ArticleThe EMBO journal1992
Intramolecular relationships in cholinesterases revealed by oocyte expression of site-directed and natural variants of human BCHE.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 56 citations in OpenAlex.
- The Selectivity of Butyrylcholinesterase Inhibitors Revisited.Molecules (Basel, Switzerland) · 2025Review
- Normal and atypical butyrylcholinesterases in placental development, function, and malfunction.Cellular and molecular neurobiology · 1997Article
- Natural inhibitors of cholinesterases: implications for adverse drug reactions.Canadian journal of anaesthesia = Journal canadien d'anesthesie · 1997Review
- Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene.American journal of human genetics · 1996Article
- Synaptic and epidermal accumulations of human acetylcholinesterase are encoded by alternative 3'-terminal exons.Molecular and cellular biology · 1995Article
- Antisense inhibition of butyrylcholinesterase gene expression predicts adverse hematopoietic consequences to cholinesterase inhibitors.Cellular and molecular neurobiology · 1994Article
- Transgenic engineering of neuromuscular junctions in Xenopus laevis embryos transiently overexpressing key cholinergic proteins.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase.The EMBO journal · 1994Article
- Expression of a human acetylcholinesterase promoter-reporter construct in developing neuromuscular junctions of Xenopus embryos.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins.Protein science : a publication of the Protein Society · 1993Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structure-function relationships of cholinesterases (CHEs) were studied by expressing site-directed and naturally occurring mutants of human butyrylcholinesterase (BCHE) in microinjected Xenopus oocytes. Site-directed mutagenesis of the conserved electronegative Glu441,Ile442,Glu443 domain to Gly441,Ile442,Gln443 drastically reduced the rate of butyrylthiocholine (BTCh) hydrolysis and caused pronounced resistance to dibucaine binding. These findings implicate the charged Glu441,Ile442,Glu443 domain as necessary for a functional CHE catalytic triad as well as for binding quinoline derivatives. Asp70 to Gly substitution characteristic of 'atypical' BCHE, failed to alter its Km towards BTCh or dibucaine binding but reduced hydrolytic activity to 25% of control. Normal hydrolytic activity was restored to Gly70 BCHE by additional His114 or Tyr561 mutations, both of which co-appear with Gly70 in natural BCHE variants, which implies a likely selection advantage for these double BCHE mutants over the single Gly70 BCHE variant. Gly70 BCHE variants also displayed lower binding as compared with Asp70 BCHE to cholinergic drugs, certain choline esters and solanidine. These effects were ameliorated in part by additional mutations or in binding solanidine complexed with sugar residues. These observations indicate that structural interactions exist between N' and C' terminal domains in CHEs which contribute to substrate and inhibitor binding and suggest a crucial involvement of both electrostatic and hydrophobic domains in the build-up of the CHE active center.
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