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Literature summary for 3.4.21.112 extracted from
- Molecular characterization of the processing of arenavirus envelope glycoprotein precursors by subtilisin kexin isozyme-1/site-1 protease (2012), J. Virol., 86, 4935-4946.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| functional expression of full-length wild-type enzyme, which undergoes complete autoprocessing, in SRD12B cells. Recombinant expression HEK-293T and CHO cells, real-time quantitative PCR expression analysis | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
| Golgi apparatus | - |
Homo sapiens | 5794 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required | Homo sapiens |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arenavirus envelope glycoprotein precursor + H2O | Homo sapiens | activation/maturation | ? | - |
? | |
| additional information | Homo sapiens | the enzyme performs autocatalytic cleavage and activation. The cleavage of arenavirus glycoproteins, but not cellular substrates, critically depends on the autoprocessing of the enzyme, suggesting differences in the processing of cellular and viral substrates. The exogenous soluble enzyme is unable to process arenavirus lymphocytic choriomeningitis virus and pathogenic Lassa virus envelope glycoproteins displayed at the surface of enzyme-deficient cells, indicating that glycoprotein processing occurs in an intracellular compartment | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q14703 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the enzyme performs autocatalytic cleavage and activation depending on the recognition site RRLL, present in the enzyme prodomain | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arenavirus envelope glycoprotein precursor + H2O | - |
Homo sapiens | ? | - |
? | |
| arenavirus envelope glycoprotein precursor + H2O | activation/maturation | Homo sapiens | ? | - |
? | |
| Lassa virus envelope glycoprotein precursor + H2O | the enzyme recognition motif RRLL is critical for the processing of the Lassa virus envelope glycoprotein in the endoplasmic reticulum/cis-Golgi compartment | Homo sapiens | ? | - |
? | |
| additional information | the enzyme performs autocatalytic cleavage and activation. The cleavage of arenavirus glycoproteins, but not cellular substrates, critically depends on the autoprocessing of the enzyme, suggesting differences in the processing of cellular and viral substrates. The exogenous soluble enzyme is unable to process arenavirus lymphocytic choriomeningitis virus and pathogenic Lassa virus envelope glycoproteins displayed at the surface of enzyme-deficient cells, indicating that glycoprotein processing occurs in an intracellular compartment | Homo sapiens | ? | - |
? | |
| additional information | the SKI-1/S1P recognition site RRLL is present in the enzyme SKI-1/S1P prodomain and Lassa virus envelope glycoprotein precursor , but not in the lymphocytic choriomeningitis virus envelope glycoprotein precursor, it is crucial for the processing of the Lassa virus glycoprotein in the endoplasmic reticulum/cis-Golgi compartment | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| subtilisin kexin isozyme-1/site-1 protease | - |
Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | soluble enzyme is unable to process arenavirus glycoproteinss at the cell surface | Homo sapiens |
| additional information | the transmembrane anchorage and the cytoplasmic domain of SKI-1/S1P are dispensable for arenavirus glycoprotein processing | Homo sapiens |
| physiological function | a crucial step in the life cycle of arenaviruses is the biosynthesis of the mature fusion-active viral envelope glycoprotein that is essential for virus-host cell attachment and entry. The maturation of the arenavirus envelope glycoprotein precursor critically depends on proteolytic processing by the cellular proprotein convertase subtilisin kexin isozyme-1/site-1 protease | Homo sapiens |
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