Enzymes
| UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline chlorogenate Identifier CHEBI:57644 (Beilstein: 6097142) help_outline Charge -1 Formula C16H17O9 InChIKeyhelp_outline CWVRJTMFETXNAD-JUHZACGLSA-M SMILEShelp_outline O[C@@H]1C[C@](O)(C[C@@H](OC(=O)\C=C\c2ccc(O)c(O)c2)[C@@H]1O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (E)-caffeate Identifier CHEBI:57770 (Beilstein: 8986917) help_outline Charge -1 Formula C9H7O4 InChIKeyhelp_outline QAIPRVGONGVQAS-DUXPYHPUSA-M SMILEShelp_outline Oc1ccc(\C=C\C([O-])=O)cc1O 2D coordinates Mol file for the small molecule Search links Involved in 12 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-quinate Identifier CHEBI:29751 Charge -1 Formula C7H11O6 InChIKeyhelp_outline AAWZDTNXLSGCEK-WYWMIBKRSA-M SMILEShelp_outline O[C@@H]1C[C@@](O)(C[C@@H](O)[C@H]1O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:20689 | RHEA:20690 | RHEA:20691 | RHEA:20692 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
|||
| EC numbers help_outline | ||||
| Gene Ontology help_outline | ||||
| KEGG help_outline | ||||
| MetaCyc help_outline |
Publications
-
[Further characterization of a chlorogenic acid hydrolase from Aspergillus niger (author's transl)].
Schobel B., Pollmann W.
In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamide gel electrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis showed a molecular weight of 60 000, demonstra ... >> More
In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamide gel electrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis showed a molecular weight of 60 000, demonstrating four subunits of the enzyme (total molecular weight 240 000). The enzyme is stable in a pH-range of 3.0--8.5 and up to a temperature of 55 degrees C. The temperature coefficient Q10 is 1.5, the activation energy EA is 6.0 kcal/mol. The amino acid analysis and substrate specificity data are given in tables. Essential for the enzyme activity is the C=C double bound neighbouring the ester linkage. The enzyme crystallizes in prisms. << Less
Z Naturforsch C Biosci 35:699-701(1980) [PubMed] [EuropePMC]
-
Coffee pulp koji of Aspergillus sojae as stable immobilized catalyst of chlorogenate hydrolase.
Adachi O., Ano Y., Akakabe Y., Shinagawa E., Matsushita K.
Chlorogenate hydrolase (EC 3.1.1.42, CHase) was highly induced in mycelia of Aspergillus sojae AKU 3312 grown in Czapek medium containing either instant coffee powder or coffee pulp as inducer. No CHase formation was observed in the mycelia when cultivated without the inducer. CHase was purified r ... >> More
Chlorogenate hydrolase (EC 3.1.1.42, CHase) was highly induced in mycelia of Aspergillus sojae AKU 3312 grown in Czapek medium containing either instant coffee powder or coffee pulp as inducer. No CHase formation was observed in the mycelia when cultivated without the inducer. CHase was purified readily from CHase-induced mycelia to high homogeneity, and the purified CHase revealed the molecular weight of 180,000 consisting of two identical subunits of 88 kDa. Equimolar quinate (QA) and caffeate (CA) were confirmed on hydrolysis of chlorogenate (CGA). The purified CHase was only useful for a laboratory scale hydrolysis of CGA. For practical QA and CA production using scaled up hydrolysis of vegetable extracts of natural CGA resources, the enzyme activity of purified CHase decreased and denatured irreversibly. Preparation of coffee pulp koji and its application to QA and CA production were proposed instead of purified CHase. When coffee pulp koji was heated at 60 degrees C for 30 min, CHase survived without any appreciable loss of enzyme activity while vegetative mycelial growth and spore germination were terminated. The heated coffee pulp koji thus prepared was effective itself as stable immobilized catalyst of CHase for QA and CA production from vegetable CGA resources such as coffee powders, coffee pulp, and others. << Less
Appl Microbiol Biotechnol 81:143-151(2008) [PubMed] [EuropePMC]
-
Isolation and characterization of a chlorogenic acid esterase from Aspergillus niger.
Schobel B., Pollmann W.
The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum ... >> More
The isolation and characterization of a specific chlorogenic acid esterase is described. The enzyme activity is measured by determination of the hydrolysis product caffeic acid. The enzyme had been concentrated by means of ultrafiltration and column-chromatography. The pH- and temperature optimum were 6.5 and 45 degrees C respectively. Divalent cations were not required for the enzyme activity. As other esterases, this enzyme is inhibited by di-isopropyl-phosphorofluoridate. The Km-value is 0.70 mM chlorogenic acid, the molecule weight 240 000. The described enzyme is specific for chlorogenic acid. On the other hand a typical unspecific esterase like the pig liver esterases does not split chlorogenic acid. The isoelectric focusing reveals several isoenzymes of chlorogenase within a pI-range of 4.0-4.5. << Less
Z Naturforsch C Biosci 35:209-212(1980) [PubMed] [EuropePMC]