| IED ID | IndEnz0005000207 |
| Enzyme Type ID | lipase000207 |
| Protein Name |
GDSL esterase/lipase ACHE EC 3.1.1.- Acetylcholinesterase AChE |
| Gene Name | ACHE ZEAMMB73_Zm00001d021961 Zm00014a_018493 |
| Organism | Zea mays (Maize) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Liliopsida Petrosaviidae commelinids Poales Poaceae PACMAD clade Panicoideae Andropogonodae Andropogoneae Tripsacinae Zea Zea mays (Maize) |
| Enzyme Sequence | MATAATATAGSRAAVLLLLSLALALALRPSDAGAGGDCHFPAVFNFGDSNSDTGGLSSLFGAAPPPNGRTFFGMPAGRYCDGRLVIDFIAESLGLTHLSAYLNSIGSNFTQGANFATAGSSIRRQNTSLFLSGFSPISLDVQFWEFEQFINRSQLVYNNKGGIYREILPRAEYFSQALYTFDIGQNDITSSYFVNNTTEEVEAIIPDLMERLTSIIQSVYSRGGRYFWIHNTGPLGCLPYALLHRPDLAIPADGTGCSVTYNKVAQLFNLRLKETVASLRKTHPDAAFTYVDVYTAKYKLISQANKLGFDDPLLTCCGYGGGRYNLDLSVGCGGKKQVNGTSVVVGKSCENPSKRVSWDGVHFTEAANKFVFDQIVAGALSDPPVALRQACHSRGQ |
| Enzyme Length | 396 |
| Uniprot Accession Number | B4FZ87 |
| Absorption | |
| Active Site | ACT_SITE 49; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P0ADA1; ACT_SITE 359; /evidence=ECO:0000250|UniProtKB:P0ADA1; ACT_SITE 362; /evidence=ECO:0000250|UniProtKB:P0ADA1 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Esterase that can hydrolyze acetylthiocholine and propionylthiocholine in vitro (PubMed:15980188). Substrate preference is propionylthiocholine > acetylthiocholine (PubMed:15980188). Possesses extremely low activity against butyrylthiocholine (PubMed:15980188). {ECO:0000269|PubMed:15980188}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Glycosylation (5); Sequence conflict (4); Signal peptide (1) |
| Keywords | Direct protein sequencing;Glycoprotein;Hydrolase;Lipid degradation;Lipid metabolism;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000269|PubMed:15980188 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,680 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.7 mM for acetylthiocholine {ECO:0000269|PubMed:15980188}; KM=3.1 mM for propionylthiocholine {ECO:0000269|PubMed:15980188}; Vmax=1.7 umol/min/mg enzyme with acetylthiocholine as substrate {ECO:0000269|PubMed:15980188}; Vmax=1.7 umol/min/mg enzyme with propionylthiocholine as substrate {ECO:0000269|PubMed:15980188}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |