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Information on EC 3.4.21.19 - glutamyl endopeptidase and Organism(s) Bacillus intermedius and UniProt Accession Q9EXR9
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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: Bacillus intermedius
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 proteinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: Glu-/-, Asp-/-
specific for cleavage on the carboxylic site of glutamic acid, catalytic site are His47 and Ser171, the N-terminus is involved in formation of the substrate binding pocket, a direct structural relation between zymogen activation and substrate charge compensation exists
-
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
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
-
-
-
?
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
-
preferred peptide substrate
-
?
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-Glu-4-nitroanilide + H2O
benzyloxycarbonyl-Glu + 4-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
-
-
-
-
?
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
-
?
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
-
?
benzyloxycarbonyl-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Glu-p-nitroanilide + H2O
benzyloxycarbonyl-Glu + p-nitroaniline
-
-
-
?
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
?
-
-
substrate specificity, preferrence for Glu-cleavage site before Asp-cleavage site
-
?
additional information
?
-
-
no cleavage of certain substrates of chymotrypsin
-
-
?
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
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
-
strong stimulation, up to 400%, of enzyme expression in recombinant Bacillus subtilis strain at 5 mM
Mg2+
-
stimulation of enzyme expression in recombinant Bacillus subtilis strain at 1 mM
Ca2+
-
stimulation of enzyme expression in recombinant Bacillus subtilis strain at 2 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
-
gradual inhibition of enzyme expression in recombinant Bacillus subtilis strain at 1-10 mM
Fe2+
-
gradual inhibition of enzyme expression in recombinant Bacillus subtilis strain at 1-10 mM
Zn2+
-
gradual inhibition of enzyme expression in recombinant Bacillus subtilis strain at 1-10 mM
additional information
-
no inhibition by EDTA, benzamidine, duck ovomucoid, inhibitor from marine anemone, soybean trypsin inhibitor
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.67
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-L-Glu-4-nitroanilide
-
wild-type, pH 8.5, 37°C
3.3
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-L-Glu-4-nitroanilide
-
mutant H186T, pH 8.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.027
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-L-Glu-4-nitroanilide
-
mutant H186T, pH 8.5, 37°C
16.6
benzyloxycarbonyl-L-Ala-L-Ala-L-Leu-L-Glu-4-nitroanilide
-
wild-type, pH 8.5, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
-
enzyme possesses 2 optima at pH 7.2 and pH 9.5 for reaction with casein
9.5
-
enzyme possesses 2 optima at pH 7.2 and pH 9.5 for reaction with casein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
secretion to the culture medium during the late stages of growth
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified enzyme in 0.01 M Tris-HCl, pH 7.0, 2 mM CaCl2, 1.2 M potassium phosphate, with or without 3% 2-methyl-2,4-pentanediol, presence of the latter leads to a second crystal form, X-ray diffraction structure determination and analysis at 1.5-1.75 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H186T
-
no effect on enzyme specificity, 4.9fold increase in KM-value, 600fold decrease in kcat-value
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant Bacillus intermedius glutamyl endopeptidase (BIGEP-Bs) is purified from Bacillus subtilis AJ73 strain
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
different BIGEP forms (full-length precursor, precursor without signal peptide and mature part) are expressed in Escherichia coli
expressed in enzyme deficient strain Bacillus subtilis AJ73, sporulation and enzyme expression is strongly reduced when 1% glucose is added to the culture medium at the beginning of the growth phase, no effect of glucose addition after 20 h of cultivation period, slightly enhanced activity when glucose is added after 30 h of cultivation
expressed in Bacillus subtilis recombinant strains with mutations in the regulatory proteins Spo0A, KinA, and Ger
-
expression in Bacillus subtilis, optimization of culture medium composition for production of recombinant enzyme, recombinant enzyme is secreted to the medium from Bacillus subtilis cells, 2-5% of the enzyme remain bound to the cell wall
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
increased accumulation of recombinant enzyme in Bacillus subtilis by growth in presence of casein or gelatin. During stationary growth phase, enzyme production is stimulated by Ca2+, Mn2+, and Co2+, and inhibited by Zn2+, Fe2+, and Cu2+
synthesis
-
increased accumulation of recombinant enzyme in Bacillus subtilis during stationary growth phase by growth in presence of phosphate or ammonium ions, and in presence of gelatin or casein. During sporulation, enzyme production is stimulated by Ca2+, Mn2+, and Co2+, and inhibited by Zn2+, Fe2+, and Cu2+. Glucose is not inhibitory to enzyme production during stationary growth
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
-
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
-
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
-
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
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
-
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
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