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Literature summary for 3.4.21.79 extracted from

  • Dotiwala, F.; Sen Santara, S.; Binker-Cosen, A.A.; Li, B.; Chandrasekaran, S.; Lieberman, J.
    Granzyme B disrupts central metabolism and protein synthesis in bacteria to promote an immune cell death program (2017), Cell, 171, 1125-1137 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ClpA unfoldase + H2O Homo sapiens Escherichia coli ClpA ?
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ClpP protease + H2O Homo sapiens Escherichia coli ClpP ?
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ClpS adaptor + H2O Homo sapiens Escherichia coli ClpS ?
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ClpX unfoldase + H2O Homo sapiens Escherichia coli ClpX ?
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additional information Homo sapiens 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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Organism

Organism UniProt Comment Textmining
Homo sapiens P10144
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Source Tissue

Source Tissue Comment Organism Textmining
natural killer cell
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Homo sapiens
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T-lymphocyte cytotoxic T lymphocytes Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ClpA unfoldase + H2O Escherichia coli ClpA Homo sapiens ?
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?
ClpP protease + H2O Escherichia coli ClpP Homo sapiens ?
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?
ClpS adaptor + H2O Escherichia coli ClpS Homo sapiens ?
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?
ClpX unfoldase + H2O Escherichia coli ClpX Homo sapiens ?
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?
ClpX unfoldase + H2O Escherichia coli N-terminal GST-tagged 37kDa ClpX. Human GzmB is predicted to cut ClpX after Asp144, in the AAA domain and interfere with its unfolding activity Homo sapiens ?
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additional information 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 Homo sapiens ?
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?
additional information no activity with Escherichia coli ClpB protein Homo sapiens ?
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?

Synonyms

Synonyms Comment Organism
GzmB
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Homo sapiens

General Information

General Information Comment Organism
physiological function granzyme B disrupts central metabolism and protein synthesis in bacteria to promote an immune cell death program. 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. Because killer cells use a multi-pronged strategy to target vital pathways, bacteria may not easily become resistant to killer cell attack. The cytotoxic granule pore-forming protein, perforin (PFN), delivers the death-inducing granzyme (Gzm) serine proteases into the target cell, where they cleave multiple substrates to kill the target cell. These cytotoxic cells also kill intracellular bacteria and protozoa. Granzymes A and B (Gzms A and B), the most abundant of the five human Gzms, rapidly trigger oxidative bacterial death by cleaving and disrupting electron transport chain complex I (ETC I), which generates toxic superoxide anions. At the same time, the Gzms degrade bacterial oxidative defense enzymes to disrupt the ability of bacteria to survive oxidative stress. GzmB cleavage of Clp system proteins disrupts the Clp function of removing proteins targeted for degradation Homo sapiens