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Information on EC 3.4.21.19 - glutamyl endopeptidase and Organism(s) Staphylococcus epidermidis and UniProt Accession P0C0Q1

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.19 glutamyl endopeptidase
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This record set is specific for:
Staphylococcus epidermidis
UNIPROT: P0C0Q1 not found.
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Word Map
The taxonomic range for the selected organisms is: Staphylococcus epidermidis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Preferential cleavage: Glu-/-, Asp-/-
Synonyms
v8 protease, endoproteinase glu-c, glu-c, protease v8, v8 proteinase, glutamyl endopeptidase, v8-protease, blase, gluv8, gluse, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutamyl endopeptidase
-
BLase
-
-
-
-
endoproteinase Glu-C
-
-
-
-
GluSE
glutamate specific endopeptidase
-
-
-
-
glutamate-specific proteinase
-
-
-
-
glutamic acid-specific proteinase
-
-
-
-
glutamic-acid-specific endopeptidase
-
-
-
-
glutamyl endopeptidase
-
-
GSE
-
-
-
-
protease V8
-
-
-
-
proteinase, glutamate-specific
-
-
-
-
proteinase, staphylococcal serine
-
-
-
-
SGPE
-
-
-
-
staphylococcal serine proteinase
-
-
-
-
V8 proteinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
137010-42-5
-
82062-91-7
formerly
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Glu-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Leu-Leu-Glu-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Leu-Leu-Glu-MCA + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 4.15
Leu-Leu-Glu-4-methylcoumaryl-7-amide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6147 - 9059
Leu-Leu-Glu-4-methylcoumaryl-7-amide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GSEA_STAEP
282
0
30809
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
mature protease, small amounts of proenzymes with molecular masses of 32, 30, and 29 kDa are identified in the extracellular and cell wall-associated fractions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 29000-32000, SDS-PAGE, full length protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
full length form of C-terminally His-tagged GluSE is purified as three proenzymes equivalent to the native ones
large scale purification as one step purification using Talon affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed as soluble His-tag fusion protein in Escherichia coli
-
expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team