21 research outputs found
Amino acid sequence of the active site of human serum cholinesterase from usual, atypical, and atypical-silent genotypes
Active-site tryptic peptides were isolated from three genetic types of human serum cholinesterase. The active-site peptide was identified by labeling the active-site serine with [ 3 H] diisopropylfluorophosphate. Peptides were purified by high-performance liquid chromatography. Amino acid composition and sequence analysis showed that the peptide from the usual genotype contained 29 residues with the sequence Ser-Val-Thr-Leu-Phe-Gly-Glu-Ser-Ala-Gly-Ala-Ala-Ser-Val-Ser-Leu-His-Leu-Leu-Ser-Pro-Gly-Ser-His-Ser-Leu-Phe-Thr-Arg. The active-site serine was the eighth residue from the N- terminal. The peptide containing the active-site serine from the atypical genotype contained 22 residues with the sequence Ser-Val-Thr-Leu-Phe-Gly-Glu-Ser-Ala-Gly-Ala-Ala-Ser-Val-Ser-Leu-His-Leu-Leu-Ser-Pro-Gly. The peptide from the atypical-silent genotype contained eight residues with the sequence Gly-Glu-Ser-Ala-Gly-Ala-Ala-Ser. Thus, the sequences of the atypical and atypical-silent active-site peptides were identical to the corresponding portions of the usual peptide.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/44153/1/10528_2004_Article_BF00499101.pd
Preservation of acetylcholinesterase enzyme activity in non-frozen rectal biopsy specimens for Hirschsprung disease
Bivalent Organophosphorus CompoundsβSynthesis and Acetylcholinesterase Inhibitory Activity
Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus
Genome organization, phylogenies, expression patterns, and three-dimensional protein models of two acetylcholinesterase genes from the red flour beetle
Citation: Lu, Y., . . . & Zhu, K. (2012). Genome Organization, Phylogenies, Expression Patterns, and Three-Dimensional Protein Models of Two Acetylcholinesterase Genes from the Red Flour Beetle. PLoS ONE, 7(2).
https://doi.org/10.1371/journal.pone.0032288Since the report of a paralogous acetylcholinesterase (AChE, EC3.1.1.7) gene in the greenbug (Schizaphis graminum) in 2002, two different AChE genes (Ace1 and Ace2) have been identified in each of at least 27 insect species. However, the gene
models of Ace1 and Ace2, and their molecular properties have not yet been comprehensively analyzed in any insect species. In this study, we sequenced the full-length cDNAs, computationally predicted the corresponding three-dimensional protein models, and profiled developmental stage and tissue-specific expression patterns of two Ace genes from the red flour beetle (Tribolium castaneum; TcAce1 and TcAce2), a globally distributed major pest of stored grain products and an emerging model organism. TcAce1 and TcAce2 encode 648 and 604 amino acid residues, respectively, and have conserved motifs including a choline-binding site, a catalytic triad, and an acyl pocket. Phylogenetic analysis show that both TcAce
genes are grouped into two insect Ace clusters and TcAce1 is completely diverged from TcAce2, suggesting that these two
genes evolve from their corresponding Ace gene lineages in insect species. In addition, TcAce1 is located on chromosome 5,
whereas TcAce2 is located on chromosome 2. Reverse transcription polymerase chain reaction (PCR) and quantitative realtime
PCR analyses indicate that both genes are virtually transcribed in all the developmental stages and predominately
expressed in the insect brain. Our computational analyses suggest that the TcAce1 protein is a robust acetylcholine (ACh)
hydrolase and has susceptibility to sulfhydryl agents whereas the TcAce2 protein is not a catalytically efficient ACh hydrolase