ArticleThe Biochemical journal1997
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 81 citations in OpenAlex.
- Contribution of a C-Terminal Extension to the Substrate Affinity and Oligomeric Stability of Aldehyde Dehydrogenase fromBiochemistry · 2024Article
- Protein overproduction alters exosome secretion in Chinese hamster ovary cells.Analytical and bioanalytical chemistry · 2023Article
- Cryo-electron microscopy of cholinesterases, present and future.Journal of neurochemistry · 2021Review
- Dimerization of human butyrylcholinesterase expressed in bacterium for development of a thermally stable bioscavenger of organophosphorus compounds.Chemico-biological interactions · 2019Article
- Plant-expressed cocaine hydrolase variants of butyrylcholinesterase exhibit altered allosteric effects of cholinesterase activity and increased inhibitor sensitivity.Scientific reports · 2017Article
- Polyclonal Antibodies in Microplates to Predict the Maximum Adsorption Activities of Enzyme/Mutants from Cell Lysates.The protein journal · 2017Article
- Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana.Frontiers in plant science · 2016Article
- Radiometric assay of ghrelin hydrolase activity and 3H-ghrelin distribution into mouse tissues.Biochemical pharmacology · 2015Article
- Reassessment of the role of the central cholinergic system.Journal of molecular neuroscience : MN · 2014Review
- Amino-acid mutations to extend the biological half-life of a therapeutically valuable mutant of human butyrylcholinesterase.Chemico-biological interactions · 2014Article
- Neuronal AChE splice variants and their non-hydrolytic functions: redefining a target of AChE inhibitors?British journal of pharmacology · 2013Review
- The proline-rich tetramerization peptides in equine serum butyrylcholinesterase.The FEBS journal · 2012Article
- His-tag truncated butyrylcholinesterase as a useful construct for in vitro characterization of wild-type and variant butyrylcholinesterases.Protein expression and purification · 2011Article
- Cocrystallization studies of full-length recombinant butyrylcholinesterase (BChE) with cocaine.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Article
- Molecular Assembly and Biosynthesis of Acetylcholinesterase in Brain and Muscle: the Roles of t-peptide, FHB Domain, and N-linked Glycosylation.Frontiers in molecular neuroscience · 2011Article
- The PRiMA-linked cholinesterase tetramers are assembled from homodimers: hybrid molecules composed of acetylcholinesterase and butyrylcholinesterase dimers are up-regulated during development of chicken brain.The Journal of biological chemistry · 2010Article
- Use of a novel radiometric method to assess the inhibitory effect of donepezil on acetylcholinesterase activity in minimally diluted tissue samples.British journal of pharmacology · 2010Article
- The butyrylcholinesterase K variant confers structurally derived risks for Alzheimer pathology.The Journal of biological chemistry · 2009Article
- Model of human butyrylcholinesterase tetramer by homology modeling and dynamics simulation.The journal of physical chemistry. B · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Butyrylcholinesterase (BChE) in human serum consists predominantly of tetramers. Recombinant BChE, however, expressed in Chinese hamster ovary (CHO) cells, consists of approx. 55% dimers, 10-30% tetramers and 15-40% monomers. To determine the origin of the monomer species we added the FLAG epitope (epitope tag, amino acid sequence DYKDDDDK) to the C-terminus of the enzyme, and expressed BChE-FLAG in CHO cells. We found that secreted, active monomers had lost their FLAG epitope, suggesting that the monomers were made by proteolysis of dimers or tetramers at the C-terminus. To estimate the number of amino acids that could be deleted from the C-terminus without losing BChE activity, we expressed deletion mutants. We found that deletion of up to 50 amino acids from the C-terminus yielded active monomers, but that deletion of 51 amino acids destroyed BChE activity and caused the inactive protein to remain within the cell. Deletion of eight or more amino acids from the N-terminus also resulted in inactive protein that remained inside the cell. Monomeric BChE had wild-type Km and kcat values (8 microM and 24000 min-1 for butyrylthiocholine) and showed substrate activation. The Cys-571-->Ala mutant, though incapable of forming the interchain disulphide bond, had nearly the same amount of tetrameric BChE as recombinant wild-type BChE. These results support the conclusion that the tetramerization domain of BChE is at the C-terminus, within the terminal 50 amino acids, and that the interchain disulphide bond is not essential for tetramerization. Molecular modelling suggested that the tetramerization domain was a four-helix bundle, stabilized by interactions of seven conserved aromatic amino acids.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.