AChE, acetylcholinesterase, DmAChE
Gene model reviewed during 5.47
Annotated transcripts do not represent all supported alternative splices within 5' UTR.
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.55
4.291 (compiled cDNA)
66, 64, 60, 57 (kD)
Homodimer; disulfide-linked. The active unit is formed by non-covalent association of the 55 kDa and 16 kDa subunits.
Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell.
Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but protects the protein against proteolytic digestion.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Ace using the Feature Mapper tool.
Developmental profiles of enzyme activity were carried out. The soluble form is seen only in pupae and adults.
Development profiles of enzyme activity were carried out. The soluble form is seen only in pupae an adults.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Ace in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
Localisation of the Ace-specific RNA in developing wild type and mutant embryos is determined.
Biochemical analysis reveals recombinant Ace produced in insect cells is correctly processed (cleavage of the signal peptide, endoproteolytic cleavage of the precursor, formation of fucnctional dimers and addition of a GPI residue).
In situ hybridisation studies imply that the non-CNS-specific Ace can also be non-neuronal. It is dispensable for the late embryonic development and it does not substitute for the acetylcholine hydrolysing capacity of the CNS-specific enzyme.
Four subclass I cholinesterases (EST4, EST5, EST8 and EST13) are isoforms of Ace.
Tyrosine at position 109 contributes to the conformation of the active site; the Tyr charge is very important for catalytic properties. Sensitivity to organophosphorus and carbamate compounds depends on the residues at position 109: this Tyr is a potential site of resistance for insects to insecticides.
13 strains of D.melanogaster were isolated that showed resistance to parathion. The level of resistance varied among the strains implying that several forms of Ace exist, the mutations responsible for insecticide resistance are not described.
Comparison of CpG distribution in the coding region of 121 genes from six species supports the mCpG mutational hotspot explanation of CpG suppression in methylated species at position II-III and III-I.
Protein products identified as EST4, EST5, EST8 and EST9 isozymes.
The kinetics of inhibition of Ace by the carbamate inhibitor eserine sulphate were investigated in five resistant strains.
Cross-hybridization, DNA blot hybridization and hybridization selection experiments demonstrated that the Drosophila and human 2 kb fragments from the vicinity of Ace are directly involved in controlling acetylcholineesterase biosynthesis.
Structural gene for acetyl cholinesterase, the enzyme that terminates synaptic transmission by rapidly hydrolyzing the neurotransmitter acetylcholine. Biochemical analysis (e.g., FBrf0039804; FBrf0046585; FBrf0048054; FBrf0047579; FBrf0048523; FBrf0048525) indicates that the mature enzyme contains noncovalently associated subunits of 16 and 55kD, which are processed from a primary translation product of ca 70kD such that the 16kD moiety is from the N terminus and the 55kD moiety is from the C terminus; two such associations are linked via disulfide bonds connecting the 55kD polypeptides anchored to membrane via a glycoinositol phospholipid anchor covalently linked to the C termini of the 55kD subunits. Extracts contain amphiphilic dimers and monomers as well as hydrophilic dimers and monomers, which lack the glycoinositol phospholipid anchor. Developmental profile studied (FBrf0021148) see also (FBrf0048366); total Ace activity shows a transient peak during first larval instar and rises again to a maximum in the adult. In the developing eye disc, Ace protein first appears in retinula cells three to four days before they are functional and when it cannot have a synaptic function; levels are reduced in retinula cells midway through pupal development and the enzyme accumulates rapidly in the neuropils of the optic lobes of the brain and the midbrain (FBrf0049490). Variation at Ace contributes to variation in the sensitivity of Drosophila to certain insecticides.
Loss of function alleles are recessive lethal dying at end of embryonic stage; then ultrastructural observations of CNS in such mutants suggest neural-degenerative defects (FBrf0047827). Ace-minus tissues survive in mosaics unless enzyme absent from posterior midbrain; surviving mosaics have defective visual physiology, optomotor behavior or courtship, depending on location of mutant clone. Such clones associated with defective morphology or neuropil of various ganglia in central nervous system (FBrf0035219). In temperature-sensitive combinations of Ace mutations (FBrf0035219), both membrane-bound and soluble enzyme has reduced activity (FBrf0050574). All alleles lethal in the hemizygous condition.