| IED ID | IndEnz0005001017 |
| Enzyme Type ID | lipase001017 |
| Protein Name |
Chlorogenic acid esterase EC 3.1.1.42 Chlorogenic acid hydrolase CGA hydrolase |
| Gene Name | chlE |
| Organism | Aspergillus niger |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Circumdati Aspergillus niger |
| Enzyme Sequence | MLLRLCIIATLLVSHCVAVSTSPATRDTNGEGLLVQTSSGPIQGFFNQTAPDVRQWLGVPFAEPPVGDLRFSSPVKKQPNGTVNAFALPSSCIQQTSNSSTIYTTYETGFLISGGDSEDCLYLSIWAPRIENIQSQQRPLPVLLYIPGGGFTSGGEASLYKIPDKWVQRTQSHIVVIMNYRVNVFGFPNAEGLSEPNVGLLDQRMAVEWVAANIANFGGDPARIALWGQSAGAASVTAYSYGYPEDPIVAALIADSGAPNIVDNEDYAHTNFTFLASLVGCDGLSSTEELSCMRNVSARKLQTALSTYSGSPSISFTPAVDNKTFFANWTERAITGKVAKIPLITGSNTNEGAGFVSFTPAGPSKSTLFEITESIIACPVAEEVKNRNLANLTTYRYQYAGNFTNISPLPWFGAYHSAELPILFGTHYEYGGPSTQYEWDVSYAMQALWLSFVEDPTRGPVRLAVGNVPANPTNESYFAWPAFEQGSDDLLVFAEGGKVMQLVGAGRIDDYC |
| Enzyme Length | 512 |
| Uniprot Accession Number | A7YN26 |
| Absorption | |
| Active Site | ACT_SITE 230; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:P21836; ACT_SITE 351; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P21836; ACT_SITE 416; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P21836 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=chlorogenate + H2O = (E)-caffeate + H(+) + L-quinate; Xref=Rhea:RHEA:20689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, ChEBI:CHEBI:57644, ChEBI:CHEBI:57770; EC=3.1.1.42; Evidence={ECO:0000269|PubMed:17630312};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20690; Evidence={ECO:0000269|PubMed:17630312}; |
| DNA Binding | |
| EC Number | 3.1.1.42 |
| Enzyme Function | FUNCTION: Extracellular chlorogenic acid esterase that releases caffeic acid from chlorogenic acid (CGA) contained in natural substrates such as apple marc and coffee pulp (PubMed:17630312). Shows no activity towards 5-O-p-coumaroyl quinic acid, another quinic ester derivative, and rosmarinic acid, another caffeic ester derivative (PubMed:17630312). {ECO:0000269|PubMed:17630312}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000303|PubMed:17630312}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000303|PubMed:17630312}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Glycosylation (10); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17630312}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,265 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.5 uM for chlorogenic acid {ECO:0000269|PubMed:17630312}; Vmax=250 nmol/sec/mg enzyme towards chlorogenic acid {ECO:0000269|PubMed:17630312}; |
| Metal Binding | |
| Rhea ID | RHEA:20689; RHEA:20690 |
| Cross Reference Brenda | 3.1.1.42; |