Characteristics of the caspase-like catalytic domain of human paracaspase
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Scott J. Snipas
Abstract
Human paracaspase has been predicted to be a member of the protein structural fold that encompasses protease clan CD. To determine whether paracaspase has catalytic activity we have expressed the region corresponding to the catalytic domain and used protease activity-based chemical probes to profile the putative active site. A leucine-based acyloxymethyl ketone probe that covalently labels cysteine proteases discloses a hydrophobic P1 preference in the putative active site. The probe covalently labels Cys539, which is not the predicted catalytic site based on structural and sequence comparisons with other clan CD proteases. Using a combinatorial peptide substrate library approach we have been unable to detect amidolytic activity of paracaspase, implying that if it is a protease it must be very specific. We suggest a switch in the use of catalytic residues to generate an enzyme overlapping the canonical clan CD protease active site.
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© Walter de Gruyter
Articles in the same Issue
- Hiroshi Maeda – 40 years of research
- Activation of the kallikrein-kinin system and release of new kinins through alternative cleavage of kininogens by microbial and human cell proteinases
- Molecular mechanism for activation and regulation of matrix metalloproteinases during bacterial infections and respiratory inflammation
- Role of bacterial proteases in pseudomonal and serratial keratitis
- Cysteine cathepsins in human cancer
- Secretory leukoprotease inhibitor and pulmonary surfactant serve as principal defenses against influenza A virus infection in the airway and chemical agents up-regulating their levels may have therapeutic potential
- Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases
- Roles of Arg- and Lys-gingipains in coaggregation of Porphyromonas gingivalis: identification of its responsible molecules in translation products of rgpA, kgp, and hagA genes
- Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR
- Genetic characterization of staphopain genes in Staphylococcus aureus
- Visualisation of tissue kallikrein, kininogen and kinin receptors in human skin following trauma and in dermal diseases
- Reduction of myocardial infarction by calpain inhibitors A-705239 and A-705253 in isolated perfused rabbit hearts
- A proteinase inhibitor from Caesalpinia echinata (pau-brasil) seeds for plasma kallikrein, plasmin and factor XIIa
- Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases
- Characteristics of the caspase-like catalytic domain of human paracaspase
- mRNA expression analysis of a variety of apoptosis-related genes, including the novel gene of the BCL2-family, BCL2L12, in HL-60 leukemia cells after treatment with carboplatin and doxorubicin
- Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases
- Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella
Articles in the same Issue
- Hiroshi Maeda – 40 years of research
- Activation of the kallikrein-kinin system and release of new kinins through alternative cleavage of kininogens by microbial and human cell proteinases
- Molecular mechanism for activation and regulation of matrix metalloproteinases during bacterial infections and respiratory inflammation
- Role of bacterial proteases in pseudomonal and serratial keratitis
- Cysteine cathepsins in human cancer
- Secretory leukoprotease inhibitor and pulmonary surfactant serve as principal defenses against influenza A virus infection in the airway and chemical agents up-regulating their levels may have therapeutic potential
- Design of inhibitors against HIV, HTLV-I, and Plasmodium falciparum aspartic proteases
- Roles of Arg- and Lys-gingipains in coaggregation of Porphyromonas gingivalis: identification of its responsible molecules in translation products of rgpA, kgp, and hagA genes
- Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR
- Genetic characterization of staphopain genes in Staphylococcus aureus
- Visualisation of tissue kallikrein, kininogen and kinin receptors in human skin following trauma and in dermal diseases
- Reduction of myocardial infarction by calpain inhibitors A-705239 and A-705253 in isolated perfused rabbit hearts
- A proteinase inhibitor from Caesalpinia echinata (pau-brasil) seeds for plasma kallikrein, plasmin and factor XIIa
- Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases
- Characteristics of the caspase-like catalytic domain of human paracaspase
- mRNA expression analysis of a variety of apoptosis-related genes, including the novel gene of the BCL2-family, BCL2L12, in HL-60 leukemia cells after treatment with carboplatin and doxorubicin
- Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases
- Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella