Detail Information for IndEnz0005000491
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;