3.4.23.50: human endogenous retrovirus K endopeptidase
This is an abbreviated version!
For detailed information about human endogenous retrovirus K endopeptidase, go to the full flat file.
Reaction
Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-/-PIVQ- cleavage site. =
Synonyms
endogenous retrovirus encoded protease, endogenous retrovirus HERV-K10 putative protease, HERV K10 endopeptidase, HERV K10 retropepsin, HERV-K PR, HERV-K protease, HERV-K(HML-2) Pro, HERV-K(HML-2) protease, HERV-K113 protease, HML-2 Pro, human endogenous retrovirus K retropepsin, human endogenous retrovirus K113 protease, human retrovirus K10 retropepsin, More
ECTree
3.4.23.50 human endogenous retrovirus K endopeptidaseAdvanced search results
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results (Cloned
Cloned on EC 3.4.23.50 - human endogenous retrovirus K endopeptidase
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CLONED (Commentary) 
ORGANISM
UNIPROT
LITERATURE
213 amino acids of the 3'-end of the HERV-K protease open reading frame are expressed in Escherichia coli. Autocatalytic cleavage of the expressed polypeptide results in a catalytically active 18200 Da protein
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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
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expression of a full-length and C-terminally truncated enzyme in Escherichia coli
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nucleotide sequence determination and analysis, detailed phylogenetic analysis of virus from primates and humans, and structural analysis of 100 HERV-K(HML-5) provirus sequences, reconstruction of a coding-competent HML-5 provirus, overview
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sequence determination and analysis, expression of wild-type and C-terminally truncated mutant enzymes in Escherichia coli
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targeting of the HERV-K PR to protease-deficient HIV-1 virions by expressing it as a Vpr fusion partner. The Vpr fusion proteins are sucessfully delivered to the HIV-1 virions, where the HERV-K PR not only autoprocesses itself to ist mature form, but also cleaves a number of HIV-1 polyproteins
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the enzyme is expressed either as a full-length native protein or as truncated protein in Escherichia coli
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the HERV-K113 sequence is cloned into a small plasmid vector. It is shown that based on a substantial LTR-promoter activity, full length messenger RNA and spliced env-, rec- and 1.5 kb (hel)-transcripts are produced. Envelope protein of HERV-K113 is synthesized as an 85 kDa precursor that is found partially processed. The accessory Rec protein is highly expressed and accumulates in the nucleus. Expression analysis reveals synthesis of the Gag precursor and the protease in lysates of transfected HEK-293T cells. The cloned HERV-K113 provirus is not replication competent
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