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Information on EC 3.4.24.40 - serralysin and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q03023

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.40 serralysin
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Select one or more organisms in this record: ?
This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q03023 not found.
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Preferential cleavage of bonds with hydrophobic residues in P1'
Synonyms
protease i, serralysin, arazyme, protease c, extracellular metalloproteinase, zinc proteinase, thermostable alkaline protease, pseudomonas aeruginosa alkaline protease, amp-p, thermoalkaline protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aeruginolysin
-
-
Alkaline protease
-
-
calcium-regulated alkaline protease
-
-
Escherichia freundii proteinase
-
-
-
-
Extracellular metalloproteinase
-
-
-
-
Proteinase, Serratia marcescens metallo-
-
-
-
-
pseudomonal serralysin
-
-
Pseudomonas aeruginosa alk. protease
-
-
-
-
Pseudomonas aeruginosa alkaline protease
-
-
Pseudomonas aeruginosa alkaline proteinase
-
-
-
-
Pseudomonas alkaline protease
-
-
Serratia marcescens extracellular proteinase
-
-
-
-
Serratia marcescens metalloprotease
-
-
-
-
Serratia marcescens metalloproteinase
-
-
-
-
thermostable alkaline protease
-
-
zinc proteinase
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
70851-98-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
-
?
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt + 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
-
-
-
-
?
Benzyloxycarbonyl tripeptides + H2O
?
show the reaction diagram
-
overview
-
-
?
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
?
show the reaction diagram
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-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Ala-Phe-Gly-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Ala-Phe-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-D-Ala-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Gly-Ala-Ala + H2O
?
show the reaction diagram
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-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Leu-Gly-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
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-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Gly-Leu-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
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-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-Gly-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
?
show the reaction diagram
-
best substrate
-
-
?
benzyloxycarbonyl-Phe-Phe-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
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-Val-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
?
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
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
human complement component C1 + H2O
?
show the reaction diagram
-
-
-
-
?
human complement component C2 + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
peptide 6A + H2O
?
show the reaction diagram
-
-
-
?
Phe-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
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-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
activates
Mn2+
-
activates
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-bipyridyl
-
not
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-bromosuccinimide
-
-
N-ethylmaleimide
-
not (Serratia marcescens enzyme)
Sodium thioglycolate
-
not
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 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
17.3
Phe-Gly-Leu-Ala
-
-
0.021
t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide
-
pH 7.8, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.52 - 2.94
angiotensin I
0.53 - 6.08
angiotensin II
0.0073 - 0.026
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
0.038
peptide 6A
-
pH 8.6, 30°C
-
33
substance P 1-7
-
pH 8.6, 30°C
56
substance P 1-9
-
pH 8.6, 30°C
0.08
substance P 7-11
-
pH 8.6, 30°C
0.02
substance P 8-11
-
pH 8.6, 30°C
160
substance P(free acid)
-
pH 8.6, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
-
broad
7
-
benzyloxycarbonyl-Phe-Ala-Ala or benzyloxycarbonyl-Ala-Phe-Gly-Ala as substrate
7 - 9
-
egg white albumin, hemoglobin as substrates
8 - 9
-
casein as substrate
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
6.5 - 10
-
about half-maximal activity at pH 6.5 and about 65% of maximal activity at pH 10, hemoglobin as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42 - 62
-
about half-maximal activity at 42°C and 62°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
isoelectric focusing
8.7
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the calcium-regulated alkaline protease is a member of the repeats in toxin, RTX, family of proteins
physiological function
additional information
-
the enzyme is compatible at 60°C with commercial detergents
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48400
-
Pseudomonas aeruginosa, sedimentation velocity centrifugation
49500
57000
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 49500, full length mature enzyme, mass spectrometry
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
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
Pseudomonas aeruginosa
-
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 11
-
stable in this range
31249
5 - 9
-
10 min, fairly stable at 30°C
31249
6 - 9
-
room temperature
667022
7 - 10
-
stable within this range, maximum stability at pH 10.0 after 2 h
717655
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 40
-
stable at 25°C, but declining activity above 40°C
30
-
pH 5-9, fairly stable
50
-
below, 10 min, fairly stable at neutral pH-values
55
-
10 min, partly unstable in distilled water, 100 mM phosphate or 10 mM CaCl2 stabilizes
63
-
10 min, inactivation in the presence of stabilizing agents
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to trypsin degradation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
apr gene requires the lasR gene for transcription
-
expression of wild-type and mutant AP proteins and domains at high levels in inclusion bodies
-
RENATURED/Commentary
ORGANISM
UNIPROT
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
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Morihara, K.
Pseudomonas aeruginosa proteinase. I. Purification and general properties
Biochim. Biophys. Acta
73
113-124
1963
Pseudomonas aeruginosa
-
Manually annotated by BRENDA team
Inoue, H.; Nakagawa, T.; Morihara, K.
Pseudomonas aeruginosa proteinase. II. Molecular weight and molecular dimension
Biochim. Biophys. Acta
73
125-131
1963
Pseudomonas aeruginosa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team