3.4.21.79: granzyme B
This is an abbreviated version!
For detailed information about granzyme B, go to the full flat file.
Word Map on EC 3.4.21.79
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3.4.21.79
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perforin
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t-cells
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cd8
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cytolytic
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immunotherapy
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vaccine
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lymphoma
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rejection
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tnf
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dendritic
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cell-mediated
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ifn-gamma
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allograft
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tregs
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tia-1
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fasl
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foxp3
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autologous
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interferon-gamma
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caspases
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degranulation
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allogeneic
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epstein-barr
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antigen-specific
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virus-specific
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immunophenotype
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ctla-4
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anti-cd3
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tumor-infiltrating
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nk-cell
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extranodal
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elispot
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synthesis
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eomes
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graft-versus-leukemia
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cd45ro
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alcls
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biotechnology
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death-1
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analysis
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intragraft
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lag-3
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hiv-specific
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medicine
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diagnostics
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degradation
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alloreactive
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lymphocyte-mediated
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lymphokine-activated
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crma
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b-mediated
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pharmacology
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ag-specific
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banff
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hepatosplenic
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anti-pd-1
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interleukin-15
- 3.4.21.79
- perforin
- t-cells
- cd8
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cytolytic
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immunotherapy
- vaccine
- lymphoma
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rejection
- tnf
- dendritic
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cell-mediated
- ifn-gamma
-
allograft
-
tregs
- tia-1
- fasl
- foxp3
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autologous
- interferon-gamma
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caspases
-
degranulation
-
allogeneic
-
epstein-barr
-
antigen-specific
-
virus-specific
-
immunophenotype
-
ctla-4
-
anti-cd3
-
tumor-infiltrating
-
nk-cell
-
extranodal
-
elispot
- synthesis
-
eomes
-
graft-versus-leukemia
-
cd45ro
-
alcls
- biotechnology
-
death-1
- analysis
-
intragraft
- lag-3
-
hiv-specific
- medicine
- diagnostics
- degradation
-
alloreactive
-
lymphocyte-mediated
-
lymphokine-activated
- crma
-
b-mediated
- pharmacology
-
ag-specific
-
banff
-
hepatosplenic
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anti-pd-1
- interleukin-15
Reaction
preferential cleavage: -Asp-/- >> -Asn-/- > -Met-/-, -Ser-/- =
Synonyms
Asp-ase, C11, CCP1, CCPII, CTLA1, CTSGL1, Cytotoxic cell proteinase-1, cytotoxic lymphocyte-associated protease, cytotoxic lymphocyte-specific protein, cytotoxic serine protease granzyme B, cytotoxic T-lymphocyte-associated gene transcript-1, gB, Gra-b, granzyme B, Granzyme G, Granzyme H, GrB, GrzmB, GzB, Gzm, Gzm B, GzmB, GzmB-like enzyme, GzmH, HLp, Human lymphocyte protein, Lymphocyte protease, natural killer cell protease 1, pro-apoptotic serine protease, proGrB, Proteinase, CCP1, rat grB[N66Q], SECT, T-cell serine protease 1-3E
ECTree
3.4.21.79 granzyme BAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.21.79 - granzyme B
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
interleukin IL-1alpha + H2O
?
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cleavage after the motif IAND103, no substrate for caspases -1, -3, -4, -5, and -7
granzyme B-mediated processing of IL-1alpha potently enhances the biological activity
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?
interleukin proIL-18 + H2O
interleukin IL-18 + ?
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cleavage at residues D35-Y36 of proIL-18, identical to cleavage site of caspase-1
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?
Notch1 + H2O
?
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transmembrane receptor, Notch1 is a direct and caspase-independent substrate. GrB cleaves the intracellular Notch1 domain at least twice, at residues D1860 and D1961. GrB cleavage of Notch1 can occur in all subcellular compartments, during maturation of the receptor, at the membrane, and in the nucleus. GrB also displays perforin-independent functions by cleaving the extracellular domain of Notch1
cleavage of Notch1 by GrB results in a loss of transcriptional activity, independent of Notch1 activation. GrB disables Notch1 function, probably resulting in anti-cellular proliferation and cell death signals
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?
peptidylarginine deiminase 4 + H2O
PAD4 peptides
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GrB cleaves PAD4 exclusively at D388
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?
transaldolase + H2O
?
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specifically cleaved by human GrB. The recognition site is a VVAD motif at aa residue 27
the major C-terminal GrB cleavage product of transaldolase, residues 28-337, has no enzymatic activity but retains the antigenicity of full-length transaldolase, effectively stimulating the proliferation and cytotoxic lymphocyte activity of peripheral blood mononuclear cells and of CD8+ T cell lines from patients with multiple sclerosis. Sera of multiple sclerosis patients exhibit similar binding affinity to wild-type and GrB-cleaved transaldolase
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?
Vitronectin + H2O
?
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Grb expressed in human bladder cancer cell lines 1512 and RT112 cleave vitronectin
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?
DNA-PKcs + H2O
?
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directly and efficiently cleaved in vitro and in vivo, abolishes kinase activity
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?
pro-mCASP-3 + H2O
caspase-3 + ?
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activational cleavage of the caspase proform
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?
pro-mCASP-7 + H2O
caspase-7 + ?
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activational cleavage of the caspase proform
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?
additional information
?
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plays an essential role in cytotoxic T-lymphocyte-mediated cell killing
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?
additional information
?
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the enzyme cleaves and activates CPP32, the precursor of the protease responsible for cleavage of poly(ADPribose)polymerase
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?
additional information
?
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participates in target cell death inflicted by cytotoxic lymphocytes
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?
additional information
?
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induces apoptosis of abnormal cells by cleaving intracellular proteins
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?
additional information
?
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protects the organism against intracellular infections and cellular transformation, implicated in the generation of tissue damage in a variety of chronic conditions, including autoimmunity and transplant rejection
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?
additional information
?
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triggers apoptosis in target cells by activating the caspase pathway, implicated in the etiology of rheumatoid arthritis
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?
additional information
?
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triggers apoptosis in target cells by activating the caspase pathway, implicated in the etiology of rheumatoid arthritis <6>
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?
additional information
?
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after prolonged incubation, enzyme causes pronounced morphological changes in human tumor cells, leading to partial loss of contact to the culture support
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?
additional information
?
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compared with granzyme B, granzyme A is minor effector of target cell lysis by natural killer cells
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?
additional information
?
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granzyme B cleaves a highly conserved set of proteins in all three bacteria, i.e. Escherichia coli, Listeria monocytogenes, and Mycobacteria tuberculosis, which function in vital biosynthetic and metabolic pathways that are critical for bacterial survival under diverse environmental conditions. Key proteins required for protein synthesis, folding and degradation are also substrates, including multiple aminoacyl-tRNA synthetases, ribosomal proteins, protein chaperones and the Clp system. GzmB cleaves core metabolic enzymes and disrupts protein synthesis globally. GzmB disrupts Escherichia coli ribosomes (crude ribosomal fraction or purified 70S, 50S and 30S subunits) by cleaving ribosome proteins. GzmB cleaves and inactivates aminoacyl tRNA synthetases. And GzmB disrupts bacterial protein folding and removal of misfolded proteins. Substrate specificity and metabolic effect of granzyme B, overview
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?
additional information
?
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granzyme B cleaves a highly conserved set of proteins in all three bacteria, i.e. Escherichia coli, Listeria monocytogenes, and Mycobacteria tuberculosis, which function in vital biosynthetic and metabolic pathways that are critical for bacterial survival under diverse environmental conditions. Key proteins required for protein synthesis, folding and degradation are also substrates, including multiple aminoacyl-tRNA synthetases, ribosomal proteins, protein chaperones and the Clp system. GzmB cleaves core metabolic enzymes and disrupts protein synthesis globally. GzmB disrupts Escherichia coli ribosomes (crude ribosomal fraction or purified 70S, 50S and 30S subunits) by cleaving ribosome proteins. GzmB cleaves and inactivates aminoacyl tRNA synthetases. And GzmB disrupts bacterial protein folding and removal of misfolded proteins. Substrate specificity and metabolic effect of granzyme B, overview
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?
additional information
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many autoantigens are substrates for the protease granzyme B
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additional information
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involved in cell killing by cytotoxic T lymphocytes, activates the apoptotic death pathway in the target cell
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?
additional information
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both human or mouse BID are highly resistant to cleavage by mouse GrB
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?
additional information
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involved in cell killing by cytotoxic T lymphocytes, activates the apoptotic death pathway in the target cell
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?
additional information
?
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mediates cell death by cytotoxic lymphocytes
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?
