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Literature summary extracted from
- Production of 10R-hydroxy unsaturated fatty acids from hempseed oil hydrolyzate by recombinant Escherichia coli cells expressing PpoC from Aspergillus nidulans (2016), Appl. Microbiol. Biotechnol., 100, 7933-7944 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.13.11.62 | synthesis | under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization | Aspergillus nidulans |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.13.11.62 | functional recombinant expression of His-tagged enzyme in Escherichia coli strain ER2566 | Aspergillus nidulans |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.13.11.62 | additional information | under the optimized conditions, the biotechnological production of (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate by enzyme PpoC from Aspergillus nidulans strain ATCC 10074 from linoleic acid, alpha-linolenic acid, and hempseed oil hydrolyzate as substrates is achieved, method optimization, optimization of concentrations of cells and substrate, pH and temperature, for the production of 10R-hydroxy unsaturated fatty acids, overview. Recombinant enzyme PpoC in Escherichia coli cells is more stable than the purified recombinant PpoC | Aspergillus nidulans |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.62 | alpha-linolenate + O2 | Aspergillus nidulans | - |
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate | - |
? |  |
| 1.13.11.62 | alpha-linolenate + O2 | Aspergillus nidulans ATCC 10074 | - |
(8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate | - |
? | |
| 1.13.11.62 | linoleate + O2 | Aspergillus nidulans | - |
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate | - |
? | |
| 1.13.11.62 | linoleate + O2 | Aspergillus nidulans ATCC 10074 | - |
(8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate | - |
? | |
| 1.13.11.62 | additional information | Aspergillus nidulans | the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate | ? | - |
? | |
| 1.13.11.62 | additional information | Aspergillus nidulans ATCC 10074 | the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.13.11.62 | Aspergillus nidulans | - |
- |
- |
| 1.13.11.62 | Aspergillus nidulans ATCC 10074 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.13.11.62 | recombinant His-tagged enzyme from Escherichia coli strain ER2566 by nickel affinity chromatography and ultafiltration | Aspergillus nidulans |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.62 | 0.065 | - |
purified recombinant enzyme, substrate oleate, pH 8.0, 30°C | Aspergillus nidulans |
| 1.13.11.62 | 0.108 | - |
purified recombinant enzyme, substrate palmitoleate, pH 8.0, 30°C | Aspergillus nidulans |
| 1.13.11.62 | 0.485 | - |
purified recombinant enzyme, substrate alpha-linolenate, pH 8.0, 30°C | Aspergillus nidulans |
| 1.13.11.62 | 0.761 | - |
purified recombinant enzyme, substrate linoleate, pH 8.0, 30°C | Aspergillus nidulans |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.13.11.62 | alpha-linolenate + O2 | - |
Aspergillus nidulans | (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate | - |
? | |
| 1.13.11.62 | alpha-linolenate + O2 | moderate activity | Aspergillus nidulans | (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate | - |
? | |
| 1.13.11.62 | alpha-linolenate + O2 | - |
Aspergillus nidulans ATCC 10074 | (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate | - |
? | |
| 1.13.11.62 | alpha-linolenate + O2 | moderate activity | Aspergillus nidulans ATCC 10074 | (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate | - |
? | |
| 1.13.11.62 | linoleate + O2 | - |
Aspergillus nidulans | (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate | - |
? | |
| 1.13.11.62 | linoleate + O2 | best substrate | Aspergillus nidulans | (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate | - |
? | |
| 1.13.11.62 | linoleate + O2 | - |
Aspergillus nidulans ATCC 10074 | (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate | - |
? | |
| 1.13.11.62 | additional information | the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate | Aspergillus nidulans | ? | - |
? | |
| 1.13.11.62 | additional information | assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview | Aspergillus nidulans | ? | - |
? | |
| 1.13.11.62 | additional information | the enzyme produces both (8E,10R,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate and (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate from hempseed oil hydrolyzate | Aspergillus nidulans ATCC 10074 | ? | - |
? | |
| 1.13.11.62 | additional information | assay method optimization for the recombinant enzyme exprssed in Escherichia coli, overview | Aspergillus nidulans ATCC 10074 | ? | - |
? | |
| 1.13.11.62 | oleate + O2 | low activity | Aspergillus nidulans | 8-hydroperoxy-9(Z)-octadecenoic acid | - |
? | |
| 1.13.11.62 | palmitoleate + O2 | low activity | Aspergillus nidulans | 8-hydroperoxy-9(Z)-hexadecenoic acid | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.13.11.62 | 10R-dioxygenase | - |
Aspergillus nidulans |
| 1.13.11.62 | PpoC | - |
Aspergillus nidulans |
| 1.13.11.62 | Psi-producing oxygenase | - |
Aspergillus nidulans |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.62 | 30 | - |
recombinant enzyme | Aspergillus nidulans |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.62 | 20 | 40 | over 70% of maximal activity within this range | Aspergillus nidulans |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.62 | 30 | 40 | half-lives of recombinant PpoC in Escherichia coli cells at 30°C, 35°C, and 40°C are 530, 315, and 97 min, respectively, while those of purified recombinant enzyme are 41, 29, and 18 min, respectively. The half-lives of the recombinant enzyme in Escherichia coli cells are 12.9, 10.9, and 5.4fold higher at 30°C, 35°C, and 40°C, respectively, than those of the purified recombinant enzyme, indicating that thermal stability of recombinant PpoC in expressing cells is higher than that of the purified recombinant PpoC | Aspergillus nidulans |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.13.11.62 | 8 | - |
recombinant enzyme | Aspergillus nidulans |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.13.11.62 | evolution | Psi-producing oxygenases (Ppo enzymes) are classified as three enzyme types: PpoA (5,8-diol synthase), PpoB (suggested as 8,11-diol synthase), and PpoC (10R-dioxygenase) | Aspergillus nidulans |
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