Literature summary for 1.11.1.10 extracted from
Ghorbani, S.; Housaindokht, M.; Bozorgmehr, M.
Investigating the effect of 1-butyl-3-methylimidazolium bromide and 1-butyl-3-methylimidazolium methyl sulfate ionic liquids on structure and function of chloroproxidase by molecular dynamics simulation (2021), J. Mol. Liq., 332, 115850 .
No PubMed abstract available
Organism
Organism |
UniProt |
Comment |
Textmining |
Leptoxyphium fumago |
P04963 |
Caldariomyces fumago |
- |
Posttranslational Modification
Posttranslational Modification |
Comment |
Organism |
glycoprotein |
chloroperoxidase (CPO) is a glycosidic hemoprotein enzyme |
Leptoxyphium fumago |
Subunits
Subunits |
Comment |
Organism |
? |
x * 42000, SDS-PAGE |
Leptoxyphium fumago |
Synonyms
Synonyms |
Comment |
Organism |
chloroproxidase |
- |
Leptoxyphium fumago |
CPO |
- |
Leptoxyphium fumago |
pH Optimum
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
2.9 |
- |
assay at |
Leptoxyphium fumago |
Cofactor
Cofactor |
Comment |
Organism |
Structure |
heme |
chloroperoxidase (CPO) is a glycosidic hemoprotein enzyme |
Leptoxyphium fumago |
|
additional information |
the CPO prosthetic group is Fe (IV) protoporphyrin |
Leptoxyphium fumago |
|
pI Value
Organism |
Comment |
pI Value Maximum |
pI Value |
Leptoxyphium fumago |
- |
4 |
3.2 |
General Information
General Information |
Comment |
Organism |
evolution |
chloroperoxidase (CPO) is a glycosidic hemoprotein enzyme of the peroxidase family |
Leptoxyphium fumago |
additional information |
analysis of the effect of 1-butyl-3-methylimidazolium bromide ([BMIM][Br]) and 1-butyl-3-methylimidazolium methyl sulfate ([BMIM] [MeSO4]) ionic liquids on the structure and function of chloroperoxidase (CPO) by molecular dynamics (MD) simulation using the enzyme structure (PDB ID 2CPO) as template, detailed overview. [BMIM][MeSO4] possesses greater influence on the enzyme structure, because of the special structure of the corresponding anion group. Besides, the number of cavities interprets the activation of the enzyme at the low concentrations and its inactivation at the high concentrations. The penetration of the anions into the enzyme structure is confirmed at the high concentrations of the ionic liquids. The role of ionic liquids at low concentrations is related to their binding to the enzyme structure. Their role at the high concentrations depends on the changes in the solvent arrangement as well as the attachment to the enzyme. Low concentration of ionic liquid play an important role and cause higher chloroproxidase activity.Whereas in high concentration due to surface coating of chloroproxidase by ionic liquid, despite the access of the substrate to the active site, CPO activity decreases. In chloroperoxidase, the substrate accesses the active site and heme group through a small channel above heme |
Leptoxyphium fumago |