IED ID | IndEnz0005000491 |
Enzyme Type ID | lipase000491 |
Protein Name |
3-O-acetylpapaveroxine carboxylesterase CXE2 EC 3.1.1.105 Carboxylesterase 2 |
Gene Name | CXE2 |
Organism | Papaver somniferum (Opium poppy) |
Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae Ranunculales Papaveraceae Papaveroideae Papaver Papaver somniferum (Opium poppy) |
Enzyme Sequence | MADPYEFLMCIHDPEEDTLTRNFPIPATPLDQNTKDISLNLDRKTSLRIFRPPTEEFCVTTNKLLPIIIYFHGGGFVLFNADSTINHDFCQSIATHLPALVVSVDYRLAPENRLPAAYDDAVDALNWVKDQGLGKLNNSEVWLKEYGDFSKCFIMGCSSGGNIAYHASLRAIEMDLEPVIINGLILHSPFFGSLQRTESDLKVINDQDLPLAVRDVMWELALPLGSSRDHVYCNPNIANDGSSSGNMAGLIKRCLVIGFYGDPLIDRQIQLVKMLEEKGVKVETWIEQEGYHGVPCFDPKIRETLLGKIKYFI |
Enzyme Length | 313 |
Uniprot Accession Number | A0A0A1EQ07 |
Absorption | |
Active Site | ACT_SITE 158; /evidence=ECO:0000250|UniProtKB:Q5NUF3; ACT_SITE 262; /evidence=ECO:0000250|UniProtKB:Q5NUF3; ACT_SITE 292; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=3-O-acetylpapaveroxine + H2O = acetate + H(+) + narcotine hemiacetal; Xref=Rhea:RHEA:57400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:141645, ChEBI:CHEBI:141667; EC=3.1.1.105; Evidence={ECO:0000269|PubMed:25485687};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57401; Evidence={ECO:0000305|PubMed:25485687}; |
DNA Binding | |
EC Number | 3.1.1.105 |
Enzyme Function | FUNCTION: Carboxylesterase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:25485687). Converts 3-O-acetylpapaveroxine to narcotine hemiacetal (PubMed:25485687). {ECO:0000269|PubMed:25485687}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Alkaloid biosynthesis. {ECO:0000305}. |
nucleotide Binding | |
Features | Active site (3); Chain (1); Motif (1) |
Keywords | Alkaloid metabolism;Hydrolase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 72..74; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
Gene Encoded By | |
Mass | 35,154 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25.2 uM for 3-O-acetylpapaveroxine {ECO:0000269|PubMed:25485687}; Vmax=1535 nmol/min/mg enzyme with 3-O-acetylpapaveroxine as substrate {ECO:0000269|PubMed:25485687}; |
Metal Binding | |
Rhea ID | RHEA:57400; RHEA:57401 |
Cross Reference Brenda | 3.1.1.105; |