ArticleProceedings of the National Academy of Sciences of the United States of America1990
Mutagenesis of essential functional residues in acetylcholinesterase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 139 citations in OpenAlex.
- Article
- Novel Sulfonamide-Based Carbamates as Selective Inhibitors of BChE.International journal of molecular sciences · 2021Article
- Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif.Protein science : a publication of the Protein Society · 2021Article
- Structural insights into the putative bacterial acetylcholinesterase ChoE and its substrate inhibition mechanism.The Journal of biological chemistry · 2020Article
- 2D-SAR and 3D-QSAR analyses for acetylcholinesterase inhibitors.Molecular diversity · 2017Article
- Functional characterization of a juvenile hormone esterase related gene in the moth Sesamia nonagrioides through RNA interference.PloS one · 2013Article
- Naturally occurring variations in the human cholinesterase genes: heritability and association with cardiovascular and metabolic traits.The Journal of pharmacology and experimental therapeutics · 2011Article
- Association between arsenic exposure and plasma cholinesterase activity: a population based study in Bangladesh.Environmental health : a global access science source · 2010Article
- Thermal denaturation of wild type and mutant recombinant acetylcholinesterase from amphioxus: effects of the temperature of in vitro expression and of reversible inhibitors.Invertebrate neuroscience : IN · 2008Article
- Article
- N-acetylanthranilate amidase from Arthrobacter nitroguajacolicus Rü61a, an alpha/beta-hydrolase-fold protein active towards aryl-acylamides and -esters, and properties of its cysteine-deficient variant.Journal of bacteriology · 2006Article
- Structural insights into substrate traffic and inhibition in acetylcholinesterase.The EMBO journal · 2006Article
- Influence of the water structure on the acetylcholinesterase efficiency.Biophysical journal · 2005Article
- Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.Journal of bacteriology · 1999Article
- Two invertebrate acetylcholinesterases show activation followed by inhibition with substrate concentration.The Biochemical journal · 1998Article
- Aging of phosphylated human acetylcholinesterase: catalytic processes mediated by aromatic and polar residues of the active centre.The Biochemical journal · 1996Article
- Evidence for a Zn(2+)-binding site in human serum butyrylcholinesterase.The Biochemical journal · 1996Article
- Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene.American journal of human genetics · 1996Article
- Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Structure, expression and gene sequence of a juvenile hormone esterase-related protein from metamorphosing larvae of Trichoplusia ni.The Biochemical journal · 1994Article
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
The cholinesterases are serine hydrolases that show no global similarities in sequence with either the trypsin or the subtilisin family of serine proteases. The cholinesterase superfamily includes several esterases with distinct functions and other proteins devoid of the catalytic serine and known esterase activity. To identify the residues involved in catalysis and conferring specificity on the enzyme, we have expressed wild-type Torpedo acetylcholinesterase (EC 3.1.1.7) and several site-directed mutants in a heterologous system. Mutation of serine-200 to cysteine results in diminished activity, while its mutation to valine abolishes detectable activity. Two conserved histidines can be identified at positions 425 and 440 in the cholinesterase family; glutamine replacement at position 440 eliminates activity whereas the mutation at 425 reduces activity only slightly. The assignment of the catalytic histidine to position 440 defines a rank ordering of catalytic residues in cholinesterases distinct from trypsin and subtilisin and suggests a convergence of a catalytic triad to form a third, distinct family of serine hydrolases. Mutation of glutamate-199 to glutamine yields an enzyme with a higher Km and without the substrate-inhibition behavior characteristic of acetylcholinesterase. Hence, modification of the acidic amino acid adjacent to the serine influences substrate association and the capacity of a second substrate molecule to affect catalysis.
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