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Literature summary extracted from
- Effects of the deglycosylation on the structure and activity of chloroperoxidase molecular dynamics simulation approach (2020), J. Mol. Graph. Model., 97, 107570 .
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.1.10 | Fe2+ | in CPO, the sulfur atom in the Cys29 is located at the appropriate distance from the amide group of the Leu 32 and Glu 51 that leads to the hydrogen bonding formation of the amidesulfur groups, which is important for metalloproteins for the iron alignment | Leptoxyphium fumago |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.10 | RH + chloride + H2O2 | Leptoxyphium fumago | - |
RCl + 2 H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.11.1.10 | Leptoxyphium fumago | P04963 | Caldariomyces fumago | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 1.11.1.10 | glycoprotein | CPO enzyme contains thirteen sugars, including five N-acetyl D-glucosamines (NAG) and eight mannoses (MAN), which are attached to the protein via the glycosidic bonds. Analysis of the effects of the sugar segments on the structure and activity of CPO through the simulation of the halo structure and the structures without the sugar segment, overview. According to molecular dynamics simulation (MD), seven channels and fifteen cavities are identified in the CPO structure. Two of the channels provide the substrate access to the active site. The MD simulation results reveal that the removal of NAG decreases the number of the cavities from fifteen to eleven. Besides, the removal of NAG is associated with removing the channel providing the substrate access. The number of the cavities decreases from fifteen to fourteen through the removal of MAN, but, channel providing the substrate access to the active site is partly preserved. The MD simulation results indicate that the structures without the sugar units are more compact in comparison with the halo structures. The removal of the sugar segments induces the significant changes in the flexibility of the residues that affect the catalytic activity of the enzyme. As a result, the enzyme activities, such as the oxidation, alkylation, halogenation, and epoxidation cannot occur when the sugar segments of the enzyme are removed | Leptoxyphium fumago |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.11.1.10 | RH + chloride + H2O2 | - |
Leptoxyphium fumago | RCl + 2 H2O | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.11.1.10 | chloroperoxidase | - |
Leptoxyphium fumago |
| 1.11.1.10 | CPO | - |
Leptoxyphium fumago |
| 1.11.1.10 | heme-containing CPO | - |
Leptoxyphium fumago |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.10 | 3 | - |
- |
Leptoxyphium fumago |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.11.1.10 | 3 | 6 | high activity at | Leptoxyphium fumago |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.11.1.10 | heme | the heme group of CPO is nonplanar and saddle, with the iron positioned under the main plane of the porphyrin toward the Cys29 ligand. The distal pocket of the heme group in CPO is polar. In the peroxidases, the edge of the heme group is open for the reaction with the substrate, while the direct access to its Fe4+ =O center is limited | Leptoxyphium fumago | |
| 1.11.1.10 | additional information | the enzyme involves the protoporphyrin prosthetic group with the pI range of 3.2-4.0 | Leptoxyphium fumago |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.11.1.10 | Leptoxyphium fumago | the enzyme involves the protoporphyrin prosthetic group with the pI range of 3.2-4.0 | - |
additional information |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.11.1.10 | evolution | Caldariomyces fumago chloroperoxidase (CPO) is a glycosylated hemoprotein enzyme from the peroxidase family | Leptoxyphium fumago |
| 1.11.1.10 | malfunction | CPO enzyme contains thirteen sugars, including five N-acetyl D-glucosamines (NAG) and eight mannoses (MAN), which are attached to the protein via the glycosidic bonds. Removal of the sugars from CPO leads to increase the hydrophobicity of the enzyme, as well as the reduction of the alkylation reactions | Leptoxyphium fumago |
| 1.11.1.10 | additional information | computational molecular dynamics calculation, simulation, and modeling, using the glycosylated enzyme structure PDB ID 2CPO, overview | Leptoxyphium fumago |
| 1.11.1.10 | physiological function | the heme-containing CPO exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing the halogenation reactions. CPO selectively causes the oxidation and epoxidation of the diverse chemical compounds through the specific stereochemistry mechanism | Leptoxyphium fumago |
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