| IED ID | IndEnz0005001028 |
| Enzyme Type ID | lipase001028 |
| Protein Name |
Chlorogenic acid esterase EC 3.1.1.42 |
| Gene Name | chlE |
| Organism | Ustilago maydis (Corn smut fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Basidiomycota Ustilaginomycotina Ustilaginomycetes Ustilaginales Ustilaginaceae Ustilago Ustilago maydis (Corn smut fungus) |
| Enzyme Sequence | MRLPNLTLLVWAATSVGLVSALPQVSYKADATASAPTVKLHQGTVRGLADDNYGLEQFFGIPYAKPPVGSLRFAKPQPLGPASSHKTVIDATRFGDICMQTVAPSPLYNMSEDCLNLNVVRPKGTTAKDKLPVLVWIYGGAFRQGSTPIYNASELVQKSVEIGKPIVFVAISYRVGPFGFIGGSEIADSDSATSNAGLYDQRLGLKWIRHNIGKFGGDKNRVTLFGQSAGAMSIALQNFAYDGNNHGLWHAAIMNSGGIAPGPLLTPKHPTVEQSFKRLANGVGCTGGSLLRCLRKANASEVQTVASNLTAQAGGTFPIPGALAWLPLVDYELITNYPSVNLPQGKLADIPVIQGNALDEGTSFAQKQLNSSADFERWVRSAAVIHNTSYTEQALQKVFELYPDVPEQGSPFYNAETATSAATTSDLNSRQYPPLTSNQYKRSAAFFGDFTFQAQRRTYLKAATLGWKKNKAKVWSYEFQQNDKFANGTGSLLGPYHGADVKYYFIRPDGRQKDPVLADRMPRAYISFVYHHDPTVLGGFEWPPYGKGKKLLQMKGDNTTVIEDAYRKEAMDALTNRKAAKVFGF |
| Enzyme Length | 585 |
| Uniprot Accession Number | A0A060S684 |
| Absorption | |
| Active Site | ACT_SITE 228; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:P21836; ACT_SITE 360; /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|Ref.1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20690; Evidence={ECO:0000269|Ref.1}; |
| DNA Binding | |
| EC Number | 3.1.1.42 |
| Enzyme Function | FUNCTION: Extracellular chlorogenic acid esterase that displays a surprisingly broad substrate profile (Ref.1). The enzyme's unique properties may contribute to the specific environmental interaction between the pathogenic fungus and its host, Zea mays (Ref.1). Additionally, the release of caffeic, p-coumaric, and ferulic acids from agroindustrial by-products such as destarched wheat bran (DSWB) and coffee pulp (CP) renders this enzyme an attractive candidate for the generation of natural aroma precursors and antioxidants (Ref.1). {ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000303|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000303|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (2); Glycosylation (8); Signal peptide (1) |
| Keywords | Disulfide bond;Glycoprotein;Hydrolase;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 63,689 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19.6 uM for chlorogenic acid {ECO:0000269|Ref.1}; KM=64.1 uM for methyl p-coumarate {ECO:0000269|Ref.1}; KM=72.5 uM for methyl caffeate {ECO:0000269|Ref.1}; KM=101.8 uM for methyl ferulate {ECO:0000269|Ref.1}; |
| Metal Binding | |
| Rhea ID | RHEA:20689; RHEA:20690 |
| Cross Reference Brenda | 3.1.1.42; |