Information on EC 3.4.21.B50 - DegQ peptidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.4.21.B50
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
DegQ peptidase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene deg2
UniProt
Manually annotated by BRENDA team
strain FZB42
-
-
Manually annotated by BRENDA team
strain FZB42
-
-
Manually annotated by BRENDA team
strain 168
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
strain T4, a pathogenic strain isolated from diseased fish
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
The Deg2 protease domain consists of a catalytic triad comprising His159, Asp190, and Ser268. The enzyme contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of the enzyme, a conserved internal ligand for PDZ2 mediates hexamer formation and locks the protease in the resting state
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Arc-st11 repressor + H2O
?
show the reaction diagram
-
cleavage sites: Val22-/-Arg23, Val25-/-Ala25 and Val41-/-Met42
-
-
?
beta-casein + H2O
?
show the reaction diagram
casein + H2O
hydrolyzed casein
show the reaction diagram
endoprotease, active serine protease whose activity requires the integrity of the catalytic site and the PDZ domains
-
-
?
lambda-repressor variant 105 + H2O
?
show the reaction diagram
-
cleavage sites: Val36-/-Ala37, Val71-/-Ser72, Ile84-/-Tyr85, Val91-/-Ser92
-
-
?
OmpA protein + H2O
?
show the reaction diagram
-
-
-
-
?
unfolded bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-casein + H2O
?
show the reaction diagram
-
-
-
-
?
OmpA protein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
10 mM, 42% increase in activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phenylmethanesulfonyl fluoride
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
exhibits more than 70% of the maximum activity over the pH range of 5 to 9
6 - 9.5
activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 55
exhibits more than 70% of the maximum activity over the temperature range of 40 to 55°C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
300000
-
hexamer, gel filtration
320000 - 440000
-
gel filtration
600000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
hexamer
-
6 * 50000, SDS-PAGE
hexamer or dodecamer
hexameric structure of mature enzyme, the Deg2 hexamer exists predominantly during substrate incubation in a resting state,the large oligomeric state is the active state, model of oligomeric state change, overview
trimer
-
substrate-free form
additional information
structure-function analysis of the dimerization interface between Deg2 trimers, overview. The enzyme contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of the enzyme, a conserved internal ligand for PDZ2 mediates hexamer formation and locks the protease in the resting state. Because loop JK lies outside the hexamer shell, it provides protection for the loop LA-PDZ2 interface from solvents and may play a role in changes in the oligomeric enzyme state
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
1 h, enzyme retains 81% activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel-affinity column chromatography, gel filtration
-
recombinant
-
recombinant enzyme
recombinant maltose-binding protein- and His6-tagged enzyme from Escherichia coli by dextrin affinity chromatography, folloed by tag cleavage through tobacco etch virus protease
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli KU98 cells
-
expression in Escherichia coli
gene deg2, recombinant expression of the maltose-binding protein- and His6-tagged enzyme in Escherichia coli
overexpression in Escherichia coli JM105
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S187A
-
protease-deficient mutant that retains chaperone-like activity
D113A
mutant exhibits 97.5% reduction in activity
H83A
mutant exhibits 93.4% reduction in activity
S188A
mutant exhibits 91.8% reduction in activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the purified recombinant DegQVh is a protective immunogen that could confer protection upon fish against infection by Vibrio harveyi. In order to improve the efficiency of DegQVh as a vaccine, a genetic construct in the form of the plasmid pAQ1 is built, in which the DNA encoding the processed DegQVh protein is fused with the DNA encoding the secretion region of AgaV, an extracellular beta-agarase. The Escherichia coli strain harboring pAQ1 can express and secrete the chimeric DegQVh protein into the culture supernatant. Vaccination of fish with viable Escherichia coli expressing chimeric degQVh significantly enhanced the survival of fish against Vibrio harveyi challenge, which is possibly due to the relatively prolonged exposure of the immune system to the recombinant antigen produced constitutively