3.4.21.19: glutamyl endopeptidase

This is an abbreviated version!
For detailed information about glutamyl endopeptidase, go to the full flat file.

Reaction

Preferential cleavage: Glu-/-, Asp-/- =

Synonyms

Alcalase, BIEP, BIGEP, BL-GSE, BLase, BS-GSE, endoproteinase Glu-C, endoproteinase V8, Glu C, Glu-C, Glu-endopeptidase, Glu-specific endopeptidase, GluScoh, GluScpr, GluSE, GluSsap, GluSW, glutamate specific endopeptidase, glutamate-specific proteinase, glutamate-specific serine endopeptidase, glutamic acid-specific endopeptidase, glutamic acid-specific proteinase, glutamic-acid-specific endopeptidase, glutamyl endopeptidase, glutamyl endopeptidase 2, glutamyl endopeptidase I, glutamyl specific endopeptidase, GluV8, GSE, gseBi gene product, protease V8, proteinase, glutamate-specific, proteinase, staphylococcal serine, SG-GSE, SGPE, Sspa, staphylococcal serine proteinase, V8 protease, V8 proteinase, V8-GSE, V8-protease, VSPase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.19 glutamyl endopeptidase

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Results	in table
5	Activating Compound
145	AA Sequence
9	Application
2	CAS Registry Number
19	Cloned(Commentary)
5	Crystallization (Commentary)
2	General Stability
32	Inhibitors
1	kcat/KM [mM/s]
38	KM Value [mM]
19	Localization
10	Metals/Ions
19	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
165	Organism
19	PDB ID
31	pH Optimum
2	pH Range
3	pH Stability
2	pI Value
4	Posttranslational Modification
40	Protein Variants
22	Purification (Commentary)
8	Reaction
4	Reaction Type
82	Reference
1	Renatured (Commentary)
6	Source Tissue
13	Specific Activity [micromol/min/mg]
3	Storage Stability
226	Substrates and Products (Substrate)
22	Subunits
102	Synonyms
19	Temperature Optimum [°C]
8	Temperature Stability [°C]
32	Turnover Number [1/s]

Natural Substrates Products

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of the Enzyme Summary Page.

Natural Substrates Products on EC 3.4.21.19 - glutamyl endopeptidase

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

alpha-casein + H2O

?

Bacillus licheniformis

-

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

731853

-

-

?

Gelatin + H2O

?

Bacillus intermedius

-

-

651024

-

651024

?

GluV8 + H2O

?

Staphylococcus aureus

-

degradation of the C-terminus at the Glu279-Asp280 bond is suspected to be a result from autoproteolysis

679805

38 kDa species

-

?

prothrombin + H2O

?

2 entries

additional information

?

-

7 entries

prothrombin + H2O

?

Staphylococcus aureus

-

the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin

717680

-

-

?

prothrombin + H2O

?

Staphylococcus aureus C-66

-

the enzyme preferentially cleaves peptide bonds at the carboxyl sides of glutamate residues in prothrombin

717680

-

-

?

additional information

?

-

Bacillus intermedius

Q9EXR9

enzyme suspected to be involved in the outgrowth of spores when the germinating endospore converts into the vegetative cell

681845

-

-

?

additional information

?

-

Bacillus intermedius

-

enzyme suspected to be involved in the outgrowth of spores when the germinating endospore converts into the vegetative cell

681845

-

-

?

additional information

?

-

Bacillus intermedius

Q9EXR9

splits specifically the peptide bonds formed by alpha-carboxyl groups of glutamic and, and to a lesser extent, of aspartic acid

681845

-

-

?

additional information

?

-

Bacillus intermedius

-

splits specifically the peptide bonds formed by alpha-carboxyl groups of glutamic and, and to a lesser extent, of aspartic acid

681845

-

-

?

additional information

?

-

Staphylococcus aureus

-

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

679805

-

-

?

additional information

?

-

Staphylococcus epidermidis

-

specifically cleaves the peptide bond after the negatively charged residues Glu and, less potently, Asp

679805

-

-

?

additional information

?

-

Thermoactinomyces sp. CDF

-

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

752559

-

-

?