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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
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Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago P04963 Caldariomyces fumago
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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