| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | ultrasound application during FeCH extraction leads to an improved enzymatic activity and further increase in the formation of Zn-protoporphyrin (ZnPP) method of increasing the enzyme catalysis, optimization, overview. Improvement of the rate of ZnPP formation with ultrasound extraction by up to 33.3% compared to conventional extraction | Sus scrofa |
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | ultrasound intensification of ferrochelatase extraction from pork liver as a strategy to improve Zn-protoporphyrin formation. Ultrasound application during FeCH extraction leads to an improved enzymatic activity and further increase in the formation of ZnPP, method optimization, overview | Sus scrofa |
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics of ZnPP formation using a FeCH extract from pork liver obtained by conventional and continuous ultrasound extraction for 5 min, the latter resulting in higher activity. And kinetics of ZnPP formation using a FeCH extract from pork liver obtained by continuous ultrasound extraction (US-C) and pulsed ultrasound extraction, the first resulting in higher activity | Sus scrofa |
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| protoporphyrin + Fe2+ | Sus scrofa | - |
protoheme + 2 H+ | - |
? | |
| protoporphyrin + Zn2+ | Sus scrofa | - |
Zn-protoporphyrin + 2 H+ | - |
? |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | A0A287B3T2 | - |
- |
| Purification (Comment) | Organism |
|---|---|
| usage of high power ultrasound in continuous and pulsed modes to intensify the extraction of the enzyme FeCH from pork liver | Sus scrofa |
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Sus scrofa | - |
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the specific enzymatic activity is 7.6 nmol of ZnPP/g dry matter * min and the product forms at 120 min of 684 nmol/l ZnPP, stationary reaction phase measurement | Sus scrofa |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Zn-protoporphyrin (ZnPP) is quantified by fluorescence measurements as the product of the reaction due to its ability to emit fluorescence (unlike myoglobin and nitrosylmyoglobin) with excitation and emission peaks at around 420 nm and 590 nm, respectively | Sus scrofa | ? | - |
- |
|
| protoporphyrin + Fe2+ | - |
Sus scrofa | protoheme + 2 H+ | - |
? | |
| protoporphyrin + Zn2+ | - |
Sus scrofa | Zn-protoporphyrin + 2 H+ | - |
? |
| Synonyms | Comment | Organism |
|---|---|---|
| FeCH | - |
Sus scrofa |
| ferrochelatase | - |
Sus scrofa |
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Sus scrofa |
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Sus scrofa |
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme ferrochelatase (FeCH), which is naturally present in pork liver, catalyses the formation of Zinc-protoporphyrin (ZnPP), a natural pigment responsible for the typical color of dry-cured Italian Parma ham | Sus scrofa |