Information on EC 3.4.22.58 - caspase-5

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.58
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RECOMMENDED NAME
GeneOntology No.
caspase-5
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-/- but also cleaves at Asp-Glu-Val-Asp-/-
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
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CAS REGISTRY NUMBER
COMMENTARY hide
192465-11-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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caspase-5 knockdown by shRNA reduces caspase-1 protein expression and activation and inhibited TNF-alpha–induced interleukin-8 and MCP-1
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
show the reaction diagram
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optimal tetrapeptide recognition motif
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-
?
CrmA + H2O
?
show the reaction diagram
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-
-
-
?
interleukin-1beta + H2O
?
show the reaction diagram
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50 nM enzyme partly cleaves interleukin-1beta into the 28000 Da form and a very faint 17500 Da band can be detected, with other dilutions of TY no cleavage is detected
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-
?
MDIGAYPHFMPTNLAGDPY + H2O
AYPHFMPTNLA + AYPHFMPTNLAGD + DIGAYPHFMPTNLAG + IGAYPHFMPTNLAGD + MDIGAYPHFMPTNL + MDIGAYPHFMPTNLA + MDIGAYPHFMPTNLAGD + MDIGAYPHFMPTNLAGDP + Met + MDIG + Met-Asp + Tyr + Pro-Tyr + GDPY + DPY
show the reaction diagram
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quantitative product mass spectrometric analysis, overview
-
?
p35 + H2O
?
show the reaction diagram
-
-
-
-
?
pro-caspase-3 + H2O
p12 + pro-p17
show the reaction diagram
-
-
-
?
pro-caspase-5 + H2O
?
show the reaction diagram
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caspase-5 has protease activity on its own precursor
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-
?
succinyl-YVAD-7-amido-4-methylcoumarin + H2O
succinyl-YVAD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
WEHD-4-nitroanilide + H2O
WEHD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
additional information
?
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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
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-AEVD-aldehyde
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acetyl-DEVD-aldehyde
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acetyl-IETD-aldehyde
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acetyl-WEHD-aldehyde
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acetyl-YVAD-aldehyde
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
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t1/2 at 0.001 mM
cowpox serpin CrmA
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CrmA
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inhibits cleavage of pro-caspase-3
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WEHD-CHO
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YVAD-CHO
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Z-VAD-fluoromethylketone
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pan-caspase inhibitor
Z-WEHD-fluoromethylketone
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a caspase-5 and -1 inhibitor
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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activation of caspase-5 is enhanced by ATP and endoplasmic reticulum stress inducers, and 2.2-5.4fold by interleukin-1beta, TNF-alpha, lipopolysaccharide and hRPE cell co-culture, but not by IFN-gamma
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
acetyl-WEHD-7-amido-4-methylcoumarin
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pH 7-5-8.0
0.86
succinyl-YVAD-7-amido-4-methylcoumarin
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pH 7.5, 37°C
additional information
additional information
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allosteric site on caspase-5
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.3
acetyl-WEHD-7-amido-4-methylcoumarin
Homo sapiens
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pH 7-5-8.0
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0014
acety-DEVD-aldehyde
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pH 7.5, 37°C
0.0008
acety-YVAD-aldehyde
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pH 7.5, 37°C
0.000438
acetyl-AEVD-aldehyde
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pH 7.5, 25°C
0.000205
acetyl-IETD-aldehyde
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pH 7.5, 25°C
0.000043 - 0.000223
acetyl-WEHD-aldehyde
0.000163
acetyl-YVAD-aldehyde
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pH 7.5, 25°C
additional information
additional information
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the Ki-value for cowpox serpin CrmA is below below 0.1 nM
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8
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cleavage of acetyl-WEHD-7-amido-4-methylcoumarin
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
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primary cultured hRPE cells, telomerase-immortalized hTERT-RPE1 cells
Manually annotated by BRENDA team
additional information
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no activity detected in brain
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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x * 50000, SDS-PAGE
55000
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x * 55000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 50000, SDS-PAGE; x * 55000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in 293-cells
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overexpression in COS cells
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overexpression in Escherichia coli, Rat-1 or HeLa cells
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the enzyme is expressed in baculovirus-infected insect cells, as a 30000 Da protein lacking the propeptide
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
caspase-5 is induced 1.9-2.3fold by interleukin-1beta, TNF-alpha, lipopolysaccharide and hRPE cell co-culture, but not by IFN-gamma
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expression of caspase-5 is inhibited by caspase-1-specific inhibitor Z-YVAD-fluoromethylketone
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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stable knockdown of caspase-5 by shRNA3554