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Literature summary for 1.11.1.10 extracted from

  • He, J.; Zhang, Y.; Yuan, Q.; Liang, H.
    Catalytic activity and application of immobilized chloroperoxidase by biometric magnetic nanoparticles (2019), Ind. Eng. Chem. Res., 58, 3555-3560 .
No PubMed abstract available
Search for more literature for 1.11.1.10

Protein Variants

Protein Variants Comment Organism
additional information development of an immobilization method for chloroperoxidase (CPO) via carbohydrate-binding lectin protein, concanavalin A (ConA). ConA is attached on the surface of silica-coated magnetic nanoparticles (MNPs) for effective recovery (ConA/Fe3O4-SiO2). CPO shows about 100% activity recovery after its immobilization on ConA functionalized MNPs. After storing for four weeks, the immobilized CPO still maintains 80% activity while only 46% of activity of free enzyme is retained. Immobilized CPO by biometric magnetic nanoparticles exhibits excellent reusability and enantioselectivity in asymmetric synthesis of modafinil. More than 82% of original conversion rate and 70% enantiomeric excess (ee) value are observed after being run eight times. Synthesis and characterization of the ConA-functionalized magnetic nanoparticles, overview. CPO is fixed in the surface of nanoparticles without steric limitation and exposed to medium as free CPO. The immobilization temperature has little effect on immobilization efficiency, but CPO lost its activity at high temperature (>40°C). Meanwhile, CPO has a high immobilization efficiency at acidic conditions, but its activity greatly decreases at pH 7.0. Maximum immobilization efficiency and relative activity for immobilized CPO is obtained at 20°C and pH 6.0. ConA can efficiently conserve the natural activity of original CPO during the immobilization Leptoxyphium fumago

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Leptoxyphium fumago

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago P04963 Caldariomyces fumago
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein CPO is a glycosylated enzyme Leptoxyphium fumago

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information asymmetric sulfoxidation of 2-(diphenylmethylthio) acetamide to (R)-modafinil Leptoxyphium fumago ?
-
-

Synonyms

Synonyms Comment Organism
chloroperoxidase
-
 Leptoxyphium fumago
CPO
-
 Leptoxyphium fumago

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Leptoxyphium fumago

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3
-
 assay at Leptoxyphium fumago

pH Range

pH Minimum pH Maximum Comment Organism
3 7 activity range Leptoxyphium fumago

Cofactor

Cofactor Comment Organism Structure
heme
-
 Leptoxyphium fumago

General Information

General Information Comment Organism
physiological function chloroperoxidase (CPO), which is a versatile heme-containing enzyme, can catalyze sulfoxidation, epoxidation, dismutation, halogenation, and oxidation of numerous compounds with extensive high regioselectivity and enantioselectivity Leptoxyphium fumago