of its original value, while Zn2+ is inefficient
2,2'-bipyridyl
-
5 mM
Ca2+
-
inhibitory above 0.1 mM
Ca2+
-
10 mM, 90% residual activity
Co2+
-
inhibitory above 5 mM
Cu2+
-
-
Cu2+
-
10 mM, 58% residual activity
Cysteine hydrochloride
-
not Serratia marcescens enzyme
Cysteine hydrochloride
-
not Serratia marcescens enzyme
Cysteine hydrochloride
-
not Serratia marcescens enzyme
Cysteine hydrochloride
-
not Serratia marcescens enzyme
Cysteine hydrochloride
-
not Serratia marcescens enzyme
Cysteine hydrochloride
-
weak
Cysteine hydrochloride
-
not Serratia marcescens enzyme
Cysteine hydrochloride
-
not Serratia marcescens enzyme
DTT
-
weak, Serratia marcescens
DTT
-
weak, Serratia marcescens
DTT
-
weak, Serratia marcescens
DTT
-
weak, Serratia marcescens
DTT
-
weak, Serratia marcescens
DTT
-
weak, Serratia marcescens
DTT
-
weak, Serratia marcescens
EDTA
-
0.1 mM at pH 10, 5 mM at pH 7
EDTA
-
complete inhibition
EDTA
-
Co2+; Mn2+; strong, 5 mM
EDTA
-
30 min, room temperature, pH 7.5, complete inhibition in a concentration range below 1 mM
EDTA
-
1 mmol, pH 8.1, no inactivation by 0.1 M EDTA
EDTA
-
10 mM, almost complete inactivation at pH 5.5 and pH 8.0 with and without addition of 1 mM Co2+
EDTA
5 mM, 23% residual activity
EDTA
-
10 mM, pH 8, strong inhibition
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
-
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
-
strong inhibition with 2.6% residual activity at 10 mM, enzyme activity can be regained by the addition of Co2+, Cu2+, Fe2+, Mg2+, and Zn2+ ions after chelation of ions with EDTA
EDTA
-
10 mM, 42% residual activity
EDTA
-
10 mM, 3% residual activity
EDTA
-
inhibits the activity only partially even either after long incubation or in excess amount
EGTA
-
complete inhibition
EGTA
5 mM, 33% residual activity
EGTA
-
10 mM, pH 8, strong inhibition
Fe2+
-
strong
Fe2+
-
68.66% residual activity at 5 mM
Hg2+
-
-
Hg2+
-
10 mM, 5.5% residual activity
iodoacetamide
-
0.1 mM, 72% residual activity
iodoacetamide
-
10 mM, 96% residual activity
KCN
-
at pH 10, no inhibition at pH 7.5
KMnO4
-
-
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
leupeptin
-
weak, only Serratia marcescens MW 56000 enzyme
N-bromosuccinimide
-
strong
N-bromosuccinimide
-
strong
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
N-ethylmaleimide
-
0.1 mM, 14% inhibition at pH 8.0 and 1 mM Co2+ addition
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
NaCl
1 M, 56% residual activity
NaCl
-
inhibitory effect depends on substrate
o-phenanthroline
0.5 mM, 10% residual activity
o-phenanthroline
-
2 mM, no residual activity
Pb2+
-
-
Periplasmic endogen inhibitor peptide of Serratia marcescens
-
-
-
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
-
phenylmethylsulfonyl fluoride
-
0.5 mM, 81% residual activity
phenylmethylsulfonyl fluoride
-
10 mM, 97% residual activity
PMSF
-
not
PMSF
-
weak, Serratia marcescens
Sodium thioglycolate
-
1 mM, at pH 10, no inhibition at pH 7.5
Sodium thioglycolate
-
not
Sodium thioglycolate
-
weak
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
additional information
-
2-mercaptoethanol; diisopropyl phosphofluoridate; iodine, ovomucoid; monoiodoacetic acid; PCMB; potato inhibitor; soybean trypsin inhibitor
-
additional information
-
-
-
additional information
-
not inhibitory: PMSF, E-64 and pepstatin
-
additional information
-
diisopropyl phosphofluoridate; PCMB; potato inhibitor; soybean trypsin inhibitor; tosyl-L-Phe chloromethyl ketone or tosyl-L-Lys chloromethyl ketone
-
additional information
-
-
-
additional information
-
citrate, NaF, oxalate; diisopropyl phosphofluoridate; monoiodoacetic acid; PCMB; potato inhibitor; soybean trypsin inhibitor
-
additional information
-
not inhibited by chloromethylketone or hydroxamate
-
additional information
-
not inhibited by dithiothreitol, PMSF and DFP
-
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
-
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
-
IAA; PCMB
-
additional information
-
PCMB
-
additional information
-
not inhibited by iodoacetic acid and phenylmethylsulfonyl fluoride
-
additional information
-
not inhibitory: pepstatin (0.0015 mM), tosyllysyl chloromethyl ketone (0.05 mM), tosylphenylalanyl chloromethyl ketone (0.05 mM), tiorphan (0.004 mM), Triton X-100 and Tween up to 0.1% (v/v)
-
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Adenocarcinoma
TLR4-mediated immunomodulatory properties of the bacterial metalloprotease arazyme in preclinical tumor models.
Anaphylaxis
Mast cell recovery following chronic treatment with compound 48/80.
Atherosclerosis
A disintegrin and metalloproteinase with thrombospondin motif 1 (ADAMTS1) expression increases in acute aortic dissection.
Breast Neoplasms
ARA-linker-TGF?L3: a novel chimera protein to target breast cancer cells.
Carcinoma
Serratia marcescens serralysin induces inflammatory responses through protease-activated receptor 2.
Carcinoma, Squamous Cell
Serratia marcescens serralysin induces inflammatory responses through protease-activated receptor 2.
Colorectal Neoplasms
Purification and study of anti-cancer effects of Serratia marcescens serralysin.
Dermatitis, Atopic
Inhibitory effect of arazyme on the development of atopic dermatitis-like lesions in BALB/c and Nc/Nga mice.
Fatty Liver
Arazyme Suppresses Hepatic Steatosis and Steatohepatitis in Diet-Induced Non-Alcoholic Fatty Liver Disease-Like Mouse Model.
Glioma
HIV-1 glycoprotein 120 induces the MMP-9 cytopathogenic factor production that is abolished by inhibition of the p38 mitogen-activated protein kinase signaling pathway.
Hyperglycemia
Combination Treatment of Arazyme and Soy Leaf Extract Attenuates Hyperglycemia and Hepatic Steatosis in High-Fat Diet-Fed C57BL/6J Mice.
Hypertension
Proteolytic activities in hypertensive cardiomyopathy of rats.
Infections
A proteolytic enzyme secreted by Proteus mirabilis degrades immunoglobulins of the immunoglobulin A1 (IgA1), IgA2, and IgG isotypes.
Infections
Calcium-induced folding and stabilization of the Pseudomonas aeruginosa alkaline protease.
Infections
Interdomain Contacts and the Stability of Serralysin Protease from Serratia marcescens.
Infections
Quantitation and enzymatic activity of the alkaline protease from Pseudomonas aeruginosa in culture supernatants from clinical strains.
Infections
Rapid and efficient one-step purification of a serralysin family protease by using a p-aminobenzamidine-modified affinity medium.
Infections
Serratia marcescens serralysin induces inflammatory responses through protease-activated receptor 2.
Kuru
A prion protein missense variant is integrated in kuru plaque cores in patients with Gerstmann-Sträussler syndrome.
Leiomyoma
Protease activity in fibromyoma and normal human myometrium.
Leishmaniasis, Visceral
Evaluation of Cysteine Protease C of Leishmania donovani in comparison with Glycoprotein 63 and Elongation Factor-1? for diagnosis of human visceral leishmaniasis and for post-treatment follow-up response.
Lung Neoplasms
Expression of chicken ovalbumin upstream promoter-transcription factor II enhances invasiveness of human lung carcinoma cells.
Malaria
Bayesian analysis of new and old malaria parasite DNA sequence data demonstrates the need for more phylogenetic signal to clarify the descent of Plasmodium falciparum.
Malaria
Malaria parasite sequences from chimpanzee support the co-speciation hypothesis for the origin of virulent human malaria (Plasmodium falciparum).
Melanoma
A natural bacterial-derived product, the metalloprotease arazyme, inhibits metastatic murine melanoma by inducing MMP-8 cross-reactive antibodies.
Melanoma
B.C.G. plus protease I in malignant melanoma.
Melanoma
TLR4-mediated immunomodulatory properties of the bacterial metalloprotease arazyme in preclinical tumor models.
Mouth Diseases
In vitro and in vivo studies of the Yrp1 protease from Yersinia ruckeri and its role in protective immunity against enteric red mouth disease of salmonids.
Myocardial Infarction
Influence of apelin-12 on troponin levels and the rate of MACE in STEMI patients.
Neoplasm Metastasis
ARA-linker-TGF?L3: a novel chimera protein to target breast cancer cells.
Neoplasm Metastasis
EMMPRIN and ADAM12 in prostate cancer: preliminary results of a prospective study.
Neoplasm Metastasis
Hepatitis C virus core protein promotes the migration and invasion of hepatocyte via activating transcription of extracellular matrix metalloproteinase inducer.
Neoplasm Metastasis
TLR4-mediated immunomodulatory properties of the bacterial metalloprotease arazyme in preclinical tumor models.
Neoplasms
A natural bacterial-derived product, the metalloprotease arazyme, inhibits metastatic murine melanoma by inducing MMP-8 cross-reactive antibodies.
Neoplasms
A Novel Peptide to Treat Oral Mucositis Blocks Endothelial and Epithelial Cell Apoptosis.
Neoplasms
Arazyme inhibits cytokine expression and upregulates skin barrier protein expression.
Neoplasms
Arazyme Suppresses Hepatic Steatosis and Steatohepatitis in Diet-Induced Non-Alcoholic Fatty Liver Disease-Like Mouse Model.
Neoplasms
Development of a monoclonal antibody that specifically detects tissue inhibitor of metalloproteinase-4 (TIMP-4) in formalin-fixed, paraffin-embedded human tissues.
Neoplasms
EMMPRIN and ADAM12 in prostate cancer: preliminary results of a prospective study.
Neoplasms
Targeting the EGFR in cancer cells by fusion protein consisting of arazyme and third loop of TGF-alpha: an in silico study.
Neoplasms
The effects of protease I of Aspergillus oryzae (brinase) on membrane permeability and growth of Landschütz ascites tumour cells.
Neoplasms
TLR4-mediated immunomodulatory properties of the bacterial metalloprotease arazyme in preclinical tumor models.
Periodontal Diseases
Platelet activation by Protease I of Porphyromonas gingivalis W83.
Pulmonary Embolism
[Experimental pulmonary embolism in dogs. Local administration of Aspergillus-oryzae protease I]
Sepsis
Efficacies of alkaline protease, elastase and exotoxin A toxoid vaccines against gut-derived Pseudomonas aeruginosa sepsis in mice.
Starvation
Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli.
Stomatitis, Denture
Development of a novel denture care agent with highly active enzyme, arazyme.
Thrombosis
[Experimental study of protease C--proteolytic enzyme of microbial origin]
Urinary Tract Infections
A proteolytic enzyme secreted by Proteus mirabilis degrades immunoglobulins of the immunoglobulin A1 (IgA1), IgA2, and IgG isotypes.
Vascular Diseases
A disintegrin and metalloproteinase with thrombospondin motif 1 (ADAMTS1) expression increases in acute aortic dissection.
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0.012
2-aminobenzoyl-KLCSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 5.5, 55°C
0.013
2-aminobenzoyl-KLKSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 5.5, 55°C
0.0173
2-aminobenzoyl-KLRSSKQ-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 5.5, 55°C
1.2
Ala-Ala-Ala-Ala-Ala
-
-
0.5
Ala-Ala-Ala-Ala-Ala-Ala
-
benzyloxycarbonyl-Phe-L-Ala-Ala
0.144
azocasein
-
pH 5.5, 55°C
-
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 - 0.014
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
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
0.024
casein
-
pH 5.5, 55°C
0.00308
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00096
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.0027
o-aminobenzoyl-KGRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.0007
o-aminobenzoyl-KHRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00087
o-aminobenzoyl-KLAFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.0049
o-aminobenzoyl-KLDFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00783
o-aminobenzoyl-KLEFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.002
o-aminobenzoyl-KLFFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.0026
o-aminobenzoyl-KLGFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00076
o-aminobenzoyl-KLHFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00144
o-aminobenzoyl-KLKFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00087
o-aminobenzoyl-KLLFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00276
o-aminobenzoyl-KLMFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00261
o-aminobenzoyl-KLNFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.0086
o-aminobenzoyl-KLPFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00133
o-aminobenzoyl-KLQFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.0018
o-aminobenzoyl-KLRASKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00582
o-aminobenzoyl-KLRDSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00082
o-aminobenzoyl-KLRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00498
o-aminobenzoyl-KLRLSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00292
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00208
o-aminobenzoyl-KLRRSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00137
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00303
o-aminobenzoyl-KLSFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.0022
o-aminobenzoyl-KLTFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00056
o-aminobenzoyl-KLWFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00021
o-aminobenzoyl-KLYFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00198
o-aminobenzoyl-KNRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00115
o-aminobenzoyl-KQRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00143
o-aminobenzoyl-KRRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.00157
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37°C
0.015 - 0.035
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
0.016 - 0.023
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide
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
-
-
0.4
Benzyloxycarbonyl-Phe-Ala-Ala
-
benzyloxycarbonyl-Phe-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
0.023
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
-
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, 37°C
0.023
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide
-
1 mM Co2+, pH 8.0
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Morihara, K.; Tsuzuki, H.; Oka, T.
On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic peptides
Biochim. Biophys. Acta
309
414-429
1973
Pseudomonas aeruginosa
brenda
Harada, S.; Nagara, A.; Kurisu, G.; Kai, Y.
Crystallization and preliminary X-ray studies of a protease from Pseudomonas aeruginosa
J. Mol. Biol.
230
1315-1316
1993
Pseudomonas aeruginosa
brenda
Miyatake, H.; Hata, Y.; Fujii, T.; Hamada, K.; Morihara, K.; Katsube, Y.
Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding
J. Biochem.
118
474-479
1995
Pseudomonas aeruginosa
brenda
Nakajima, M.; Mizusawa, K.; Yoshida, F.
Purification and properties of an extracellular proteinase of psychrophilic Escherichia freundii
Eur. J. Biochem.
44
87-96
1974
Citrobacter freundii
brenda
Lyerly, D.; Kreger, A.
Purification and characterization of a Serratia marcescens metalloprotease
Infect. Immun.
24
411-421
1979
Serratia marcescens, Serratia marcescens BG
brenda
Decedue, C.J.; Broussard, E.A.; Larson, A.D.; Braymer, H.D.
Purification and characterization of the extracellular proteinase of Serratia marcescens
Biochim. Biophys. Acta
569
293-301
1979
Serratia marcescens
brenda
Virca, G.D.; Lyerly, D.; Kreger, A.; Travis, J.
Inactivation of human plasma alpha 1-proteinase inhibitor by a metalloproteinase from Serratia marcescens
Biochim. Biophys. Acta
704
267-271
1982
Serratia marcescens
brenda
Kim,.K.S.; Kim, T.U.; Kim, I.J.; Byun, S.M.; Shin, Y.C.
Characterization of a metalloprotease inhibitor protein (SmaPI) of Serratia marcescens
Appl. Environ. Microbiol.
61
3035-3041
1995
Serratia marcescens
brenda
Maeda, H.; Morihara, K.
Serralysin and related bacterial proteinases
Methods Enzymol.
248
395-413
1995
Citrobacter freundii, Dickeya chrysanthemi, Proteus mirabilis, Pseudomonas aeruginosa, Pseudomonas fragi, Serratia marcescens, Serratia sp. E-15
brenda
Morihara, K.
Pseudomonas aeruginosa proteinase. I. Purification and general properties
Biochim. Biophys. Acta
73
113-124
1963
Pseudomonas aeruginosa
-
brenda
Inoue, H.; Nakagawa, T.; Morihara, K.
Pseudomonas aeruginosa proteinase. II. Molecular weight and molecular dimension
Biochim. Biophys. Acta
73
125-131
1963
Pseudomonas aeruginosa
brenda
Doerr, M.; Traub, W.H.
Purification and characterization of two Serratia marcescens proteases
Zentralbl. Bakteriol. Mikrobiol. Hyg. A
257
6-19
1984
Serratia marcescens
brenda
McGowan, E.B.; Detwiler, T.C.
Differential effect of Serratia protease on platelet surface glycoproteins Ib and V
Blood
65
1033-1035
1985
Serratia marcescens
brenda
Choi, B.B.; Kim, S.S.
Reversible inactivation of Serratia protease by 5,5'-dithiobis (2-nitrobenzoate)
Han'guk Saenghwa Hak Hoe Chi
19
287-293
1986
Serratia marcescens
-
brenda
Nakahama, K.; Yoshimura, K.; Marumoto, R.; Kikuchi, M.; Lee, I.S.; Hase, T.; Matsubara, H.
Cloning and sequencing of Serratia protease gene
Nucleic Acids Res.
14
5843-5855
1986
Serratia sp. E-15
brenda
Molla, A.; Tanase, S.; Hong, Y.; Maeda, H.
Interdomain cleavage of plasma fibronectin by zinc-metalloproteinase from Serratia marcescens
Biochim. Biophys. Acta
955
77-85
1988
Serratia marcescens
brenda
Dahler, G.S.; Barras, F.; Keen, N.T.
Cloning of genes encoding extracellular metalloproteases from Erwinia chrysanthemi EC16
J. Bacteriol.
172
5803-5815
1990
Dickeya chrysanthemi
brenda
Bode, W.; Gomis-Ruth, F.X.; Stckler, W.
Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the metzincins
FEBS Lett.
331
134-140
1993
Dickeya chrysanthemi, Pseudomonas aeruginosa, Serratia marcescens
brenda
Kim, N.; Kim, S.I.
Metal ion relevance for the stability and activity of a 52-kDa Serratia proteinase
Biosci. Biotechnol. Biochem.
57
29-33
1993
Serratia marcescens
brenda
Bae, K.H.; Kim, I.C.; Kim, K.S.; Shin, Y.C.; Byun, S.M.
The Leu-3 residue of Serratia marcescens metalloprotease inhibitor is important in inhibitory activity and binding with Serratia marcescens metalloprotease
Arch. Biochem. Biophys.
352
37-43
1998
Serratia marcescens
brenda
Louis, D.; Bernillon, J.; Wallach, J.M.
Specificity of Pseudomonas aeruginosa serralysin revisited, using biologically active peptides as substrates
Biochim. Biophys. Acta
1387
378-386
1998
Pseudomonas aeruginosa
brenda
Louis, D.; Bernillon, J.; Wallach, J.M.
Use of a 49-peptide library for a qualitative and quantitative determination of pseudomonal serralysin specificity
Int. J. Biochem. Cell Biol.
31
1435-1441
1999
Pseudomonas aeruginosa
brenda
Krunkosky, T.M.; Maruo, K.; Potempa, J.; Jarrett, C.L.; Travis, J.
Inhibition of tumor necrosis factor-alpha-induced RANTES secretion by alkaline protease in A549 cells
Am. J. Respir. Cell Mol. Biol.
33
483-489
2005
Pseudomonas aeruginosa
brenda
Leopold, I.; Fricke, B.
Inhibition, reactivation, and determination of metal ions in membrane metalloproteases of bacterial origin using high-performance liquid chromatography coupled on-line with inductively coupled plasma mass spectrometry
Anal. Biochem.
252
277-285
1997
Pseudomonas aeruginosa
brenda
Shibuya, Y.; Yamamoto, T.; Morimoto, T.; Nishino, N.; Kambara, T.; Okabe, H.
Pseudomonas aeruginosa alkaline proteinase might share a biological function with plasmin
Biochim. Biophys. Acta
1077
316-324
1991
Pseudomonas aeruginosa
brenda
Chessa, J.P.; Petrescu, I.; Bentahir, M.; Van Beeumen, J.; Gerday, C.
Purification, physico-chemical characterization and sequence of a heat labile alkaline metalloprotease isolated from a psychrophilic Pseudomonas species
Biochim. Biophys. Acta
1479
265-274
2000
Pseudomonas sp., Pseudomonas sp. TAC-II-18
brenda
Baumann, U.; Wu, S.; Flaherty, K.M.; McKay, D.B.
Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif
EMBO J.
12
3357-3364
1993
Pseudomonas aeruginosa
brenda
Kharazmi, A.; Doring, G.; Hoiby, N.; Valerius, N.H.
Interaction of Pseudomonas aeruginosa alkaline protease and elastase with human polymorphonuclear leukocytes in vitro
Infect. Immun.
43
161-165
1984
Pseudomonas aeruginosa
brenda
Horvat, R.T.; Parmely, M.J.
Pseudomonas aeruginosa alkaline protease degrades human gamma interferon and inhibits its bioactivity
Infect. Immun.
56
2925-2932
1988
Pseudomonas aeruginosa
brenda
Gambello, M.J.; Kaye, S.; Iglewski, B.H.
LasR of Pseudomonas aeruginosa is a transcriptional activator of the alkaline protease gene (apr) and an enhancer of exotoxin A expression
Infect. Immun.
61
1180-1184
1993
Pseudomonas aeruginosa
brenda
Kim, H.J.; Tamanoue, Y.; Jeohn, G.H.; Iwamatsu, A.; Yokota, A.; Kim, Y.T.; Takahashi, T.; Takahashi, K.
Purification and characterization of an extracellular metalloprotease from Pseudomonas fluorescens
J. Biochem.
121
82-88
1997
Pseudomonas fluorescens, Pseudomonas fluorescens KT1
brenda
Feltzer, R.E.; Gray, R.D.; Dean, W.L.; Pierce, W.M., Jr.
Alkaline proteinase inhibitor of Pseudomonas aeruginosa. Interaction of native and N-terminally truncated inhibitor proteins with Pseudomonas metalloproteinases
J. Biol. Chem.
275
21002-21009
2000
Pseudomonas aeruginosa
brenda
Hege, T.; Feltzer, R.E.; Gray, R.D.; Baumann, U.
Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond
J. Biol. Chem.
276
35087-35092
2001
Pseudomonas aeruginosa (Q03023), Pseudomonas aeruginosa
brenda
Ghigo, J.M.; Wandersman, C.
Cloning, nucleotide sequence and characterization of the gene encoding the Erwinia chrysanthemi B374 PrtA metalloprotease: a third metalloprotease secreted via a C-terminal secretion signal
Mol. Gen. Genet.
236
135-144
1992
Dickeya chrysanthemi, Dickeya chrysanthemi B374
brenda
Obernesser, H.J.; Doring, G.; Botzenhart, K.
Extracellular toxins of Pseudomonas aeruginosa. I. Purification and characterization of two exoproteases
Zentralbl. Bakteriol. A
A249
76-88
1981
Pseudomonas aeruginosa, Pseudomonas aeruginosa PA
brenda
Matheson, N.R.; Potempa, J.; Travis, J.
Interaction of a novel form of Pseudomonas aeruginosa alkaline protease (aeruginolysin) with interleukin-6 and interleukin-8
Biol. Chem.
387
911-915
2006
Pseudomonas aeruginosa
brenda
Walasek, P.; Honek, J.F.
Nonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease
BMC Biochem.
6
21
2005
Pseudomonas aeruginosa
brenda
Basu, B.; Apte, S.K.
A novel serralysin metalloprotease from Deinococcus radiodurans
Biochim. Biophys. Acta
1784
1256-1264
2008
Deinococcus radiodurans
brenda
Dufour, D.; Nicodeme, M.; Perrin, C.; Driou, A.; Brusseaux, E.; Humbert, G.; Gaillard, J.L.; Dary, A.
Molecular typing of industrial strains of Pseudomonas spp. isolated from milk and genetical and biochemical characterization of an extracellular protease produced by one of them
Int. J. Food Microbiol.
125
188-196
2008
Pseudomonas fluorescens (Q3YAW3)
brenda
Wang, F.; Hao, J.; Yang, C.; Sun, M.
Cloning, Expression, and Identification of a Novel Extracellular Cold-Adapted Alkaline Protease Gene of the Marine Bacterium Strain YS-80-122
Appl. Biochem. Biotechnol.
162
1497-1505
2010
Flavobacterium sp. YS-80-122 (D0VMS8)
brenda
Felfoeldi, G.; Marokhazi, J.; Kepiro, M.; Venekei, I.
Identification of natural target proteins indicates functions of a serralysin-type metalloprotease, PrtA, in anti-immune mechanisms
Appl. Environ. Microbiol.
75
3120-3126
2009
Photorhabdus luminescens
brenda
Oberholzer, A.E.; Bumann, M.; Hege, T.; Russo, S.; Baumann, U.
Metzincins canonical methionine is responsible for the structural integrity of the zinc-binding site
Biol. Chem.
390
875-881
2009
Dickeya chrysanthemi
brenda
Massaoud, M.K.; Marokhazi, J.; Venekei, I.
Enzymatic characterization of a serralysin-like metalloprotease from the entomopathogen bacterium, Xenorhabdus
Biochim. Biophys. Acta
1814
1333-1339
2011
Xenorhabdus kozodoii, Xenorhabdus kozodoii Morocco
brenda
Jain, V.; Gupta, S.; Saxena, R.; Singh, R.
Thermostable alkaline protease with detergent compatibility from newly isolated strain of Pseudomonas aeruginosa
Indian J. Agric. Biochem.
23
45-50
2010
Pseudomonas aeruginosa
-
brenda
Patil, U.; Chaudhari, A.
Optimal production of alkaline protease from solvent-tolerant alkalophilic Pseudomonas aeruginosa MTCC 7926
Indian J. Biotechnol.
10
329-339
2011
Pseudomonas aeruginosa, Pseudomonas aeruginosa MTCC 7926
-
brenda
Zhang, L.; Conway, J.F.; Thibodeau, P.H.
Calcium-induced folding and stabilization of the Pseudomonas aeruginosa alkaline protease
J. Biol. Chem.
287
4311-4322
2012
Pseudomonas aeruginosa
brenda
Laarman, A.J.; Bardoel, B.W.; Ruyken, M.; Fernie, J.; Milder, F.J.; van Strijp, J.A.; Rooijakkers, S.H.
Pseudomonas aeruginosa alkaline protease blocks complement activation via the classical and lectin pathways
J. Immunol.
188
386-393
2012
Pseudomonas aeruginosa
brenda
Singh, S.; Singh, S.; Tripathi, V.; Khare, S.; Garg, S.
Comparative one-factor-at-a-time, response surface (statistical) and bench-scale bioreactor level optimization of thermoalkaline protease production from a psychrotrophic Pseudomonas putida SKG-1 isolate
Microb. Cell Fact.
10
114
2011
Pseudomonas putida, Pseudomonas putida SKG-1
brenda
Shanks, R.; Stella, N.; Hunt, K.; Brothers, K.; Zhang, L.; Thibodeau, P.
Identification of SlpB, a cytotoxic protease from Serratia marcescens
Infect. Immun.
83
2907-2916
2015
Serratia marcescens, Serratia marcescens PIC3611
brenda
Lakshmi Bhargavi, P.; Prakasham, R.
A fibrinolytic, alkaline and thermostable metalloprotease from the newly isolated Serratia sp RSPB11
Int. J. Biol. Macromol.
61
479-486
2013
Serratia marcescens, Serratia marcescens RSPB11
brenda
Ertan, H.; Cassel, C.; Verma, A.; Poljak, A.; Charlton, T.; Aldrich-Wright, J.; Omar, S.; Siddiqui, K.; Cavicchioli, R.
A new broad specificity alkaline metalloprotease from a Pseudomonas sp. isolated from refrigerated milk: Role of calcium in improving enzyme productivity
J. Mol. Catal. B
113
1-8
2015
Pseudomonas sp., Pseudomonas sp. RC
-
brenda
Merheb-Dini, C.; Cabral, H.; Leite, R.S.; Zanphorlin, L.M.; Okamoto, D.N.; Rodriguez, G.O.; Juliano, L.; Arantes, E.C.; Gomes, E.; da Silva, R.
Biochemical and functional characterization of a metalloprotease from the thermophilic fungus Thermoascus aurantiacus
J. Agric. Food Chem.
57
9210-9217
2009
Thermoascus aurantiacus
brenda
Bersanetti, P.A.; Park, H.; Bae, K.S.; Son, K.; Shin, D.; Hirata, I.Y.; Juliano, M.A.; Carmona, A.K.; Juliano, L.
Characterization of arazyme, an exocellular metalloprotease isolated from Serratia proteamaculans culture medium
Enzyme Microb. Technol.
37
574-581
2005
Serratia proteamaculans
-
brenda