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Information on EC 3.4.21.19 - glutamyl endopeptidase and Organism(s) Staphylococcus aureus and UniProt Accession Q2FZL2
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3.4.21.19 glutamyl endopeptidaseSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
v8 protease, endoproteinase glu-c, glu-c, protease v8, v8 proteinase, glutamyl endopeptidase, v8-protease, blase, gluv8, gluse, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BLase
-
-
-
-
endoproteinase Glu-C
glutamate specific endopeptidase
-
-
-
-
glutamate-specific proteinase
-
-
-
-
glutamic acid-specific proteinase
-
-
-
-
glutamic-acid-specific endopeptidase
-
-
-
-
GSE
-
-
-
-
protease V8
-
-
-
-
proteinase, glutamate-specific
-
-
-
-
proteinase, staphylococcal serine
-
-
-
-
SGPE
-
-
-
-
staphylococcal serine proteinase
-
-
-
-
V8 protease
V8 proteinase
endoproteinase Glu-C
-
-
-
-
V8 protease
-
-
V8 protease
-
member of the glutamyl endopeptidase I family, protein of 336 amino acids that includes a prepropeptide consisting of 68 residues (Met1-Asn68) and a C-terminal tail of 52 residues consisting of a 12fold repeat of the tripeptide Pro-Asp/Asn-Asn, prosegment is essential for the suppression of proteolytic activity, as well as for the correct folding of GluV8, indicating its role as an intramolecular chaperone
V8 proteinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: Glu-/-, Asp-/-
absolutely specific for cleavage sites Glu-/-Xaa and Asp-/-Xaa, cleavage exclusively at the carboxylic side, active site Ser169
-
Preferential cleavage: Glu-/-, Asp-/-
catalytic tetrad of His213, Asp102, Ser195, and Trp214, computer modeling of S1 and S'1 sites of the enzyme's active site
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
137010-42-5
-
82062-91-7
formerly
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
-
-
?
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-Glu-4-nitrophenyl + 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
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 2-carboxyphenylthioester + H2O
benzyloxycarbonyl-Ala + 2-carboxyphenylthiol
-
-
-
?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 3-carboxyphenylester + H2O
benzyloxycarbonyl-Ala + 3-carboxyphenol
-
-
-
?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala 4-carboxyphenylester + H2O
benzyloxycarbonyl-Ala + 4-carboxyphenol
-
-
-
?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
benzyloxycarbonyl-Ala carboxyethylthioester + H2O
benzyloxycarbonyl-Ala + carboxyethylthiol
-
-
-
?
benzyloxycarbonyl-Ala carboxymethylthioester + H2O
?
-
enzyme also performs acyl-transfer reaction with substrate mimetics
-
?
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-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-Glu methyl ester + H2O
benzyloxycarbonyl-Glu + methanol
-
-
-
?
benzyloxycarbonyl-Glu methylthioester + H2O
benzyloxycarbonyl-L-Glu + methylthiol
-
-
-
?
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-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
?
-
cleavage of native myelin basic protein at Gly127-Gly128 and of carboxymethylated myelin basic protein at Phe124-Gly125
-
-
?
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
-
different isoforms
product analysis by mass spectrometry, overview
-
?
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
-
-
peptide fragments Lys1-Glu6, Arg8-Glu10 and Lys1-Glu10 are produced after 6 min
?
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
-
i.e. L-2135
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
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
?
-
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
GluV8 + H2O
?
-
degradation of the C-terminus at the Glu279-Asp280 bond is suspected to be a result from autoproteolysis
38 kDa species
-
?
prothrombin + H2O
?
-
the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin
-
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
light
-
the activity of V8 protease is inhibited in a dose-dependent manner by exposure to laser light in the presence of light-activated antimicrobial agent methylene blue leading to degradation of the V8 protease that cannot be inhibited by the addition of a protease inhibitor
-
methylene blue
-
the activity of V8 protease is inhibited in a dose-dependent manner by exposure to laser light in the presence of light-activated antimicrobial agent methylene blue leaidng to degradation of the V8 protease that cannot be inhibited by the addition of a protease inhibitor
tagged peptide GKH17
-
i.e. GKHKNKGKKNGKHNGWK,an antimicrobial peptide, derived from kininogen boosted through end tagging with hydrophobic oligopeptide stretches. Tagging results in enhanced killing of Gram-positive Staphylococcus aureus. Microbicidal potency increases with tag length, also in plasma, and is larger for Trp and Phe stretches than for aliphatic ones, overview
-
tagged peptide HKH17
-
i.e. HKHGHGHGKHKNKGKKN,an antimicrobial peptide, derived from kininogen boosted through end tagging with hydrophobic oligopeptide stretches. Tagging results in enhanced killing of Gram-positive Staphylococcus aureus. Microbicidal potency increases with tag length, also in plasma, and is larger for Trp and Phe stretches than for aliphatic ones, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.48
L-Phe-L-Leu-L-Glu-4-nitroanilide
-
pH and temperature not specified in the publication
additional information
additional information
-
kinetics and thermodynamic stability
-
additional information
additional information
-
kinetics of the acyl transfer reactions with substrate mimetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
44.4
L-Phe-L-Leu-L-Glu-4-nitroanilide
-
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30
L-Phe-L-Leu-L-Glu-4-nitroanilide
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
hydrolysis activity of the enzyme with substrate mimetics
additional information
-
the combination of W185, V188, and P189, which naturally occurr on GluV8, exerts the highest protease activity. Among them, W185 and P189 can not be replaced by other amino acids for the full activity, but V188 could be replaced by hydrophobic amino acids, such as L188 for the two substrates, F188 for AE-MCA and I188 for LLE-MCA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
44000
-
SDS-PAGE. GluV8 is scarcely expressed. Mutant GluV8mut5 shows a 44 kDa band having much higher density than that of GluV8mut4
44000
-
x * 44000, SDS-PAGE, recombinant fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, minor species of 42000 Da obtained after purification
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structural and functional rganization, overview
?
-
mobility of the mature protein on SDS-PAGE is altered by heating the samples, proteins can be fully renaturated under conditions of zymography
?
-
x * 44000, SDS-PAGE, recombinant fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, minor species of 42000 Da obtained after purification
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
upon thermolysin treatment the 44 kDa protein is converted to a 42 kDa species and, finally, to 38 and 40 kDa species, degradation of C-terminus at the Glu279-Asp280 bond is suspected to be a result from autoproteolysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
7 mg/ml purified enzyme in 50 mM HEPES, pH 8.6, 50 mM KCl, 15% PEG 500 monomethylester, hanging drop method over a reservoir solution containing 0.1 M KCl, 0.1 M HEPES, and 20% PEG 5000 monomethyl ester, 293 K, X-ray diffraction structure determination and analysis at 1.9 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant fusion protein containing the mature protein sequence and the pro-sequence of the analogous enzyme from Staphylococcus epidermidis and the four point mutant enzyme in large scale using Talon affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, poor expression of native full length protein, successful expression when mature protein sequence is fused with the pro-sequence of the analogous enzyme from Staphylococcus epidermidis, successful expression of double and four point mutant in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
synthesis
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enzyme can be used as catalyst for peptide synthesis in hydrophilic organic solvents with low water content, e.g. acetonitrile, overview
analysis
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study of structure-function organization of anti-HIV and antitumor proteins MAP30 and GAP31 by limited proteolysis with V8-GSE, enzym may be useful for studying other proteins as well
analysis
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increase in selectivity of immobilized metal affinity chromatography for phosphopeptides by use of enzyme for protein digestion. Enzyme cleaves proteins at acidic residues and reduces the number of acidic residues in peptides. Application of method to a selction of model proteins and to bovine milk
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bjrklind, A.; Jrnvall, H.
Substrate specificity of three different extracellular proteolytic enzymes from Staphylococcus aureus
Biochim. Biophys. Acta
370
524-529
1974
Staphylococcus aureus
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
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
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
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
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
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
Srinivasulu, S.; Acharya, A.S.
Product-conformation-driven ligation of peptides by V8 protease
Protein Sci.
11
1384-1392
2002
Staphylococcus aureus
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
-
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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)
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