Matches in SemOpenAlex for { <https://semopenalex.org/work/W3117432512> ?p ?o ?g. }
Showing items 1 to 83 of
83
with 100 items per page.
- W3117432512 endingPage "5" @default.
- W3117432512 startingPage "5" @default.
- W3117432512 abstract "The genes for acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) encode the proteins responsible for enzyme activity. Additional gene products, PRiMA and ColQ, anchor AChE and BChE proteins into membranes. Soluble AChE and BChE tetramers are composed of four identical subunits plus one polyproline-rich peptide. Dilution does not release the polyproline-rich peptide from tetramers. However, protein denaturation, for example, heating in a boiling water bath, dissociates the polyproline-rich peptide. Using mass spectrometry to sequence peptides released from soluble AChE and BChE tetramers, we find sequences that correspond to proline-rich regions from a variety of proteins. A typical peptide sequence contains 20 consecutive prolines in a 23-residue peptide, LPPPPPPPPPPPPPPPPPPPPLP. There is no single, common consensus sequence, i.e., no specific gene appears to be responsible for the polyproline-rich peptides found in soluble AChE and BChE tetramers. We propose that during metabolic turnover, protein fragments containing polyproline-rich sequences are scavenged by AChE and BChE dimers, to make stable AChE and BChE tetramers. The 40-residue, alpha-helical C-terminus of AChE or BChE is the tetramerization domain that binds the polyproline-rich peptide. Four parallel alpha helices wrap around a single antiparallel polyproline peptide to lock the tetramer in place. This organization was established by classical X-ray crystallography for isolated C-termini in complex with a proline-rich peptide. The organization was confirmed for intact, tetrameric human BChE using cryoelectron microscopy. When 40 amino acids are deleted from the carboxy terminus, monomeric enzymes are created that retain full enzymatic activity." @default.
- W3117432512 created "2021-01-05" @default.
- W3117432512 creator A5027670892 @default.
- W3117432512 creator A5085576102 @default.
- W3117432512 date "2020-12-31" @default.
- W3117432512 modified "2023-09-23" @default.
- W3117432512 title "Polyproline-Rich Peptides Organize Four Cholinesterase Subunits into a Tetramer; BChE and AChE Scavenge Polyproline Peptides Released during Metabolic Turnover" @default.
- W3117432512 cites W1510064740 @default.
- W3117432512 cites W1525063953 @default.
- W3117432512 cites W1631494369 @default.
- W3117432512 cites W1968294331 @default.
- W3117432512 cites W1990799654 @default.
- W3117432512 cites W1996783938 @default.
- W3117432512 cites W2020398703 @default.
- W3117432512 cites W2036010236 @default.
- W3117432512 cites W2037871774 @default.
- W3117432512 cites W2052906906 @default.
- W3117432512 cites W2055855403 @default.
- W3117432512 cites W2080938801 @default.
- W3117432512 cites W2084316147 @default.
- W3117432512 cites W2089488572 @default.
- W3117432512 cites W2161980109 @default.
- W3117432512 cites W2258278067 @default.
- W3117432512 cites W2290918185 @default.
- W3117432512 cites W2334222304 @default.
- W3117432512 cites W2582961509 @default.
- W3117432512 cites W2727003613 @default.
- W3117432512 cites W2807777635 @default.
- W3117432512 cites W2889365902 @default.
- W3117432512 cites W2899015270 @default.
- W3117432512 cites W2905032349 @default.
- W3117432512 doi "https://doi.org/10.3390/proceedings2020062005" @default.
- W3117432512 hasPublicationYear "2020" @default.
- W3117432512 type Work @default.
- W3117432512 sameAs 3117432512 @default.
- W3117432512 citedByCount "0" @default.
- W3117432512 crossrefType "journal-article" @default.
- W3117432512 hasAuthorship W3117432512A5027670892 @default.
- W3117432512 hasAuthorship W3117432512A5085576102 @default.
- W3117432512 hasBestOaLocation W31174325121 @default.
- W3117432512 hasConcept C104317684 @default.
- W3117432512 hasConcept C109300003 @default.
- W3117432512 hasConcept C167625842 @default.
- W3117432512 hasConcept C181199279 @default.
- W3117432512 hasConcept C185592680 @default.
- W3117432512 hasConcept C2778816929 @default.
- W3117432512 hasConcept C2778886173 @default.
- W3117432512 hasConcept C2779059548 @default.
- W3117432512 hasConcept C2779101902 @default.
- W3117432512 hasConcept C2779281246 @default.
- W3117432512 hasConcept C55493867 @default.
- W3117432512 hasConceptScore W3117432512C104317684 @default.
- W3117432512 hasConceptScore W3117432512C109300003 @default.
- W3117432512 hasConceptScore W3117432512C167625842 @default.
- W3117432512 hasConceptScore W3117432512C181199279 @default.
- W3117432512 hasConceptScore W3117432512C185592680 @default.
- W3117432512 hasConceptScore W3117432512C2778816929 @default.
- W3117432512 hasConceptScore W3117432512C2778886173 @default.
- W3117432512 hasConceptScore W3117432512C2779059548 @default.
- W3117432512 hasConceptScore W3117432512C2779101902 @default.
- W3117432512 hasConceptScore W3117432512C2779281246 @default.
- W3117432512 hasConceptScore W3117432512C55493867 @default.
- W3117432512 hasIssue "1" @default.
- W3117432512 hasLocation W31174325121 @default.
- W3117432512 hasOpenAccess W3117432512 @default.
- W3117432512 hasPrimaryLocation W31174325121 @default.
- W3117432512 hasRelatedWork W1968294331 @default.
- W3117432512 hasRelatedWork W1974277443 @default.
- W3117432512 hasRelatedWork W1996733328 @default.
- W3117432512 hasRelatedWork W2142601247 @default.
- W3117432512 hasRelatedWork W2174028532 @default.
- W3117432512 hasRelatedWork W2334222304 @default.
- W3117432512 hasRelatedWork W2359797698 @default.
- W3117432512 hasRelatedWork W3113160596 @default.
- W3117432512 hasRelatedWork W3117432512 @default.
- W3117432512 hasRelatedWork W308895319 @default.
- W3117432512 hasVolume "62" @default.
- W3117432512 isParatext "false" @default.
- W3117432512 isRetracted "false" @default.
- W3117432512 magId "3117432512" @default.
- W3117432512 workType "article" @default.