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Literature summary for 3.4.23.50 extracted from
- A human endogenous retrovirus encoded protease potentially cleaves numerous cellular proteins (2019), Mob. DNA, 10, 36 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| cloning of HML-2 Pro including self-processing sites and in-frame flanking sequence, HML-2 Pro is prokaryotically expressed. HML-2 Pro self-processes from the precursor during the expression, purification, and renaturation steps. Coexpression of the enzyme with HA-tagged potential human substrate proteins HSPA90AA1, MAP2K2, and C15orf57 in HEK-293 cells. The HEK293T cells harvested after 5 h do not show evidence of processing of candidate proteins due to apoptotic processes | Human endogenous retrovirus K |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | two different, enzymatically inactive mutants of HML-2 Pro harboring mutations in catalytic motifs cannot be purified due to inefficient binding to pepstatin A affinity resin | Human endogenous retrovirus K |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| pepstatin A | a specific inhibitor of retroviral aspartate proteinases | Human endogenous retrovirus K |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Human endogenous retrovirus K | hundreds of cellular proteins are potential substrates of enzyme HERV-K(HML-2) Pro | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Human endogenous retrovirus K | - |
HERV-K | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | recombinant HML-2 Pro, harboring self-processing sites, self-processes from the precursor during the expression, purification, and renaturation steps | Human endogenous retrovirus K |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme by pepstatin A affinity chromatography | Human endogenous retrovirus K |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | hundreds of cellular proteins are potential substrates of enzyme HERV-K(HML-2) Pro | Human endogenous retrovirus K | ? | - |
? | |
| additional information | identification of human cellular proteins that are substrates of HERV-K(HML-2) Pro employing a modified Terminal Amine Isotopic Labeling of Substrates (TAILS) procedure. Confirmation of cleavage of a majority of selected human proteins in vitro and in co-expression experiments in vivo, overview | Human endogenous retrovirus K | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| endogenous retrovirus encoded protease | - |
Human endogenous retrovirus K |
| HERV-K(HML-2) Pro | - |
Human endogenous retrovirus K |
| HERV-K(HML-2) protease | - |
Human endogenous retrovirus K |
| HML-2 Pro | - |
Human endogenous retrovirus K |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
- |
Human endogenous retrovirus K |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 8 | highest activity at pH 5.5, lowest activity at pH 8.0 | Human endogenous retrovirus K |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | hundreds of cellular proteins are potential substrates of enzyme HERV-K(HML-2) Pro. Thus, even low-level expression of HERV-K(HML-2) Pro affects levels of a diverse array of proteins and has a functional impact on cell biology and possible relevance for human diseases | Human endogenous retrovirus K |
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Release 2023.1 (January 2023)
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