Information on EC 3.4.21.B4 - granzyme K

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.21.B4
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
granzyme K
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endopeptidase activity. Cleaves after Lys and Arg
show the reaction diagram
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
196622-94-3
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
actin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Arg p-nitrobenzyl ester + H2O
benzyloxycarbonyl-Arg + p-nitrobenzyl alcohol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-L-Arg-thiobenzyl ester + H2O
benzyloxycarbonyl-L-Arg + thiobenzyl alcohol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-L-Lys-thiobenzyl ester + H2O
benzyloxycarbonyl-L-Lys + thiobenzyl alcohol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Lys-thiobenzyl ester + H2O
benzyloxycarbonyl-Lys + thiobenzyl alcohol
show the reaction diagram
-
-
-
-
?
beta-tubulin + H2O
?
show the reaction diagram
-
cleaves beta-tubulin after Arg62 (YVPR-/-AV) and Arg282 (QQYR-/-AL)
-
-
?
Bid protein + H2O
tBid protein + ?
show the reaction diagram
-
GzmK directly processes Bid to produce its active form tBid
-
-
?
Cbz-L-Arg-4-nitroanilide + H2O
Cbz-L-Arg + 4-nitroaniline
show the reaction diagram
little hydrolyzed by Gr3
-
-
?
Cbz-L-Arg-7-amido-4-methylcoumarin + H2O
Cbz-L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
little hydrolyzed by Gr3
-
-
?
Cbz-L-Lys-4-nitroanilide + H2O
Cbz-L-Lys + 4-nitroaniline
show the reaction diagram
little hydrolyzed by Gr3
-
-
?
Cys-Gly-Tyr-Gly-Pro-Lys-Lys-Lys-Arg-Lys-Val-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
?
Cys-Gly-Tyr-Gly-Pro-Lys-Lys-Lys-Arg-Lys-Val-Gly-Gly + H2O
Cys-Gly-Tyr-Gly-Pro-Lys + Lys-Lys-Arg + Lys-Val-Gly-Gly
show the reaction diagram
-
-
-
-
?
endoplasmic reticulum-associated SET complex + H2O
?
show the reaction diagram
-
-
-
-
?
fluorescence resonance energy transfer substrate-25Arg peptide + H2O
?
show the reaction diagram
most effectively hydrolyzes the substrate fluorescence resonance energy transfer substrate-25Arg peptide in the FRETS-25Xaa series tested
-
-
?
fluorescence resonance energy transfer substrate-25Lys peptide + H2O
?
show the reaction diagram
far less effectively cleaved than fluorescence resonance energy transfer substrate-25Arg peptide
-
-
?
heterogeneous nuclear ribonucleoprotein K + H2O
?
show the reaction diagram
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granzyme K and granzyme A cleave with different kinetics at distinct sites
-
-
?
N-acetyl-YRFK-4-nitroanilide + H2O
N-acetyl-YRFK + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-tert-butoxycarbonyl-Ala-Ala-Asp-thiobenzyl ester
?
show the reaction diagram
-
-
-
?
N-tert-butoxycarbonyl-Ala-Ala-Met-thiobenzyl ester
?
show the reaction diagram
-
-
-
?
Nalpha-benzyloxycarbonyl-L-Arg-thiobenzyl ester
?
show the reaction diagram
Nalpha-benzyloxycarbonyl-L-Lys-thiobenzyl ester
?
show the reaction diagram
Nalpha-CBZ-L-lysine thiobenzyl ester
?
show the reaction diagram
-
-
-
?
nucleosome assembly protein SET + H2O
?
show the reaction diagram
-
-
-
-
?
Protein + H2O
?
show the reaction diagram
redox factor-1/apurinic apyrimidinic endonuclease Ape1 + H2O
?
show the reaction diagram
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Ape1 cleavage by Granzyme K facilitates intracellular reactive oxygen species accumulation and enhances granzyme K-induced cell death
-
-
?
Z-Arg-thiobenzyl ester + H2O
Z-Arg + thiobenzyl alcohol
show the reaction diagram
-
-
-
-
?
Z-Leu-Arg-Gly-Gly-7-amido-4-methylcoumarin + H2O
Z-Leu-Arg + Gly-Gly-7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Lys-thiobenzyl ester + H2O
?
show the reaction diagram
-
-
-
?
Z-Lys-thiobenzyl ester + H2O
Z-Lys + thiobenzyl alcohol
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
Protein + H2O
?
show the reaction diagram
redox factor-1/apurinic apyrimidinic endonuclease Ape1 + H2O
?
show the reaction diagram
-
Ape1 cleavage by Granzyme K facilitates intracellular reactive oxygen species accumulation and enhances granzyme K-induced cell death
-
-
?
additional information
?
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,3-diphenylpropanoyl-Pro-(4-AmPhGly)P(OPh)2
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potent inhibitor
3,4-dichloroisocoumarin
4-aminobenzamidine
Aprotinin
benzamidine
bikunin
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carbobenzoxy-Thr-(4-AmPhGly)P(OPh)2
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quite specific but weak inhibitor
D-Phe-Pro-Arg-CH2Cl
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good inhibitor
diisopropylfluorophosphate
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complete inhibition at 0.1 mM
Glu-Gly-Arg-chloromethyl ketone
human blood plasma
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-
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inter-alpha-trypsin inhibitor
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complete inhibition at 66 nM
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inter-alpha-trypsin inhibitor complex
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physiologic inhibitor
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Kunitz-type inhibitor aprotinin
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-
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L-Phe-L-Pro-L-Arg-chloromethyl ketone
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complete inhibition at 0.1 mM
leupeptin
N-acetyl-YRFK-chloromethylketone
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PefablocSC
Phe-Pro-Arg-chloromethyl ketone
phenylmethylsulfonyl fluoride
Phenylmethylsulfonylfluoride
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2 mM
second carboxy-terminal Kunitz-type domain of bikunin
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Soybean trypsin inhibitor
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50% inhibition at 0.025 mM
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Tos-Lys-CH2Cl
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complete inhibition at 0.1 mM
Z-LysP(OPh)2
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best inhibitor
Z-Trp-Ch2Cl
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moderate inhibitor
Zn2+
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significant reduction of enzyme activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
benzyloxycarbonyl-Arg p-nitrobenzyl ester
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5.2
benzyloxycarbonyl-L-Lys-thiobenzyl ester
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-
0.14
Nalpha-benzyloxycarbonyl-L-Arg-thiobenzyl ester
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pH 7.6
1.7
Nalpha-benzyloxycarbonyl-L-Lys-thiobenzyl ester
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pH 7.6
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000033 - 0.00006
bikunin
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0.000064
inter-alpha-trypsin inhibitor complex
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pH 7.6
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0.000022 - 0.000027
second carboxy-terminal Kunitz-type domain of bikunin
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0529
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cell extract, using benzyloxycarbonyl-Lys-thiobenzyl ester as a substrate, at 25C
37.1
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after 1202.9fold purification, using benzyloxycarbonyl-Arg p-nitrobenzyl ester as a substrate, at 25C
63.7
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after 1202.9fold purification, using benzyloxycarbonyl-Lys-thiobenzyl ester as a substrate, at 25C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
8.2 - 8.6
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8.5 - 9
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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increased GzmK levels during viral infections
Manually annotated by BRENDA team
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from patients with allergic asthma (before and after segmental allergen challenge), and in patients with mild chronic obstructive pulmonary disease (COPD), pneumonia and in healthy controls. Expression of granzyme K is upregulated in acute airway inflammation, both in infectious and non-infectious diseases
Manually annotated by BRENDA team
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mRNA exptression
Manually annotated by BRENDA team
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granzyme serum levels are elevated in patients with autoimmune diseases and infections, including sepsis
Manually annotated by BRENDA team
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mRNA exptression
Manually annotated by BRENDA team
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cytotoxic
Manually annotated by BRENDA team
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mRNA exptression
Manually annotated by BRENDA team
additional information
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granzymes are released by cytotoxic lymphocytes
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 25000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no potential sites for N-linked glycosylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme quickly loses catalytic activity when diluted and stored in solution, Tween-20 or bovine serum albumin prevent loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DE52 anion-exchange column chromatography, Q Sepharose column chromatography, hydroxylapatite column chromatography, and Sephadex G-75 gel filtration
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homogeneity
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nickel chelation column chromatography
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recombinant wild-type and mutant enzymes by cation-exchange chromatography and affinity chromatography on Prot A/G beads, followed by dialysis
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Bacillus subtilis
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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recombinant expression of wild-type and mutant enzymes
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S195A variant expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S214A
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inactive