Information on EC 3.4.24.40 - serralysin

Word Map on EC 3.4.24.40
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.24.40
-
RECOMMENDED NAME
GeneOntology No.
serralysin
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage of bonds with hydrophobic residues in P1'
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
70851-98-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Automatic Mining of ENzyme DAta
animal
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
B374
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
plant
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
i.e. strain UH-5
-
-
Manually annotated by BRENDA team
KT1
-
-
Manually annotated by BRENDA team
MTCC 10510
-
-
Manually annotated by BRENDA team
Pseudomonas sp. TAC-II-18
-
-
-
Manually annotated by BRENDA team
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
strain BG
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain E-15
-
-
Manually annotated by BRENDA team
shrimp
-
-
-
Automatic Mining of ENzyme DAta
snake
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
-
-
-
Automatic Mining of ENzyme DAta
Xenorhabdus kozodoii Morocco strain
-
-
-
Manually annotated by BRENDA team
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
malfunction
physiological function
additional information
-
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
-
-
?
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
-
-
-
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-Phe-Gly-Ala + H2O
?
show the reaction diagram
-
-
-
-
-
Benzyloxycarbonyl-Ala-Phe-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-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-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
Benzyloxycarbonyl-Phe-Leu-Ala-Ala + H2O
?
show the reaction diagram
-
best substrate
-
-
-
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-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
-
-
-
beta-1,3 glucan recognition protein 2 + H2O
?
show the reaction diagram
-
identified target by in vitro exposure of hemolymph to PrtA
-
-
?
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
-
-
-
casein + H2O
?
show the reaction diagram
D-Ala-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
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
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
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
KMnO4
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
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
-
-
Automatic Mining of ENzyme DAta
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme from Serratia sp., expressed in Escherichia coli
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
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