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Literature summary for 3.4.21.79 extracted from
- Asp-ase activity of the Opossum granzyme B supports the role of granzyme B as part of anti-viral immunity already during early mammalian evolution (2016), PLoS ONE, 11, e0154886 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| granzyme B cloning from the chymase locus, sequence comparisons and phylogenetic analysis, recombinant expression of inactive enzyme with N-terminal His6-tag followed by an enterokinase (EK) site in HEK 293 EBNA cells | Monodelphis domestica |
| sequence comparisons and phylogenetic analysis, recombinant expression of inactive enzyme with N-terminal His6-tag followed by an enterokinase (EK) site in HEK 293 EBNA cells | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P10144 | - |
- |
| Monodelphis domestica | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzyme possibly contains N-linked carbohydrates | Monodelphis domestica |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged inactive enzyme from HEK 293 EBNA cells by nickel affinity chromatography, activation by enterokinase proteolytic cleavage | Monodelphis domestica |
| recombinant His6-tagged inactive enzyme from HEK 293 EBNA cells by nickel affinity chromatography, activation by enterokinase proteolytic cleavage | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| mast cell | - |
Monodelphis domestica | - |
| mast cell | - |
Homo sapiens | - |
| T-lymphocyte | the enzyme is primarily expressed by cytotoxic T cells | Monodelphis domestica | - |
| T-lymphocyte | the enzyme is primarily expressed by cytotoxic T cells | Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetyl-IEPD-4-nitroanilide + H2O | an asp-ase substrate | Monodelphis domestica | acetyl-IEPD + 4-nitroaniline | - |
? |  |
| acetyl-IEPD-4-nitroanilide + H2O | an asp-ase substrate, high activity | Homo sapiens | acetyl-IEPD + 4-nitroaniline | - |
? | |
| acetyl-VEID-4-nitroanilide + H2O | an asp-ase substrate | Monodelphis domestica | acetyl-VEID + 4-nitroaniline | - |
? | |
| acetyl-VEID-4-nitroanilide + H2O | an asp-ase substrate, low activity | Homo sapiens | acetyl-VEID + 4-nitroaniline | - |
? | |
| acetyl-YVAD-4-nitroanilide + H2O | an asp-ase substrate | Monodelphis domestica | acetyl-YVAD + 4-nitroaniline | - |
? | |
| additional information | granzyme B (GzmB) is an asp-ase. Granzyme B is a hematopoietic serine protease, which cleaves after negatively charged amino acids. Cleavage specificity analysis using chromogenic and recombinant substrates. Comparisons of GzmB consensus sequences, overview | Monodelphis domestica | ? | - |
? | |
| additional information | granzyme B (GzmB) is an asp-ase. Granzyme B is a hematopoietic serine protease, which cleaves after negatively charged amino acids. Cleavage specificity analysis using chromogenic and recombinant substrates. Comparisons of GzmB consensus sequences, overview | Homo sapiens | ? | - |
? | |
| additional information | human GzmB cleaves only two of the three asp-ase substrates (no activity with acetyl-YVAD-4-nitroanilide) and not the chymase substrate succinyl-AAPF-4-nitroanilide or the two elastase substrates, succinyl-AAPV-4-nitroanilide and succinyl-AAPA-4-nitroanilide. This indicates a broader specificity against different asp-ase substrates for the opossum GzmB compared to human GzmB. Also no activity of the oppossum GznB with N-(tert-butoxycarbonyl)-VLGR-4-nitroanilide (a tryptase substrate), N-benzyloxycarbonyl-GPR-4-nitroanilide (a tryptase substrate), succinyl-AAPI-4-nitroanilide (an elastase substrate), succinyl-AAPL-4-nitroanilide, and succinyl-LLVY-4-nitroanilide (a chymase substrate). Both opossum and human GzmB prefer the rat GzmB consensus sequence. The rat GzmB consensus sequence contains two negatively charged amino acids in the P1 and P3 positions of the substrate. The cleavage of these substrates results in two clearly separated smaller bands, indicating cleavage only at one site in the middle of the linker sequence. Human GzmB cleaves the human substrate sequence (LIGAD-VLVQ) almost as efficiently as the rat GzmB consensus (LIETD-SGL) | Homo sapiens | ? | - |
? | |
| additional information | opossum GzmB cleaves all three asp-ase substrates but not the chymase substrate succinyl-AAPF-4-nitroanilide or the two elastase substrates, succinyl-AAPV-4-nitroanilide and succinyl-AAPA-4-nitroanilide. This indicates a broader specificity against different asp-ase substrates for the opossum GzmB compared to human GzmB. Also no activity of the oppossum GznB with N-(tert-butoxycarbonyl)-VLGR-4-nitroanilide (a tryptase substrate), N-benzyloxycarbonyl-GPR-4-nitroanilide (a tryptase substrate), succinyl-AAPI-4-nitroanilide (an elastase substrate), succinyl-AAPL-4-nitroanilide, and succinyl-LLVY-4-nitroanilide (a chymase substrate). The opossum GzmB shows the relatively strict specificity for negatively charged amino acids in the P1 position. Both opossum and human GzmB prefer the rat GzmB consensus sequence. The rat GzmB consensus sequence contains two negatively charged amino acids in the P1 and P3 positions of the substrate. The cleavage of these substrates results in two clearly separated smaller bands, indicating cleavage only at one site in the middle of the linker sequence. The opossum enzyme cleaves the rat consensus substrate (LIETD-SGL) 5-7 times better than the mouse consensus sequence (LIGFD-VGVQ) with almost no cleavage of the human consensus substrate (LIGAD-VLVQ) | Monodelphis domestica | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 38000, recombinant inactive enzyme, SDS-PAGE, x * 37000, recombinant enterokinase-activated enzyme, SDS-PAGE | Homo sapiens |
| ? | x * 42000, recombinant inactive enzyme, SDS-PAGE, x * 39000, recombinant enterokinase-activated enzyme, SDS-PAGE | Monodelphis domestica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Asp-ase | - |
Monodelphis domestica |
| Asp-ase | - |
Homo sapiens |
| GzmB | - |
Monodelphis domestica |
| GzmB | - |
Homo sapiens |
| GzmB-like enzyme | - |
Monodelphis domestica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Monodelphis domestica |
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Monodelphis domestica |
| 7.5 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the identification of a granzyme B homologue with aspase (cleaving after aspartic acid) specificity in a non-placental mammal provides strong indications that caspase or Bid-dependent apoptosis by a serine protease with a conserved primary specificity has been part of anti-viral immunity since early mammalian evolution. An asp-ase together with a chymase were the first two serine protease genes to appear in the mammalian chymase locus. The mast cell chymase and GzmB were the first two enzymes to appear in this locus. Granzyme B is the only member of the hematopoietic serine proteases, which cleaves after negatively charged amino acids. Phylogenetic analysis and tree, overview | Monodelphis domestica |
| evolution | the identification of a granzyme B homologue with aspase (cleaving after aspartic acid) specificity in a non-placental mammal provides strong indications that caspase or Bid-dependent apoptosis by a serine protease with a conserved primary specificity has been part of anti-viral immunity since early mammalian evolution. An asp-ase together with a chymase were the first two serine protease genes to appear in the mammalian chymase locus. The mast cell chymase and GzmB were the first two enzymes to appear in this locus. Granzyme B is the only member of the hematopoietic serine proteases, which cleaves after negatively charged amino acids. Phylogenetic analysis and tree, overview | Homo sapiens |
| physiological function | Asp-ase activity of the Opossum granzyme B supports the role of granzyme B as part of anti-viral immunity | Monodelphis domestica |
| physiological function | Asp-ase activity of the Opossum granzyme B supports the role of granzyme B as part of anti-viral immunity | Homo sapiens |
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