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125I-insulin + H2O
?
-
-
-
-
?
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
-
-
?
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt + H2O
?
-
-
-
-
?
angiotensin I + H2O
DRVY + IHPFLHL + DRVYI + HPFHL
-
-
-
?
angiotensin II + H2O
?
-
-
-
?
azocasein + 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
-
Pseudomonas aeruginosa alkaline proteinase and MW 52000 Serratia enzyme
-
?
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
-
-
?
Egg albumin + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
human complement component C1 + H2O
?
-
-
-
-
?
human complement component C2 + H2O
?
-
-
-
-
?
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
-
-
?
Oxidized insulin B-chain + H2O
?
peptide 6A + H2O
?
-
-
-
?
Phe-Gly-Leu-Ala + H2O
?
-
-
-
-
?
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-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
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
?
-
-
-
-
?
additional information
?
-
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
-
-
?
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
-
-
?
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
-
-
?
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Ac-Val-Leu-Lys-4-mercaptoanilide
-
pH 7.8, 37°C, 0.2 mM 69% inhibition, 0.3 mM complete inhibition
APRin protein
-
slow binding inhibition, reversible inhibition. and truncated mutants
-
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
Cysteine hydrochloride
-
not Serratia marcescens enzyme
DTT
-
weak, Serratia marcescens
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
Sodium thioglycolate
-
not
1,10-phenanthroline
-
-
1,10-phenanthroline
-
strong
1,10-phenanthroline
-
10 mM
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
EDTA
-
strong, 5 mM
EDTA
-
1 mmol, pH 8.1, no inactivation by 0.1 M EDTA
EDTA
-
30 min, room temperature, pH 7.5, complete inhibition in a concentration range below 1 mM
additional information
-
-
-
additional information
-
PCMB
-
additional information
-
PCMB
-
additional information
-
monoiodoacetic acid
-
additional information
-
diisopropyl phosphofluoridate
-
additional information
-
diisopropyl phosphofluoridate
-
additional information
-
soybean trypsin inhibitor
-
additional information
-
soybean trypsin inhibitor
-
additional information
-
potato inhibitor
-
additional information
-
potato inhibitor
-
additional information
-
citrate, NaF, oxalate
-
additional information
-
tosyl-L-Phe chloromethyl ketone or tosyl-L-Lys chloromethyl ketone
-
additional information
-
not inhibited by chloromethylketone or hydroxamate
-
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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 - 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
0.021
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide
-
pH 7.8, 37°C
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
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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
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
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
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
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
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
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
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