3.4.21.19: glutamyl endopeptidase
This is an abbreviated version!
For detailed information about glutamyl endopeptidase, go to the full flat file.
Word Map on EC 3.4.21.19
-
3.4.21.19
-
aureus
-
staphylococcus
-
chymotrypsin
-
cyanogen
-
bromide
-
edman
-
epitope
-
cnbr
-
reverse-phase
-
phosphoprotein
-
thermolysin
-
phosphopeptide
-
alpha-chymotrypsin
-
papain
-
photolabeled
-
lysyl
-
photoaffinity
-
antiserum
-
venom
-
cooh-terminal
-
subtilisin
-
32p-labeled
-
elastase
-
n-linked
-
deglycosylation
-
polyvinylidene
-
photoaffinity-labeled
-
clostripain
-
torpedo
-
n-glycanase
-
phosphoamino
-
analysis
-
half-cystine
-
endoglycosidase
-
intermedius
-
endoprotease
-
endopeptidases
-
virion
-
photoreactive
-
difluoride
-
125i-labeled
-
doublet
-
glycopeptides
-
electroblotted
-
rp-hplc
-
n-chlorosuccinimide
-
s-carboxymethylated
-
synthesis
-
achromobacter
-
one-dimensional
-
intrachain
- 3.4.21.19
- aureus
- staphylococcus
- chymotrypsin
-
cyanogen
- bromide
-
edman
- epitope
- cnbr
-
reverse-phase
- phosphoprotein
- thermolysin
- phosphopeptide
- alpha-chymotrypsin
- papain
-
photolabeled
-
lysyl
-
photoaffinity
- antiserum
- venom
-
cooh-terminal
- subtilisin
-
32p-labeled
- elastase
-
n-linked
-
deglycosylation
-
polyvinylidene
-
photoaffinity-labeled
- clostripain
- torpedo
- n-glycanase
-
phosphoamino
- analysis
-
half-cystine
-
endoglycosidase
- intermedius
- endoprotease
- endopeptidases
- virion
-
photoreactive
-
difluoride
-
125i-labeled
-
doublet
- glycopeptides
-
electroblotted
-
rp-hplc
- n-chlorosuccinimide
-
s-carboxymethylated
- synthesis
- achromobacter
-
one-dimensional
-
intrachain
Reaction
Preferential cleavage: Glu-/-, Asp-/- =
Synonyms
Alcalase, BIEP, BIGEP, BL-GSE, BLase, BS-GSE, endoproteinase Glu-C, endoproteinase V8, Glu C, Glu-C, Glu-endopeptidase, Glu-specific endopeptidase, GluScoh, GluScpr, GluSE, GluSsap, GluSW, glutamate specific endopeptidase, glutamate-specific proteinase, glutamate-specific serine endopeptidase, glutamic acid-specific endopeptidase, glutamic acid-specific proteinase, glutamic-acid-specific endopeptidase, glutamyl endopeptidase, glutamyl endopeptidase 2, glutamyl endopeptidase I, glutamyl specific endopeptidase, GluV8, GSE, gseBi gene product, protease V8, proteinase, glutamate-specific, proteinase, staphylococcal serine, SG-GSE, SGPE, Sspa, staphylococcal serine proteinase, V8 protease, V8 proteinase, V8-GSE, V8-protease, VSPase
ECTree
3.4.21.19 glutamyl endopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.19 - glutamyl endopeptidase
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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
22 kDa human growth hormone + H2O
peptide fragment 1-32 of 22 kDa human growth hormone + peptide fragment 33-191 of 22 kDa human growth hormone
-
V8-protease digestion generates the fragment amino acids 33-191, resulting from a cleavage of the amino acids 32-33 bond
-
-
?
6-azido-4-(4-iodophenethylamino)quinazoline-labeled 49 kDa subunit of NADH-ubiquinone oxidoreductase + H2O
?
-
proteolytic mapping of the 49 kDa subunit with V8-protease, cleavage within the sequence region Asp41-Arg63: fragment A is predicted to be the peptide Thr25-Glu248, 224 amino acids, 26.0 kDa, which is further cleaved at Glu143 and give fragment B, Thr25-Glu143, 118 amino acids, overview
-
-
?
Abz-Ala-Phe-Ala-Phe-Glu-Val-Phe-(NO2)-Tyr-Asp + H2O
Abz-Ala-Phe-Ala-Phe-Glu + Val-Phe-(NO2)-Tyr-Asp
-
-
-
?
acetyl-Glu-4-nitrophenyl + H2O
acetyl-Glu + 4-nitrophenol
-
-
-
?
acetyl-Glu-4-nitrophenyl ester + H2O
acetyl-Glu + 4-nitrophenol
-
-
-
?
alpha1-antitrypsin + H2O
?
-
6-bromomethyl-2-(2-furanyl)-3-hydroxychromone-labeled substrate, V8 proteinase-induced cleavage of the reactive center loop does not generate any significant change in the Cys-232 region, but inactivates the anti-PPE property of the substrate, interaction analysis, overview
-
-
?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O
benzyloxycarbonyl-Ala + 2-carboxyphenylthiol
-
-
-
?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O
benzyloxycarbonyl-Ala + 3-carboxyphenol
-
-
-
?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O
benzyloxycarbonyl-Ala + 3-hydroxybenzoate
-
-
-
?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O
benzyloxycarbonyl-Ala + 4-carboxyphenol
-
-
-
?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O
benzyloxycarbonyl-Ala + 4-hydroxybenzoate
-
-
-
?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O
benzyloxycarbonyl-Ala + carboxyethylthiol
-
-
-
?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O
benzyloxycarbonyl-Ala + carboxymethylthiol
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Glu + 4-nitroaniline
benzyloxycarbonyl-Ala-Ala-Glu-methyl ester + leucine * HCl
benzyloxycarbonyl-Ala-Ala-Glu-Leu + methanol
-
peptide synthesis
-
?
benzyloxycarbonyl-Ala-Ala-Leu-Asp-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Leu-Asp + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Leu-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Leu-Glu + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Met-Asp-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Met-Asp + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Met-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Met-Glu + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Phe-Asp-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Phe-Asp + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Phe-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Phe-Glu + 4-nitroaniline
benzyloxycarbonyl-Ala-Ala-Trp-Asp-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Trp-Asp + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Trp-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Trp-Glu + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Glu-methyl ester + leucine * HCl
benzyloxycarbonyl-Ala-Glu-Leu + methanol
-
peptide synthesis
-
?
benzyloxycarbonyl-Ala-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Leu-Glu + p-nitroaniline
benzyloxycarbonyl-Asp-methyl ester + Ala-Ala-D-hydroxyalanine
benzyloxycarbonyl-Asp-Ala-Ala-D-hydroxyalanine + methanol
-
peptide synthesis, low activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + Ala-Ala-hydroxyproline
benzyloxycarbonyl-Asp-Ala-Ala-hydroxyproline + methanol
-
peptide synthesis, lower activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + Ala-D-hydroxyalanine
benzyloxycarbonyl-Asp-Ala-D-hydroxyalanine + methanol
-
peptide synthesis, very low activity at 25°C, but moderate activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyaspartate
benzyloxycarbonyl-Asp-Ala-hydroxyaspartate + methanol
-
peptide synthesis, low activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyglutamate
benzyloxycarbonyl-Asp-Ala-hydroxyglutamate + methanol
-
peptide synthesis, very low activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + Ala-hydroxyproline
benzyloxycarbonyl-Asp-Ala-hydroxyproline + methanol
-
peptide synthesis, no activity at 25°C, only low activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + Asp-Gly
benzyloxycarbonyl-Asp-Asp-Gly + methanol
-
peptide synthesis, no activity at 25°C, but moderate activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + aspartate
benzyloxycarbonyl-Asp-Asp + methanol
-
peptide synthesis, no activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + Glu-Gly
benzyloxycarbonyl-Asp-Glu-Gly + methanol
-
peptide synthesis, no activity at 25°C, but moderate activity at -15°C
-
?
benzyloxycarbonyl-Asp-methyl ester + glutamate
benzyloxycarbonyl-Asp-Glu + methanol
-
peptide synthesis, no activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Glu methylthioester + H2O
benzyloxycarbonyl-Glu + methylthiol
-
-
-
?
benzyloxycarbonyl-Glu methylthioester + H2O
benzyloxycarbonyl-L-Glu + methylthiol
-
-
-
?
benzyloxycarbonyl-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Glu + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Glu-methyl ester + Ala-Ala-D-Ala
benzyloxycarbonyl-Glu-Ala-Ala-D-Ala + methanol
-
peptide synthesis, low activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + Ala-Ala-Pro
benzyloxycarbonyl-Glu-Ala-Ala-Pro + methanol
-
peptide synthesis, lower activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + Ala-Asp
benzyloxycarbonyl-Glu-Ala-Asp + methanol
-
peptide synthesis, no activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + Ala-D-Ala
benzyloxycarbonyl-Glu-Ala-D-Ala + methanol
-
peptide synthesis, no activity at 25°C, but moderate activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + Ala-Glu
benzyloxycarbonyl-Glu-Ala-Glu + methanol
-
peptide synthesis, no activity at 25°C, but high activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + Ala-Pro
benzyloxycarbonyl-Glu-Ala-Pro + methanol
-
peptide synthesis, no activity at 25°C, only low activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + Asp-Gly
benzyloxycarbonyl-Glu-Asp-Gly + methanol
-
peptide synthesis, no activity at 25°C, but moderate activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + Glu-Gly
benzyloxycarbonyl-Glu-Glu-Gly + methanol
-
peptide synthesis, no activity at 25°C, but low activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + L-aspartate
benzyloxycarbonyl-Glu-Asp + methanol
-
peptide synthesis, no activity at 25°C, but moderate activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + L-glutamate
benzyloxycarbonyl-Glu-Glu + methanol
-
peptide synthesis, no activity at 25°C, but moderate activity at -15°C
-
?
benzyloxycarbonyl-Glu-methyl ester + L-tryptophan
benzyloxycarbonyl-Glu-Trp + methanol
-
peptide synthesis
-
?
benzyloxycarbonyl-Glu-methyl ester + Leu-Gly
benzyloxycarbonyl-Glu-Leu-Gly + methanol
-
peptide synthesis
-
?
benzyloxycarbonyl-Glu-methyl ester + leucine
benzyloxycarbonyl-Glu-Leu + methanol
-
peptide synthesis
-
?
benzyloxycarbonyl-Glu-methyl ester + Phe-Gly
benzyloxycarbonyl-Glu-Phe-Gly + methanol
-
peptide synthesis
-
?
benzyloxycarbonyl-Gly-Ala-Ala-Asp-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Ala-Ala-Asp + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-Ala-Ala-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Ala-Ala-Glu + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-L-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-L-Glu + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Leu-Leu-Glu + p-nitroaniline
benzyloxycarbonyl-Phe-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
benzyloxycarbonyl-Pro-Leu-Gly-S-CH2-COOH + LAFARAEAFG
benzyloxycarbonyl-PLGLAFARAEAFG + HS-CH2-COOH
-
acylation of peptide fragment by substrate mimetic
product formation 55%
?
benzyloxycarbonyl-S-CH2-COOH + LAFARAEAF-hydroxyglycine
benzyloxycarbonyl-LAFARAEAF-hydroxyglycine + HS-CH2-COOH
-
acylation of peptide fragment by substrate mimetic
product formation 99%
?
beta-type parvalbumin + H2O
peptide fragments
-
from the frog Rana catesbeiana
mass spectrometry for identification
?
bovine hemoglobin + H2O
peptide fragments
-
in presence of SDS
peptide mapping, 2 peptide fragments are Leu76-Pro-Gly-Ala-Leu-Ser-Glu82 and Lys94-Leu-His-Val-Asp-Pro-Glu100
?
bovine insulin + H2O
bovine insulin peptide fragments
-
-
mass spectrometric identification, detailed overview
-
?
carboxymethylated yeast alcohol dehydrogenase + H2O
?
-
-
5 different peptides containing the residues 5-13. 14-19, 68-77, 102-104, 105-108
?
CXCR4-T140 + H2O
?
-
T140 photolabeled CXCR4, a G-protein-coupled receptor, containing the photoreactive amino acid 4-benzoyl-L-phenylalanine, Bpa, in positions 5 or 10. V8 protease digestion of both CXCR4/125I-[Bpa5]T140 and CXCR4/125I-[Bpa10]T140 adducts generates a fragment of 6 kDa suggesting that the T140 photoanalogs labeled a fragment corresponding to Lys154-Glu179 of the receptors 4th transmembrane domain
-
-
?
GluV8 + H2O
?
-
degradation of the C-terminus at the Glu279-Asp280 bond is suspected to be a result from autoproteolysis
38 kDa species
-
?
glycosylated bovine insulin + H2O
glycosylated bovine insulin peptide fragments
-
three differently glycosylated substrate forms
mass spectrometric identification, detailed overview
-
?
hemocyanin + H2O
peptide fragments
-
hydrolysis of 2 isozymes of hemocyanin KLH1 and KLH2 from shellfish Megatura crenulata at Glu-Xaa and Asp-Xaa bonds
-
?
human hemoglobin + H2O
?
-
slpicedon consisting of a flanking region FR1, the EALER sequence, and a flanking region FR2, splicing reaction at E30-R31, facilitated by organic co-solvent-induced secondary conformation of alpha17-40 within which the sequence EALER plays a major role
-
?
insulin A-chain + H2O
peptide fragments
-
hydrolysis of Glu4-Gln5, Glu17-Asp18, and Cys11-Ser12
-
?
insulin B-chain + H2O
peptide fragments
-
hydrolysis of Glu13-Ala14, Glu21-Arg22, Cys7-Gly8, and Cys19-Gly20
-
?
insulin-like growth factor binding protein-1 + H2O
insulin-like growth factor binding protein-1 peptide fragments
-
from human decidual cells during gestation. The phosphorylation state influences the propensity of IGFBP-1 to proteolysis, overview. Generation of Glu C peptides by V8 protease, overview
identification of Glu C peptides, overview
-
?
LHCH N-terminal peptide + H2O
?
-
N-terminal loop and first turn in helix B of light-harvesting complex II from pea
-
-
?
N-acetyl-L-Glu-4-nitroanilide + H2O
N-acetyl-L-Glu + 4-nitroaniline
-
-
-
-
?
N-benzyloxycarbonyl-alpha-glutamic-p-nitroanilide + H2O
N-benzyloxycarbonyl-alpha-glutamic acid + p-nitroaniline
-
-
-
?
N-benzyloxycarbonyl-L-glutamyl-p-nitroanilide + H2O
N-benzyloxycarbonyl-L-glutamate + p-nitroaniline
-
-
-
?
N-tert-butyloxycarbonyl-L-Glu-alpha-phenyl ester + H2O
butyloxycarbonyl-L-Glu + phenol
-
-
-
?
Nile Red-dyed microsphere based on polypeptides PLL and PLGA as shell materials + H2O
Nile Red + degraded microsphere based on polypeptides PLL and PLGA as shell materials
-
-
-
-
?
p-aminobenzoyl-Ala-Phe-Ala-Phe-Glu-Val-Phe-Tyr(NO2)-Asp + H2O
p-aminobenzoyl-Ala-Phe-Ala-Phe-Glu + Val-Phe-Tyr(NO2)-Asp
-
-
-
-
?
t-butyloxycarbonyl-Ala-Ala-Asp-p-nitroanilide + H2O
t-butyloxycarbonyl-Ala-Ala-Asp + p-nitroaniline
t-butyloxycarbonyl-Ala-Ala-Glu-p-nitroanilide + H2O
t-butyloxycarbonyl-Ala-Ala-Glu + p-nitroaniline
tert-butyloxycarbonyl-Ala-Ala-Pro-Glu-4-nitroanilide + H2O
tert-butyloxycarbonyl-Ala-Ala-Pro-Glu + 4-nitroaniline
-
-
-
?
Ac-Ala-Ala-Asn-4-methylcoumaryl-7-amide + H2O
?
-
the C-terminal tripeptide of the prosequence of GluV8 (i.e., His66-Ala-Asn68) resembles the unprocessed GluV8 cleavable substrate Ac-Ala-Ala-Asn-4-methylcoumaryl-7-amide
-
-
?
Ac-Ala-Ala-Asn-4-methylcoumaryl-7-amide + H2O
?
-
the C-terminal tripeptide of the prosequence of GluV8 (i.e., His66-Ala-Asn68) resembles the unprocessed GluV8 cleavable substrate Ac-Ala-Ala-Asn-4-methylcoumaryl-7-amide
-
-
?
alpha-casein + H2O
?
-
the enzyme hydrolyses Glu(51)-Tyr(52) and Glu(50)-Glu(51) in Glu(49)-Glu(50)-Glu(51)-Tyr(52) of bovine alphs1-casein
-
-
?
alpha-casein + H2O
?
-
the enzyme is highly specific and hydrolyses the peptide bond predominantly on the carboxy side of Glu residues while hydrolysis on the carboxyl side of Asp residues is also observed. Hydrolysis does not occur while Pro is at the P1' position. In Glu-Glu-X (X equals Arg, Asn, Ile and Ser) and Glu-Glu-Glu-Lys sequences, hydrolysis of Glu-X and Glu-Lys is preferred
-
-
?
Arg-Lys-Asp-Val-Tyr + H2O
Arg-Lys-Asp + Val-Tyr
-
only 5.6% hydrolysis of the Asp-Val bond
-
?
Arg-Lys-Glu-Val-Tyr + H2O
Arg-Lys-Glu + Val-Tyr
-
completely splits Glu-Val bond, after 30 min
-
?
Arg-Lys-Glu-Val-Tyr + H2O
Arg-Lys-Glu + Val-Tyr
-
completely splits Glu-Val bond, after 30 min
-
?
Arg-Lys-Glu-Val-Tyr + H2O
Arg-Lys-Glu + Val-Tyr
-
completely splits Glu-Val bond, after 30 min
-
?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala-Ala-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Glu + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Glu + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-Phe-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Phe-Glu + 4-nitroaniline
-
preferred peptide substrate
-
?
benzyloxycarbonyl-Ala-Ala-Phe-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala-Phe-Glu + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Leu-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Leu-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Asp methyl ester + H2O
benzyloxycarbonyl-Asp + methanol
-
-
-
?
benzyloxycarbonyl-Asp methyl ester + H2O
benzyloxycarbonyl-Asp + methanol
-
-
-
?
benzyloxycarbonyl-Glu methyl ester + H2O
benzyloxycarbonyl-Glu + methanol
-
-
-
?
benzyloxycarbonyl-Glu methyl ester + H2O
benzyloxycarbonyl-Glu + methanol
-
-
-
?
benzyloxycarbonyl-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Leu-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Leu-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Leu-Leu-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Leu-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Leu-Leu-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
35% of the efficiency with succinyl-Ala-Ala-Pro-Glu-p-nitroanilide
-
-
?
benzyloxycarbonyl-Phe-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
35% of the efficiency with succinyl-Ala-Ala-Pro-Glu-p-nitroanilide
-
-
?
benzyloxycarbonyl-Phe-Leu-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Phe-Leu-Glu + p-nitroaniline
-
-
-
-
?
beta-casein + H2O
?
-
the enzyme is highly specific and hydrolyzes peptide bonds in beta-casein predominantly on the carboxy-terminal of Glu and Asp. Pro residues are not preferred, while Met is poorly preferred at the P1' position. Glu-Met hydrolysis is less preferred in comparison to Asp-Met hydrolysis
-
-
?
bovine myelin basic protein + H2O
?
-
cleavage of native myelin basic protein at Gly127-Gly128 and of carboxymethylated myelin basic protein at Phe124-Gly125
-
-
?
bovine myelin basic protein + H2O
?
-
cleavage of native myelin basic protein at Gly127-Gly128 and of carboxymethylated myelin basic protein at Phe124-Gly125
-
-
?
equine beta-casein + H2O
equine beta-casein peptide fragments
-
different isoforms
product analysis by mass spectrometry, overview
-
?
equine beta-casein + H2O
equine beta-casein peptide fragments
-
different isoforms
product analysis by mass spectrometry, overview
-
?
human parathyroid hormone(13-34) + H2O
peptides
-
-
peptide fragments Lys1-Glu7, Arg8-Glu10 and Trp11-Phe22 are produced after 6 min
?
human parathyroid hormone(13-34) + H2O
peptides
-
-
peptide fragments Lys1-Glu6, Arg8-Glu10 and Lys1-Glu10 are produced after 6 min
?
L-Phe-L-Leu-L-Glu-4-nitroanilide + H2O
L-Phe-L-Leu-L-Glu + 4-nitroaniline
-
i.e. L-2135
-
-
?
L-Phe-L-Leu-L-Glu-4-nitroanilide + H2O
L-Phe-L-Leu-L-Glu + 4-nitroaniline
-
i.e. L-2135
-
-
?
Oxidized insulin B-chain + H2O
?
-
cleavage occurs at Glu13-Ala14 and Glu21-Arg22
-
-
?
pore-forming alpha-toxin + H2O
pore-forming alpha-toxin peptide fragments
-
limited proteolysis with V8 protease
product identification, eight or more fragments are produced by V8 treatment, cleavage pattern, overview
-
?
pore-forming alpha-toxin + H2O
pore-forming alpha-toxin peptide fragments
-
limited proteolysis with V8 protease
product identification, eight or more fragments are produced by V8 treatment, cleavage pattern, overview
-
?
prothrombin + H2O
?
-
the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin
-
-
?
prothrombin + H2O
?
-
the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin
-
-
?
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Glu + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Glu + p-nitroaniline
-
-
-
?
succinyl-Ala-Ala-Pro-Glu-p-nitroanilide + H2O
succinyl-Ala-Ala-Pro-Glu + p-nitroaniline
-
-
-
-
?
t-butyloxycarbonyl-Ala-Ala-Asp-p-nitroanilide + H2O
t-butyloxycarbonyl-Ala-Ala-Asp + p-nitroaniline
-
-
-
-
?
t-butyloxycarbonyl-Ala-Ala-Asp-p-nitroanilide + H2O
t-butyloxycarbonyl-Ala-Ala-Asp + p-nitroaniline
-
-
-
-
?
t-butyloxycarbonyl-Ala-Ala-Glu-p-nitroanilide + H2O
t-butyloxycarbonyl-Ala-Ala-Glu + p-nitroaniline
-
-
-
-
?
t-butyloxycarbonyl-Ala-Ala-Glu-p-nitroanilide + H2O
t-butyloxycarbonyl-Ala-Ala-Glu + p-nitroaniline
-
-
-
-
?
Z-Ala-Ala-Asn-4-methylcoumaryl-7-amide + H2O
?
-
GluV8 also possesses trace activity toward Z-Ala-Ala-Asn-4-methylcoumaryl-7-amide that is at least 30fold higher than the activity for residual 4-methylcoumaryl-7-amide peptides that carried Ala, Phe, or Leu at their P1 position
-
-
?
Z-Ala-Ala-Asn-4-methylcoumaryl-7-amide + H2O
?
-
GluV8 also possesses trace activity toward Z-Ala-Ala-Asn-4-methylcoumaryl-7-amide that is at least 30fold higher than the activity for residual 4-methylcoumaryl-7-amide peptides that carried Ala, Phe, or Leu at their P1 position
-
-
?
additional information
?
-
-
splitting of peptide bonds of Glu and rarely of Asp in peptides and proteins
-
-
?
additional information
?
-
-
substrate specificity, preferrence for Glu-cleavage site before Asp-cleavage site
-
?
additional information
?
-
-
no cleavage of certain substrates of chymotrypsin
-
-
?
additional information
?
-
enzyme suspected to be involved in the outgrowth of spores when the germinating endospore converts into the vegetative cell
-
-
?
additional information
?
-
-
enzyme suspected to be involved in the outgrowth of spores when the germinating endospore converts into the vegetative cell
-
-
?
additional information
?
-
splits specifically the peptide bonds formed by alpha-carboxyl groups of glutamic and, and to a lesser extent, of aspartic acid
-
-
?
additional information
?
-
-
splits specifically the peptide bonds formed by alpha-carboxyl groups of glutamic and, and to a lesser extent, of aspartic acid
-
-
?
additional information
?
-
-
splitting of peptide bonds of Glu and rarely of Asp in peptides and proteins
-
-
?
additional information
?
-
-
enzyme also performs acyl-transfer reactions with substrate mimetics carboxymethyl acylthioester, carboxyethyl acylthioester, 2-carboxyphenyl acylthioester, 3-carboxyphenyl acylester, 4-carboxyphenyl acylester
-
?
additional information
?
-
-
no peptide synthesis activity with proline and D-leucine, active in semienzymatic synthesis of human growth hormone
-
?
additional information
?
-
-
cleaves specifically the peptide bonds on the carboxyl-terminal side of either Asp or Glu residues in phosphate buffer - pH 7.8, hydrolyzes only glutamoyl bonds - in either ammonium bicarbonate at pH 7.8 or ammonium acetate at pH 4.0. - of all aspartoyl bonds tested, only the Asp-Gly linkage is cleaved at a detectable rate. The enzyme hydrolyzes all of the 16 different glutamoyl bonds studied, although those involving hydrophobic amino acid residues with bulky side chains are cleaved at a lower rate
-
-
?
additional information
?
-
-
specifically cleaves peptide bonds on the COOH-terminal side of either aspartic acid or glutamic acid. Casein in which all carboxyl groups have been blocked with glycine ethyl ester in amide linkage is not hydrolyzed
-
-
?
additional information
?
-
-
enzyme also performs acyl-transfer reactions with substrate mimetics carboxymethyl acylthioester, carboxyethyl acylthioester, 2-carboxyphenyl acylthioester, 3-carboxyphenyl acylester, 4-carboxyphenyl acylester
-
?
additional information
?
-
-
splicing activity and specificity of the enzyme with complementary segments of human hemoglobin fragment alpha17-40, constructed by engineering of the primary structure, structural implications, overview
-
?
additional information
?
-
-
substrate specificity is pH-dependent due to active site His213, peptide synthesizing substrate specificity, no peptide synthesizing activity with benzyloxycarbonyl-Asp-methyl ester
-
?
additional information
?
-
-
the positively charged N-terminus is involved in determination of substrate specificity
-
?
additional information
?
-
-
specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp, key role in degrading the cell-bound Staphylococcus surface adhesion molecules of fibronectin-binding proteins and protein A
-
-
?
additional information
?
-
-
the specificity of endoproteinase Glu-C for glutamic acid depends on the pH
-
-
?
additional information
?
-
-
V8 is a very substrate-specific extracellular endopeptidase that cleaves peptide bonds on the carbonyl side of glutamate and aspartate
-
-
?
additional information
?
-
the enzyme shows little or no degradation of galectin-3
-
-
?
additional information
?
-
-
the enzyme shows little or no degradation of galectin-3
-
-
?
additional information
?
-
the enzyme shows little or no degradation of galectin-3
-
-
?
additional information
?
-
-
cleaves specifically the peptide bonds on the carboxyl-terminal side of either Asp or Glu residues in phosphate buffer - pH 7.8, hydrolyzes only glutamoyl bonds - in either ammonium bicarbonate at pH 7.8 or ammonium acetate at pH 4.0. - of all aspartoyl bonds tested, only the Asp-Gly linkage is cleaved at a detectable rate. The enzyme hydrolyzes all of the 16 different glutamoyl bonds studied, although those involving hydrophobic amino acid residues with bulky side chains are cleaved at a lower rate
-
-
?
additional information
?
-
-
specifically cleaves peptide bonds on the COOH-terminal side of either aspartic acid or glutamic acid. Casein in which all carboxyl groups have been blocked with glycine ethyl ester in amide linkage is not hydrolyzed
-
-
?
additional information
?
-
-
substrate specificity is pH-dependent due to active site His213, peptide synthesizing substrate specificity, no peptide synthesizing activity with benzyloxycarbonyl-Asp-methyl ester
-
?
additional information
?
-
-
specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp
-
-
?
additional information
?
-
-
distinct preference for Glu, characterization of the S1 binding site
-
-
?
additional information
?
-
-
the enzyme specifically hydrolyzes peptide bonds formed by alpha-carboxyl groups of Glu and Asp residues. Glu-Xaa bonds are cleaved much more efficiently than Asp-Xaa bonds
-
-
?
