3.4.24.40: serralysin
This is an abbreviated version!
For detailed information about serralysin, go to the full flat file.
Word Map on EC 3.4.24.40
-
3.4.24.40
-
elastase
-
metalloproteases
-
achromobacter
-
lyticus
-
caseinolytic
-
chrysanthemi
-
metzincins
-
medicine
- 3.4.24.40
- elastase
- metalloproteases
- achromobacter
- lyticus
-
caseinolytic
- chrysanthemi
-
metzincins
- medicine
Reaction
Preferential cleavage of bonds with hydrophobic residues in P1' =
Synonyms
aeruginolysin, Alkaline protease, AMP-P, AP, APR, AprA, AprX, arazyme, calcium-regulated alkaline protease, DR2310 protease, Escherichia freundii proteinase, Extracellular metalloproteinase, LupA, More, protease B, protease C, protease I, Proteinase, Serratia marcescens metallo-, PrtA, PrtA metalloprotease, PrtC, pseudomonal serralysin, Pseudomonas aeruginosa alk. protease, Pseudomonas aeruginosa alkaline protease, Pseudomonas aeruginosa alkaline proteinase, Pseudomonas alkaline protease, psychrophilic alkaline metalloprotease, serralysin, serralysin-like metalloprotease, Serratia marcescens extracellular proteinase, Serratia marcescens metalloprotease, Serratia marcescens metalloproteinase, SlpB, SMP, thermoalkaline protease, thermostable alkaline protease, zinc proteinase
ECTree
3.4.24.40 serralysinAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.24.40 - serralysin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
-
-
-
?
Benzyloxycarbonyl-Ala-Gly-Gly-Leu-Xaa + H2O
?
-
a hydrophobic or bulky residue at P3' results in marked increase in hydrolysis
-
-
?
Benzyloxycarbonyl-Gly-Leu-Gly-Gly-Xaa + H2O
?
-
a hydrophobic or bulky residue at P3' results in marked increase in hydrolysis
-
-
?
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-Phe-Arg 4-methylcoumarin 7-amide + H2O
Benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
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-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
-
-
?
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
-
-
?
His-Ser-4-methoxy-2-naphthylamide + H2O
His-Ser + 4-methoxy-2-naphthylamine
-
-
-
-
?
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-8 + H2O
?
-
rapid processing to a 72 amino acid form, further degradation is slow
-
-
?
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
-
-
?
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
?
-
-
-
-
?
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)
-
-
-
-
?
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(free acid) + H2O
RPKPQQFFG + LM + RPKPQQFF + GLM + RPKQQF + FGLM
-
-
-
?
t-butyloxycarbonyl-Gln-Ala-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-Met-Thr-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + 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-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
-
-
?
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
?
-
cleavage site: AlaÄ+ÄAla-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
-
?
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
-
-
?
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
-
-
?
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 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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
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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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additional information
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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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