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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
-
-
-
?
Ac-Ala-Ala-Asn-4-methylcoumaryl-7-amide + H2O
?
acetyl-Asp-p-nitroanilide + H2O
acetyl-Glu + p-nitroaniline
acetyl-Glu-4-nitrophenyl + H2O
acetyl-Glu + 4-nitrophenol
-
-
-
?
acetyl-Glu-4-nitrophenyl ester + H2O
acetyl-Glu + 4-nitrophenol
-
-
-
?
acetyl-Glu-p-nitroanilide + H2O
acetyl-Glu + p-nitroaniline
Ala-Glu-4-methylcoumaryl-7-amide + H2O
?
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
-
-
?
Arg-Lys-Asp-Val-Tyr + H2O
Arg-Lys-Asp + Val-Tyr
Arg-Lys-Glu-Val-Tyr + H2O
Arg-Lys-Glu + Val-Tyr
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O
?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O
benzyloxycarbonyl-Ala + 2-carboxyphenylthiol
-
-
-
?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O
?
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-carboxyphenylester + H2O
benzyloxycarbonyl-Ala + 4-carboxyphenol
-
-
-
?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O
benzyloxycarbonyl-Ala + 4-hydroxybenzoate
-
-
-
?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O
?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O
benzyloxycarbonyl-Ala + carboxyethylthiol
-
-
-
?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O
?
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-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-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 + 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 methyl ester + H2O
benzyloxycarbonyl-Glu + methanol
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-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
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-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-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-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
-
?
bovine myelin basic protein + H2O
?
Bovine serum albumin + H2O
?
-
-
-
-
?
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
-
-
?
equine beta-casein + H2O
equine beta-casein peptide fragments
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
-
?
human parathyroid hormone(13-34) + H2O
peptides
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
-
?
L-Phe-L-Leu-L-Glu-4-nitroanilide + H2O
L-Phe-L-Leu-L-Glu + 4-nitroaniline
Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
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
-
-
-
-
?
ovalbumin + H2O
?
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
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
-
-
-
-
?
pore-forming alpha-toxin + H2O
pore-forming alpha-toxin peptide fragments
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-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
-
-
-
?
Z-Ala-Ala-Asn-4-methylcoumaryl-7-amide + H2O
?
Z-Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
Z-Leu-Leu-Glu-MCA + H2O
?
additional information
?
-
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
-
-
?
acetyl-Asp-p-nitroanilide + H2O
acetyl-Glu + p-nitroaniline
-
-
-
-
?
acetyl-Asp-p-nitroanilide + H2O
acetyl-Glu + p-nitroaniline
-
-
-
-
?
acetyl-Glu-p-nitroanilide + H2O
acetyl-Glu + p-nitroaniline
-
-
-
-
?
acetyl-Glu-p-nitroanilide + H2O
acetyl-Glu + p-nitroaniline
-
-
-
-
?
Ala-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Ala-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Ala-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
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
-
-
-
?
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
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O
?
-
-
-
?
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
?
-
-
-
?
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
?
-
-
-
?
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
-
-
?
beta-casein + H2O
?
-
-
-
-
?
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
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
alphaS-casein and beta-casein
-
-
?
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
-
?
Glucagon + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
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
?
insulin + H2O
?
-
A-chain and B-chain
-
-
?
insulin + H2O
?
-
A-chain and B-chain
-
-
?
insulin + H2O
?
-
A-chain and B-chain
-
-
?
insulin + H2O
?
-
A-chain and B-chain
-
-
?
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
-
-
?
Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Lysozyme + H2O
?
-
-
-
-
?
Lysozyme + H2O
?
-
-
-
-
?
Oxidized insulin B-chain + H2O
?
-
-
cleavage of bond E13-A14
-
?
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
-
-
?
Ribonuclease + H2O
?
-
-
-
-
?
Ribonuclease + H2O
?
-
-
-
-
?
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
-
-
?
Z-Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Z-Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Z-Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Z-Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Z-Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
Z-Leu-Leu-Glu-MCA + H2O
?
-
-
-
-
?
Z-Leu-Leu-Glu-MCA + H2O
?
-
-
-
-
?
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
-
-
?
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H186T
-
no effect on enzyme specificity, 4.9fold increase in KM-value, 600fold decrease in kcat-value
DELTA1-48
-
the 38 and 40 kDa mature forms are obtained after thermolysin treatment
DELTA1-55
-
the 38 and 40 kDa mature forms are obtained after thermolysin treatment
DELTA1-60
-
the 38 and 40 kDa mature forms are obtained after thermolysin treatment
DELTA1-62
-
the 38 and 40 kDa mature forms are obtained after thermolysin treatment
DELTA1-64
-
poor expression in Escherichia coli, resulting enzyme thoroughly degraded upon thermolysin treatment, very low activity
DELTA1-65
-
poor expression in Escherichia coli, resulting enzyme thoroughly degraded upon thermolysin treatment, activity hardly detectable
E62Q/E65S
-
mutation prevent degradation of protein, slightly accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli
E62Q/E65S/A67P/N68P
-
efficient suppression of proteolysis, strongly accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli
G176E/Q179E/Y185W/D189P/K191E/Y192F/S194G/S195A
-
GluV8DELTAC, the C-terminal 52 residues are deleted
S237A
-
mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, no proteinolytic activity
S66R
-
insertion of a trypsin degradable sequence, successful enzyme processing by trypsin instead of thermolysin, enhanced Glu-specific activity
V69A
-
mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity
V69F
-
mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity
V69G
-
mutation introduced into the fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, normal processing of propeptide to mature protein, no proteinolytic activity
K191E/Y192F/S194G/S195A
-
GluSE-EFGA
N190H/Y192H/S169A
-
the specific activity of the mutant is 4.5fold increased from that of the wild type enzyme. The mutant potently hydrolyzes LLE-7-amido-4-methylcomarin
S66R/V69A
-
insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 4.5% of activity compared with the Val69 native form
S66R/V69F
-
insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 1.4% of activity compared with the Val69 native form
S66R/V69G
-
insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 1.1% of activity compared with the Val69 native form
S66R/V69S
-
insertion of a trypsin degradable sequence at position 66, successful enzyme processing by trypsin instead of thermolysin, 0.6% of activity compared with the Val69 native form
Y185W/D189P
-
the activity of GluSE with the two substitutions, i.e., Y185W and D189P (designated GluSE-WP), is equivalent to that of GluSE-WPEFGA
Y185W/D189P/K191E/Y192F/S194G/S195A
-
GluSE/WPEFGA
N190H/Y192H/S169A
-
the specific activity of the mutant is 4.5fold increased from that of the wild type enzyme. The mutant potently hydrolyzes LLE-7-amido-4-methylcomarin
-
H199V
-
change in the substrate preference, with a 16fold increase in the ratio of turnover number to Km-value with substrates with Phe in P1, and a 20fold increase with substrates with Glu in P1. Substitution of His199 by anything except Val completely abolishes the production of mature enzyme
H228A
-
change in substrate specificity, i.e., a slight increase in the ratio of turnover-number to Km-value for the substrate with Asp and a more than 300-fold increase in this ratio when P1 substituent is Ala
S216A
-
about 7.5fold increase in Km-value for hydrolysis of succinyl-Ala-Ala-Pro-Glu-p-nitroanilide compared to the wild-type enzyme
S216G
-
about 7.5fold increase in Km-value for hydrolysis of succinyl-Ala-Ala-Pro-Glu-p-nitroanilide compared to the wild-type enzyme
S168C
-
the mutant does not show proteolytic and azocaseinolytic activity
additional information
-
mutations within the amino acid sequence alpha17-40 influence the organic co-solvent-induced conformation and concomittant resistance of E30-R31 peptide bond to cleavage occurs, alteration of the thermaldynamic stability of the splicedon, the flanking regions are involved in stabilization
additional information
-
mature protein sequence is fused with the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, suppression of protein degradation, accelerated proliferation rate compared with wild type enzyme when expressed in Escherichia coli
additional information
-
chimera A carries the N-terminal half of GluV8 (positions 1-118) and C-terminal half of GluSE (positions 119-216), chimera B carries GluV8, in which the third quarter from the N-terminus (positions 119-169) is replaced by the sequence of GluSE, chimera C carries GluV8, in which the C-terminal quarter (positions 170-216) is replaced by the sequence of GluSE, and Chimera D carries GluV8, in which the seventh part of 8 portions (positions 170-195) is replaced by the sequence of GluSE. The chimeric proteases as well as GluSE, GluV8, and GluV8DELTAC are converted to their mature forms by thermolysin treatment. When the 6 amino acids of GluSE are simultaneously replaced by those of GluV8, i.e., Y185W, D189P, L191E, Y192F, S194G, and S195A (designated GluSE-WPEFGA), the proteolytic activity of GluSE-WPEFGA becomes 3.8fold higher than that of GuV8DELTAC, in accordance with the super-activity of chimera B
additional information
-
GluV8mut5, full-length GluV8 with five substitutions (Asp36His/Glu62Gln/Glu65Ser/Ala67Pro/Asn68Ser) in the prosegment, GluV8mut5DELTAC, GluV8mut5 with C-terminal 52 residues deleted, GluV8mut4nCSer237Ala, GluV8mut4nC with an amino acid substitution (Ser237Ala), GluV8mut5-SW, prepro-GluV8mut5 attached to mature GluSW
additional information
-
GluV8mut5, full-length GluV8 with five substitutions (Asp36His/Glu62Gln/Glu65Ser/Ala67Pro/Asn68Ser) in the prosegment, GluV8mut5DELTAC, GluV8mut5 with C-terminal 52 residues deleted, GluV8mut4nCSer237Ala, GluV8mut4nC with an amino acid substitution (Ser237Ala), GluV8mut5-SW, prepro-GluV8mut5 attached to mature GluSW
-
additional information
-
chimera A carries the N-terminal half of GluV8 (positions 1-118) and C-terminal half of GluSE (positions 119-216), chimera B carries GluV8, in which the third quarter from the N-terminus (positions 119-169) is replaced by the sequence of GluSE, chimera C carries GluV8, in which the C-terminal quarter (positions 170-216) is replaced by the sequence of GluSE, and Chimera D carries GluV8, in which the seventh part of 8 portions (positions 170-195) is replaced by the sequence of GluSE. The chimeric proteases as well as GluSE, GluV8, and GluV8DELTAC are converted to their mature forms by thermolysin treatment. When the 6 amino acids of GluSE are simultaneously replaced by those of GluV8, i.e., Y185W, D189P, L191E, Y192F, S194G, and S195A (designated GluSE-WPEFGA), the proteolytic activity of GluSE-WPEFGA becomes 3.8fold higher than that of GuV8DELTAC, in accordance with the super-activity of chimera B. GluSE/SW is composed of amino acids -66 to 169 of GluSE, which carried a putative proteolytic resistant region (residues 119-169) and amino acids 170-250 of GluSW. Activity of GluSE/SW becomes 4fold and 2fold higher than that of GluSE and GluSW
additional information
-
GluSE/SW is composed of amino acids -66 to 169 of GluSE, which carried a putative proteolytic resistant region (residues 119-169) and amino acids 170-250 of GluSW. Activity of GluSE/SW becomes 4fold and 2fold higher than that of GluSE and GluSW
additional information
-
GluV8mut5-SW, prepro-GluV8mut5 attached to mature GluSW
additional information
-
GluV8mut5-SW, prepro-GluV8mut5 attached to mature GluSW
-
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Bjrklind, A.; Jrnvall, H.
Substrate specificity of three different extracellular proteolytic enzymes from Staphylococcus aureus
Biochim. Biophys. Acta
370
524-529
1974
Staphylococcus aureus
brenda
Houmard, J.; Drapeau, G.R.
Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds
Proc. Natl. Acad. Sci. USA
69
3506-3509
1972
Staphylococcus aureus, Staphylococcus aureus V8
brenda
Drapeau, G.R.; Boily, Y.; Houmard, J.
Purification and properties of an extracellular protease of Staphylococcus aureus
J. Biol. Chem.
247
6720-6726
1972
Staphylococcus aureus, Staphylococcus aureus V8
brenda
Leshchinskaya, L.B.; Shakirov, E.V.; Itskovitch, E.L.; Balaban, N.P.; Mardanova, A.M.; Sharipova, M.R.; Viryasov, M.B.; Rudenskaya, G.N.; Stepanov, V.M.
Glutamyl endopeptidase of Bacillus intermedius, strain 3-19
FEBS Lett.
404
241-244
1997
Bacillus intermedius, Bacillus intermedius Mrz 19
brenda
Stennicke, H.R.; Birktoft, J.J.; Breddam, K.
Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomyces griseus
Protein Sci.
5
2266-2275
1996
Streptomyces griseus
brenda
Sellinger, O.Z.; Wolfson, M.F.
Carboxylmethylation affects the proteolysis of myelin basic protein by Staphylococcus aureus V8 proteinase
Biochim. Biophys. Acta
1080
110-118
1991
Staphylococcus aureus, Staphylococcus aureus V8
brenda
Leshchinskaya, I.B.; Shakirov, E.V.; Itskovitch, E.L.; Balaban, N.P.; Mardanova, A.M.; Sharipova, M.R.; Blagova, E.V.; Levdikov, V.M.; Kuranova, I.P.; Rudenskaya, G.N.; Stepanov, V.M.
Glutamyl endopeptidase of Bacillus intermedius strain 3-19. Purification, properties, and crystallization
Biochemistry
62
903-908
1997
Bacillus intermedius, Bacillus intermedius Mrz 19
brenda
Park, O.; Allen, J.C.
Preparation of phosphopeptides derived from alpha s-casein and beta-casein using immobilized glutamic acid-specific endopeptidase and characterization of their calcium binding
J. Dairy Sci.
81
2858-2865
1998
Bacillus licheniformis
brenda
Kakudo, S.; Kikuchi, N.; Kitadokoro, K.; Fujiwaera, T.; Nakamura, E.; Okamoto, H.; Shin, M.; Tamaki, M.; Teraoka, H.; Tsuzuki, H.; Yoshida, N.
Purification, characterization, cloning, and expression of a glutamic acid-specific protease from Bacillus licheniformis ATCC 14580
J. Biol. Chem.
267
23782-23788
1992
Bacillus licheniformis, Staphylococcus aureus
brenda
Prasad, L.; Leduc, Y.; Hayakawa, K.; Delbaere, L.T.
The structure of a universally employed enzyme: V8 protease from Staphylococcus aureus
Acta Crystallogr. Sect. D
60
256-259
2004
Staphylococcus aureus
brenda
Meijers, R.; Blagova, E.V.; Levdikov, V.M.; Rudenskaya, G.N.; Chestukhina, G.G.; Akimkina, T.V.; Kostrov, S.V.; Lamzin, V.S.; Kuranova, I.P.
The crystal structure of glutamyl endopeptidase from Bacillus intermedius reveals a structural link between zymogen activation and charge compensation
Biochemistry
43
2784-2791
2004
Bacillus intermedius
brenda
Balaban, N.P.; Mardanova, A.M.; Sharipova, M.R.; Gabdrakhmanova, L.A.; Sokolova, E.A.; Garusov, A.V.; Milgotina, E.I.; Rudenskaya, G.N.; Leshchinskaya, I.B.
Isolation and characterization of glutamyl endopeptidase 2 from Bacillus intermedius 3-19
Biochemistry (Moscow)
68
1217-1224
2003
Bacillus intermedius, Bacillus intermedius Mrz 19
brenda
Wehofsky, N.; Wissmann, J.D.; Alisch, M.; Bordusa, F.
Engineering of substrate mimetics as novel-type substrates for glutamic acid-specific endopeptidases: design, synthesis, and application
Biochim. Biophys. Acta
1479
114-122
2000
Bacillus licheniformis, Staphylococcus aureus
brenda
Gabdrakhmanova, L.A.; Balaban, N.P.; Sharipova, M.R.; Kostrov, S.V.; Akimkina, T.V.; Rudenskaya, G.N.; Leshchinskaya, I.B.
Optimization of Bacillus intermedius glutamyl endopeptidase production by recombinant strain of Bacillus subtilis and localization of glutamyl endopeptidase in Bacillus subtilis cells
Enzyme Microb. Technol.
31
256-263
2002
Bacillus intermedius
-
brenda
Srinivasulu, S.; Acharya, A.S.
Product-conformation-driven ligation of peptides by V8 protease
Protein Sci.
11
1384-1392
2002
Staphylococcus aureus
brenda
Mil'gotina, E.I.; Voyushina, T.L.; Chestukhina, G.G.
Glutamyl endopeptidases: structure, function, and practical application
Russ. J. Bioorg. Chem.
29
511-522
2003
Bacillus subtilis, Bacillus licheniformis, Staphylococcus aureus, Streptomyces griseus, Staphylococcus aureus V8
-
brenda
Trachuk, L.A.; Shcheglov, A.S.; Milgotina, E.I.; Chestukhina, G.G.
In vitro maturation pathway of a glutamyl endopeptidase precursor from Bacillus licheniformis
Biochimie
87
529-537
2005
Bacillus licheniformis
brenda
Kawalec, M.; Potempa, J.; Moon, J.L.; Travis, J.; Murray, B.E.
Molecular diversity of a putative virulence factor: purification and characterization of isoforms of an extracellular serine glutamyl endopeptidase of Enterococcus faecalis with different enzymatic activities
J. Bacteriol.
187
266-275
2005
Enterococcus faecalis (Q47809), Enterococcus faecalis, Enterococcus faecalis OG1RF (Q47809)
brenda
Seeley, E.H.; Riggs, L.D.; Regnier, F.E.
Reduction of non-specific binding in Ga(III) immobilized metal affinity chromatography for phosphopeptides by using endoproteinase glu-C as the digestive enzyme
J. Chromatogr. B
817
81-88
2005
Staphylococcus aureus
brenda
Chastukhina, I.B.; Sharipova, M.R.; Gabdrakhmanova, L.A.; Balaban, N.P.; Safina, D.R.; Kostrov, S.V.; Rudenskaya, G.N.; Leshchinskaya, I.B.
The regulation of Bacillus intermedius glutamyl endopeptidase biosynthesis in the recombinant Bacillus subtilis strain AJ73 during sporulation
Microbiology
73
279-285
2004
Bacillus intermedius
-
brenda
Chastukhina, I.B.; Sharipova, M.R.; Gabdrakhmanova, L.A.; Balaban, N.P.; Kostrov, S.V.; Rudenskaya, G.N.; Leshchinskaya, I.B.
Peculiarities of the biosynthesis of Bacillus intermedius glutamyl endopeptidase in recombinant Bacillus subtilis cells during the stationary growth phase
Microbiology
74
32-39
2005
Bacillus intermedius
-
brenda
Forsberg, J.; Stroem, J.; Kieselbach, T.; Larsson, H.; Alexciev, K.; Engstroem, A.; Akerlund, H.
Protease activities in the chloroplast capable of cleaving an LHCII N-terminal peptide
Physiol. Plant.
123
21-29
2005
Pisum sativum
-
brenda
Demidyuk, I.V.; Romanova, D.V.; Nosovskaya, E.A.; Chestukhina, G.G.; Kuranova, I.P.; Kostrov, S.V.
Modification of substrate-binding site of glutamyl endopeptidase from Bacillus intermedius
Protein Eng. Des. Sel.
17
411-416
2004
Bacillus intermedius
brenda
Nemoto, T.K.; Ohara-Nemoto, Y.; Ono, T.; Kobayakawa, T.; Shimoyama, Y.; Kimura, S.; Takagi, T.
Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli
FEBS J.
275
573-587
2008
Staphylococcus aureus, Staphylococcus epidermidis
brenda
Shagimardanova, E.I.; Chastukhina, I.B.; Shamsutdinov, T.R.; Balaban, N.P.; Mardanova, A.M.; Kostrov, S.V.; Sharipova, M.R.
Heterologous expression of Bacillus intermedius gene of glutamyl endopeptidase in Bacillus subtilis strains defective in regulatory proteins
Microbiology
76
569-574
2007
Bacillus intermedius
-
brenda
Sharipova, M.R.; Shagimardanova, E.I.; Chastukhina, I.B.; Shamsutdinov, T.R.; Balaban, N.P.; Mardanova, A.M.; Rudenskaya, G.N.; Demidyuk, I.V.; Kostrov, S.V.
The expression of Bacillus intermedius glutamyl endopeptidase gene in Bacillus subtilis recombinant strains
Mol. Biol. Rep.
34
79-87
2007
Bacillus intermedius (Q9EXR9), Bacillus intermedius
brenda
Ono, T.; Nemoto, T.K.; Shimoyama, Y.; Kimura, S.; Ohara-Nemoto, Y.
An Escherichia coli expression system for glutamyl endopeptidases optimized by complete suppression of autodegradation
Anal. Biochem.
381
74-80
2008
Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus warneri, Staphylococcus warneri JCM 2415, Staphylococcus aureus V8
brenda
Ohara-Nemoto, Y.; Ono, T.; Shimoyama, Y.; Kimura, S.; Nemoto, T.K.
Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis
Biol. Chem.
389
1209-1217
2008
Staphylococcus epidermidis (P0C0Q1), Staphylococcus epidermidis
brenda
Nemoto, T.K.; Ono, T.; Shimoyama, Y.; Kimura, S.; Ohara-Nemoto, Y.
Determination of three amino acids causing alteration of proteolytic activities of staphylococcal glutamyl endopeptidases
Biol. Chem.
390
277-285
2008
Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus warneri
brenda
Gasanov, E.V.; Demidyuk, I.V.; Shubin, A.V.; Kozlovskiy, V.I.; Leonova, O.G.; Kostrov, S.V.
Hetero- and auto-activation of recombinant glutamyl endopeptidase from Bacillus intermedius
Protein Eng. Des. Sel.
21
653-658
2008
Bacillus intermedius (Q9EXR9), Bacillus intermedius
brenda
Boulais, P.E.; Dulude, D.; Cabana, J.; Heveker, N.; Escher, E.; Lavigne, P.; Leduc, R.
Photolabeling identifies transmembrane domain 4 of CXCR4 as a T140 binding site
Biochem. Pharmacol.
78
1382-1390
2009
Staphylococcus aureus
brenda
Murai, M.; Sekiguchi, K.; Nishioka, T.; Miyoshi, H.
Characterization of the inhibitor binding site in mitochondrial NADH-ubiquinone oxidoreductase by photoaffinity labeling using a quinazoline-type inhibitor
Biochemistry
48
688-698
2009
Staphylococcus aureus
brenda
Tubby, S.; Wilson, M.; Nair, S.P.
Inactivation of staphylococcal virulence factors using a light-activated antimicrobial agent
BMC Microbiol.
9
211
2009
Staphylococcus aureus
brenda
Dolcini, L.; Sala, A.; Campagnoli, M.; Labo, S.; Valli, M.; Visai, L.; Minchiotti, L.; Monaco, H.L.; Galliano, M.
Identification of the amniotic fluid insulin-like growth factor binding protein-1 phosphorylation sites and propensity to proteolysis of the isoforms
FEBS J.
276
6033-6046
2009
Staphylococcus aureus
brenda
Such-Sanmartin, G.; Bosch, J.; Segura, J.; Gutierrez-Gallego, R.
Generation of 5 and 17 kDa human growth hormone fragments through limited proteolysis
Growth Factors
27
255-264
2009
Staphylococcus aureus
brenda
Guedes, S.; Vitorino, R.; Domingues, M.R.; Amado, F.; Domingues, P.
Mass spectrometry characterization of the glycation sites of bovine insulin by tandem mass spectrometry
J. Am. Soc. Mass Spectrom.
20
1319-1326
2009
Staphylococcus aureus
brenda
Schmidtchen, A.; Pasupuleti, M.; Moergelin, M.; Davoudi, M.; Alenfall, J.; Chalupka, A.; Malmsten, M.
Boosting antimicrobial peptides by hydrophobic oligopeptide end tags
J. Biol. Chem.
284
17584-17594
2009
Staphylococcus aureus
brenda
Kwak, Y.K.; Hoegbom, M.; Colque-Navarro, P.; Moellby, R.; Vecsey-Semjen, B.
Biological relevance of natural alpha-toxin fragments from Staphylococcus aureus
J. Membr. Biol.
233
93-103
2010
Staphylococcus aureus, Staphylococcus aureus Wood 46
brenda
Boudier, C.; Klymchenko, A.S.; Mely, Y.; Follenius-Wund, A.
Local environment perturbations in alpha1-antitrypsin monitored by a ratiometric fluorescent label
Photochem. Photobiol. Sci.
8
814-821
2009
Staphylococcus aureus
brenda
Mateos, A.; Girardet, J.M.; Molle, D.; Corbier, C.; Gaillard, J.L.; Miclo, L.
Identification of phosphorylation sites of equine beta-casein isoforms
Rapid Commun. Mass Spectrom.
24
1533-1542
2010
Staphylococcus aureus, Staphylococcus aureus V8
brenda
Ono, T.; Ohara-Nemoto, Y.; Shimoyama, Y.; Okawara, H.; Kobayakawa, T.; Baba, T.T.; Kimura, S.; Nemoto, T.K.
Amino acid residues modulating the activities of staphylococcal glutamyl endopeptidases
Biol. Chem.
391
1221-1232
2010
Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus saprophyticus, Staphylococcus warneri, Staphylococcus cohnii subsp. cohnii, Staphylococcus caprae, Staphylococcus aureus ATCC 25923, Staphylococcus cohnii subsp. cohnii GTC 248, Staphylococcus caprae GTC 378, Staphylococcus warneri JCM 2415, Staphylococcus epidermidis ATCC 14990
brenda
Park, J.W.; Park, J.E.; Park, J.K.; Lee, J.S.
Purification and biochemical characterization of a novel glutamyl endopeptidase secreted by a clinical isolate of Staphylococcus aureus
Int. J. Mol. Med.
27
637-645
2011
Staphylococcus aureus, Staphylococcus aureus C-66
brenda
Craig, M.; Amiri, M.; Holmberg, K.
Bacterial protease triggered release of biocides from microspheres with an oily core
Colloids Surf. B Biointerfaces
127C
200-205
2015
Staphylococcus aureus
brenda
Kalyankar, P.; Zhu, Y.; OKeeffe, M.; OCuinn, G.; FitzGerald, R.J.
Substrate specificity of glutamyl endopeptidase (GE): hydrolysis studies with a bovine alpha-casein preparation
Food Chem.
136
501-512
2013
Bacillus licheniformis
brenda
Zhu, Y.S.; Kalyankar, P.; FitzGerald, R.J.
Relative quantitation analysis of the substrate specificity of glutamyl endopeptidase with bovine alpha-caseins
Food Chem.
167
463-467
2015
Bacillus licheniformis
brenda
Kalyankar, P.; Zhu, Y.; OCuinn, G.; FitzGerald, R.J.
Investigation of the substrate specificity of glutamyl endopeptidase using purified bovine beta-casein and synthetic peptides
J. Agric. Food Chem.
61
3193-3204
2013
Bacillus licheniformis
brenda
Liu, F.; Zhao, Z.S.; Ren, Y.; Cheng, G.; Tang, X.F.; Tang, B.
Autocatalytic activation of a thermostable glutamyl endopeptidase capable of hydrolyzing proteins at high temperatures
Appl. Microbiol. Biotechnol.
100
10429-10441
2016
Thermoactinomyces sp. CDF
brenda
Elmwall, J.; Kwiecinski, J.; Na, M.; Ali, A.A.; Osla, V.; Shaw, L.N.; Wang, W.; Saevman, K.; Josefsson, E.; Bylund, J.; Jin, T.; Welin, A.; Karlsson, A.
Galectin-3 is a target for proteases involved in the virulence of Staphylococcus aureus
Infect. Immun.
85
e00177-17
2017
Staphylococcus aureus (Q2FZL2), Staphylococcus aureus, Staphylococcus aureus NCTC 8325 (Q2FZL2)
brenda