Information on EC 3.4.24.40 - serralysin

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
3.4.24.40
-
RECOMMENDED NAME
GeneOntology No.
serralysin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage of bonds with hydrophobic residues in P1'
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
70851-98-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
B374
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
i.e. strain UH-5
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Manually annotated by BRENDA team
PA
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Manually annotated by BRENDA team
KT1
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
MTCC 10510
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Manually annotated by BRENDA team
MTCC 10510
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Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Pseudomonas sp. TAC-II-18
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Manually annotated by BRENDA team
strain BG
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
formerly Aranicola proteolyticus, symbiotic bacterium of spider Nephila clavata
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Manually annotated by BRENDA team
strain E-15
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Manually annotated by BRENDA team
Xenorhabdus kozodoii Morocco strain
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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the calcium-regulated alkaline protease is a member of the repeats in toxin, RTX, family of proteins
malfunction
physiological function
additional information
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the enzyme is compatible at 60C with commercial detergents
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
2-Aminobenzoyl-Gly-Phe-Arg-Xaa 4-nitrobenzyl amide + H2O
?
show the reaction diagram
Abz-LGMISLMKRPPGFSPFRSSRI-NH2 + H2O
?
show the reaction diagram
-
peptide corresponds to fragment L373-I393 of human kininogen, cleavage of Arg-Ser, Gly-Phe and Lys-Arg bond
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-
?
Ac-Pro-Leu-Gly-[2-mercapto-4-methylpentanoyl]-Leu-Gly-OEt + H2O
?
show the reaction diagram
-
-
-
-
?
Aminoethylated lysozyme + H2O
?
show the reaction diagram
-
-
-
-
-
angiotensin I + H2O
DRVY + IHPFLHL + DRVYI + HPFHL
show the reaction diagram
-
-
-
?
Angiotensin II + H2O
?
show the reaction diagram
-
-
-
?
azocasein + H2O
?
show the reaction diagram
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl tripeptides + H2O
?
show the reaction diagram
-
overview
-
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-
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
?
show the reaction diagram
Benzyloxycarbonyl-Ala-Gly-Gly-Leu + H2O
?
show the reaction diagram
-
-
-
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Benzyloxycarbonyl-Ala-Gly-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
-
-
-
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Benzyloxycarbonyl-Ala-Gly-Gly-Leu-Xaa + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P3' results in marked increase in hydrolysis
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Benzyloxycarbonyl-Ala-Phe-Gly-Ala + H2O
?
show the reaction diagram
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Benzyloxycarbonyl-Ala-Phe-Leu-Ala + H2O
?
show the reaction diagram
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-
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Benzyloxycarbonyl-Gly-Ala-Ala + H2O
?
show the reaction diagram
Benzyloxycarbonyl-Gly-Gly-Gly-Leu + H2O
?
show the reaction diagram
-
poor substrate
-
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Benzyloxycarbonyl-Gly-Gly-Leu amide + H2O
?
show the reaction diagram
-
poor substrate
-
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Benzyloxycarbonyl-Gly-Leu-Gly-Gly + H2O
?
show the reaction diagram
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-
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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
-
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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
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Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
?
show the reaction diagram
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-
-
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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
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
?
show the reaction diagram
-
best substrate
-
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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
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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
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Benzyloxycarbonyl-Xaa-Gly-Leu-Ala + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
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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
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Benzyloxycarbonyl-Xaa-Phe-Gly-Ala + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
-
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Benzyloxycarbonyl-Xaa-Phe-Leu-Ala + H2O
?
show the reaction diagram
-
a hydrophobic or bulky residue at P2 results in marked increase in hydrolysis
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beta-1,3 glucan recognition protein 2 + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
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?
Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Boc-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Bovine serum albumin + H2O
?
show the reaction diagram
C-terminal octapeptide of glucagon + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
Carboxymethyl-beta-insulin + H2O
?
show the reaction diagram
-
cleavage sites
-
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-
casein + H2O
?
show the reaction diagram
D-Ala-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
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?
Dabcyl-Glu-Val-Tyr-Ala-Val-Glu-Ser-EDANS + H2O
?
show the reaction diagram
-
-
-
-
?
DL-Val-Leu-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
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?
Egg albumin + H2O
?
show the reaction diagram
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-
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Fibrin + H2O
?
show the reaction diagram
Fibrinogen + H2O
?
show the reaction diagram
Fibronectin + H2O
?
show the reaction diagram
-
-
-
?
furylacryloyl-Ala-Leu-Val-Tyr + H2O
?
show the reaction diagram
-
-
-
-
?
furylacryloyl-Leu-Gly-Pro-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
gelatine + H2O
?
show the reaction diagram
Glucagon + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
Glycoprotein G + H2O
?
show the reaction diagram
-
i.e. thrombin-sensitive protein, thrombospondin, MW 190000
-
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hemocyte aggregation inhibitor protein (HAIP) + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
Hemoglobin + H2O
?
show the reaction diagram
hide powder azure + H2O
?
show the reaction diagram
-
-
-
-
-
His-Ser-4-methoxy-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
His-Ser-4-methoxy-2-naphthylamide + H2O
His-Ser + 4-methoxy-2-naphthylamine
show the reaction diagram
-
-
-
-
?
Human alpha1-proteinase inhibitor + H2O
?
show the reaction diagram
-
MW 52000
-
-
-
human complement component C1 + H2O
?
show the reaction diagram
-
-
-
-
?
human complement component C2 + H2O
?
show the reaction diagram
-
-
-
-
?
Human platelet surface glycoprotein Ib + H2O
?
show the reaction diagram
-
-
-
-
-
Immunoglobulin A1 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin A2 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin G1 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin G2 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin G3 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
Immunoglobulin G4 + H2O
?
show the reaction diagram
-
Serratia marcescens, MW 56000 enzyme, predominantly interdomain cleavage at hinge region
-
-
-
including serpin-1I + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
interleukin-6 + H2O
?
show the reaction diagram
-
complete digestion
-
-
?
interleukin-8 + H2O
?
show the reaction diagram
-
rapid processing to a 72 amino acid form, further degradation is slow
-
-
?
L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala + L-Ala-L-Ala
show the reaction diagram
-
-
-
-
L-Ala-L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala + L-Ala-L-Ala-L-Ala
show the reaction diagram
-
-
-
-
L-Ala-L-Ala-L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala-L-Ala + L-Ala-L-Ala-L-Ala
show the reaction diagram
-
-
-
-
L-Ala-oligopeptides + H2O
?
show the reaction diagram
-
proteolytic activity increases drastically with increasing chain length from tetramer to hexamer, no substrate: dipeptide or tripeptide
-
-
-
L-Ser-7-amido-4-methylcoumarin + H2O
L-Ser + 7-amino-4-methylcoumarin
show the reaction diagram
N-alpha-benzoyl-DL-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
artificial substrate BAPNA
-
?
N-benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-terminal hexapeptide of glucagon + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KDR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KFR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KGRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KGR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KHRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KHR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLAFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLA + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLDFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLD + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLEFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLE + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLFFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLF + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLGFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLG + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLHFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLH + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLKFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLK + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLLFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLL + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLMFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLM + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLNFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLN + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLPFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLP + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLQFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLQ + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRASKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + ASKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRDSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + DSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRLSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + LSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + NSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRRSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + RSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLR + SSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLSFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLS + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLTFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLT + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLXWFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLXW + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KLYFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KLY + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KNRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KNR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KQRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KQR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KRRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KRR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine) + H2O
o-aminobenzoyl-KSR + FSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
show the reaction diagram
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
show the reaction diagram
peptide 6A + H2O
?
show the reaction diagram
-
-
-
?
Plasma fibronectin + H2O
?
show the reaction diagram
Pro-Phe-Arg 4-methylcoumarin 7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
Pro-Phe-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Ribonuclease + H2O
?
show the reaction diagram
-
-
-
-
-
scolexins A + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
scolexins B + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
serine proteinase homolog 3 + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
serpin-1 variants + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA, six serpin-1 variants differing in their 40- to 50-amino-acid-long C-terminal sequences are identified
-
-
?
substance P + H2O
RPKPQQFFG + LM-NH2 + RPKPQQFF + GLM-NH2 + RPKQQF + FGLM-NH2
show the reaction diagram
-
-
-
?
substance P 1-7 + H2O
?
show the reaction diagram
-
-
-
?
substance P 1-9 + H2O
RPKP + QQFFG + RPKQQ + FFG
show the reaction diagram
-
-
-
?
substance P 7-11 + H2O
?
show the reaction diagram
-
-
-
?
substance P 8-11 + H2O
?
show the reaction diagram
-
-
-
?
substance P(free acid) + H2O
RPKPQQFFG + LM + RPKPQQFF + GLM + RPKQQF + FGLM
show the reaction diagram
-
-
-
?
Suc-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Succ-Ala-Ala-Pro-Phe-thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Succ-Ala-Ala-Pro-Xaa-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
t-butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Gln-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
t-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Gly-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Gly-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Leu-Lys-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
t-butyloxycarbonyl-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
-
-
-
-
?
Tryptic insulin heptapeptide + H2O
?
show the reaction diagram
-
cleavage sites
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Fibrin + H2O
?
show the reaction diagram
Fibrinogen + H2O
?
show the reaction diagram
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
Fe2+
-
restores activity after EDTA treatment, Serratia marcescens MW 56000 enzyme, not MW 60000 enzyme
Mn2+
-
activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,2'-bipyridyl
8-hydroxyquinoline
-
0.1 mM at pH 10, 5 mM at pH 7
Ac-Val-Leu-Lys-4-mercaptoanilide
-
pH 7.8, 37C, 0.2 mM 69% inhibition, 0.3 mM complete inhibition
Ag2+
-
strong
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
-
Ca2+
-
inhibitory above 0.1 mM
Cd2+
-
at pH 10, not at pH 7
chymostatin
-
0.1 mM, 18% inhibition at pH 8.0
Cysteine hydrochloride
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
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
-
Leupeptin
N-bromosuccinimide
N-ethylmaleimide
N-tosyl-L-phenylalanine chloromethyl ketone
-
0.1 mM, 18% inhibition at pH 8.0
Ni2+
-
at pH 10, not at pH 7
nitrilotriacetate
-
weak
o-phenanthroline
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
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
Sodium thioglycolate
Soybean trypsin inhibitor
-
0.01 mM, 9% inhibition at pH 5.5
-
Tetraethylenepentamine
-
zinc-specific chelator
Tetramethylenepentamine
-
Serratia marcescens
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide
-
-
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
0.00308
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.00096
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.0027
o-aminobenzoyl-KGRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.0007
o-aminobenzoyl-KHRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.002
o-aminobenzoyl-KLFFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.00582
o-aminobenzoyl-KLRDSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00292
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00137
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00056
o-aminobenzoyl-KLWFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
-
pH 8.0, 37C
0.00198
o-aminobenzoyl-KNRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00115
o-aminobenzoyl-KQRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
0.00157
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
-
pH 8.0, 37C
17.3
Phe-Gly-Leu-Ala
-
-
0.015 - 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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.52 - 2.94
angiotensin I
0.53 - 6.08
angiotensin II
0.045
azocasein
Pseudomonas sp.
-
at pH 6.5 and 25C
-
0.0073 - 0.026
benzyloxycarbonyl-L-Arg-L-Arg-4-nitroanilide
1.3
o-aminobenzoyl-KDRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
Serratia proteamaculans
-
pH 8.0, 37C
3.8 - 20.67
o-aminobenzoyl-KFRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
9.5
o-aminobenzoyl-KGRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
Serratia proteamaculans
-
pH 8.0, 37C
32.5
o-aminobenzoyl-KHRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
Serratia proteamaculans
-
pH 8.0, 37C
44.2
o-aminobenzoyl-KLFFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
Serratia proteamaculans
-
pH 8.0, 37C
0.57
o-aminobenzoyl-KLRDSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
Serratia proteamaculans
-
pH 8.0, 37C
0.26 - 52.17
o-aminobenzoyl-KLRNSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
0.3 - 35.07
o-aminobenzoyl-KLRSSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
6.7
o-aminobenzoyl-KLWFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)-dinitrophenyl
Serratia proteamaculans
-
pH 8.0, 37C
28.19
o-aminobenzoyl-KNRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
Serratia proteamaculans
-
pH 8.0, 37C
40.41
o-aminobenzoyl-KQRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
Serratia proteamaculans
-
pH 8.0, 37C
0.52 - 14.43
o-aminobenzoyl-KSRFSKQ-(N-(2,4-dinitrophenyl)-ethylenediamine)
0.038
peptide 6A
Pseudomonas aeruginosa
-
pH 8.6, 30C
-
33
substance P 1-7
Pseudomonas aeruginosa
-
pH 8.6, 30C
56
substance P 1-9
Pseudomonas aeruginosa
-
pH 8.6, 30C
0.08
substance P 7-11
Pseudomonas aeruginosa
-
pH 8.6, 30C
0.02
substance P 8-11
Pseudomonas aeruginosa
-
pH 8.6, 30C
160
substance P(free acid)
Pseudomonas aeruginosa
-
pH 8.6, 30C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00217
L3D SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000903
L3DSmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000791
L3F SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.00107
L3G SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000723
L3I SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.00184
L3K SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000958
L3P SmaPI
-
pH 7.0, 25C, mutant inhibitor
-
0.000713
SmaPI
-
pH 7.0, 25C, wild-type inhibitor
-
0.000728
SmaPIAddA
-
pH 7.0, 25C, mutant inhibitor
-
0.000725
SmaPIDelG1
-
pH 7.0, 25C, mutant inhibitor
-
0.00274
SmaPIDelG1-L3
-
pH 7.0, 25C, mutant inhibitor
-
0.000736
SmaPIDelG1-S2
-
pH 7.0, 25C, mutant inhibitor
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.98
-
7-amino-4-methyl-coumarin, 37C, pH 8.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
with substrate t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide in absence and presence of Co2+
5.5 - 7.5
-
azocasein as substrate
6 - 10
6 - 7
-
two optima: 6-7 and 8-10, strain SF 178
7 - 9
-
egg white albumin, hemoglobin as substrates
8 - 9
-
casein as substrate
8 - 10
-
two optima: 6-7 and 8-10, strain SF 178
9 - 10
-
-
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 8.8
-
more than 90% of maximal activity between pH 6.0 and 8.8, 44% activity at pH 5.2
6 - 10
-
about half-maximal activity at pH 6 and about 80% of maximal activity at pH 10, casein as substrate, about 75% of maximal activity at pH 6 and about 60% of maximal activity at pH 10, egg white albumin as substrate
6 - 8
-
in absence and presence of Co2+
6.5 - 10
-
about half-maximal activity at pH 6.5 and about 65% of maximal activity at pH 10, hemoglobin as substrate
7 - 11
-
more than 50% activity between pH 7.0 and 11.0
7.2 - 10.8
-
about half-maximal activity at pH 7.2 and 10.8
7.5 - 10.6
-
-
8 - 9
-
with substrate t-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide in the presence of Co2+
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
highest acitivity after 4 days of culture
25
-
at pH 10, in sodium carbonate buffer
40
-
at pH 8, in phosphate buffer
additional information
-
assay carried out at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
more than 50% activity between 30 and 50C
42 - 62
-
about half-maximal activity at 42C and 62C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
isoelectric focusing
8.5
-
isoelectric focusing
8.7
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme from Serratia sp., expressed in Escherichia coli
Manually annotated by BRENDA team
-
and extracellular
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Serratia marcescens (strain ATCC 21074 / E-15)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
-
Serratia marcescens, gel filtration
45000
-
Escherichia freundii, gel filtration
45400
-
Escherichia freundii, minimum MW calculated on the basis of zinc content
45800
-
Escherichia freundii, sedimentation equilibrium studies
46000
-
gel filtration
47000
-
SDS-PAGE
48400
-
Pseudomonas aeruginosa, sedimentation velocity centrifugation
48690
-
calculated; electrospray mass spectrometry
48730
-
electrospray mass spectrometry
48770
-
electrospray mass spectrometry
50600
-
Serratia piscatrum, deduced from nucleotide sequence
50630
-
Serratia piscatrum, deduced from nucleotide sequence
51100
-
Erwinia chrysanthemi, recombinant protease C, calculated from nucleotide sequence
51900
-
Serratia marcescens, sedimentation equilibrium centrifugation
56000
-
Serratia marcescens, strain kums, two enzymes: MW 56000 and MW 60000
60000
-
Serratia marcescens, two enzymes: MW 56000 and MW 60000
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
0.69 mol sugar/mol enzyme
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
two-domain protein with a calcium binding parallel beta roll motif, 1.64A by multiple isomorphous replacement and non-crystallographic symmetry averaging between different crystal forms, crystallization at 4 and 18 C, spanning pH range of 3-9
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 4
-
inactivation
31244
3.5 - 11
-
stable in this range
31249
5 - 10
-
3 h, stable at 30C
31243
5 - 9
-
10 min, fairly stable at 30C
31249
5 - 10
-
1 h, at room temperature
31244
6 - 8.5
-
1 h, stable at 30C
31243
6 - 9
-
room temperature
667022
6 - 10
-
the enzyme shows more than 50% activity at pH 6.0-10.0 after 1 h incubation time, while residual activities ranging from 43.20-8.30% are observed at higher pH (11.0-12.0) and lower pH (4.0-5.0) values
733986
6.5
-
10 min, stable below 45C
31243
7 - 10
-
stable within this range, maximum stability at pH 10.0 after 2 h
717655
7.5
-
15 min, stable at 25-45C
31244
10
-
10 min, stable below 25C, inactivation at 35C
31243
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 70
-
after 1 h of incubation, the enzyme shows 100% activity between 4 and 37C, 95% activity at 40C, 85% activity at 50C, 65% activity at 60C, and 50% activity at 70C
10 - 45
-
stable within this range, sharp decrease in stability above
25
-
and below, 10 min stable at pH 10
25 - 40
-
stable at 25C, but declining activity above 40C
25 - 45
-
15 min, stable at pH 7.5
35
-
10 min, pH 10, inactivation
42 - 48
-
the enzyme shows a half-life of 4.9 min, 3.4 min, 2.2 min, and 1.2 min at 42C, 44C, 46C, and 48C, respectively
50
-
below, 10 min, fairly stable at neutral pH-values
63
-
10 min, inactivation in the presence of stabilizing agents
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
sensitive to trypsin degradation
-
Unstable in the presence of 10 mM CaCl2
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, lyophilized Serratia marcescens enzyme, several months
-
0C, pH 4.5-11.5, 1 day
-
4C, 5 mg enzyme/ml deionized glass-distilled water, 1 day
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 immunologically not related enzymes: MW 56000 and MW 60000
-
ammonium sulfate precipitation, anion exchange column chromatography, and gel filtration
-
ammonium sulfate precipitation, DEAE-cellulose column chromatography, and Sephadex G-75 gel filtration
-
ammonium sulfate precipitation, gel filtration, chromatography
-
dialysis against 10 mM N-methyldiethanolamine, DE-52 gel filtration, chelating Sepharose 6B gel filtration, dialysis against 0.02M triethanolamine-HCl buffer
-
gel filtration
-
metal chelate chromatography with copper and hydrophobic interaction chromatography, dialysis
-
native enzyme by two different steps of anion exchange chromatography
-
precipitation with ammonium sulfate and acetone, gel filtration and chromatography
-
purification from culture fluid
-
purified to homogeneity by precipitation with ammonium sulfate (65%). After dialysis, the crude enzyme is further purified by FPLC using Superdex 200 column
recombinant refolded His-tagged wild-type and mutant AP proteins and domains from inclusion bodies by nickel affinity chromatography
-
to near homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apr gene requires the lasR gene for transcription
-
Erwinia chrysanthemi; expressed in Escherichia coli
-
expressed in Escherichia coli
expressed in Escherichia coli; expressed in Serratia marcescens strain pSP2; Serratia marcescens (wild-type)
-
expressed in Escherichia coli; expressed in Serratia marcescens; Serratia piscatrum
-
expression in Escherichia coli C600, synthesized as a zymogen ProA
-
expression of wild-type and mutant AP proteins and domains at high levels in inclusion bodies
-
recombinantly expressed in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
secretion of SlpB requires type I secretion protein LipD
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
M226A
-
using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants
M226A/E189A
-
introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
M226H
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mutant could not be purified, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants
M226H/E189A
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introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
M226I
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M226I possesses 50% of wild-type activity, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants
M226I/E189A
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introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
M226L
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M226L possesses 85% of wild-type activity, using a resorufin-casein assay proteolytic activity decreases in the following order: M226 higher than M226L higher than M226I higher than M226H higher than M226A. The levels of secreted protein decrease in the same order, indicating some defect in synthesis and secretion or stability of the mutants
M226L/E189A
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introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
M226N
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mutant could not be purified
M226N/E189A
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introduction of additional E189A mutation leads to a complete enzymatic inactivation since catalytic base is knocked out. This helps in purification and crystallization. Replacement of the methionine side chain results in an increasing distortion of the zinc-binding geometry, especially pronounced in the lambda2 angles of the first and third histidine of the consensus sequence. This is correlated with an increasing loss of proteolytic activity and a sharp increase of flexibility of large segments of the polypeptide chain
additional information
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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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