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Literature summary for 1.11.1.10 extracted from

  • Pesic, M.; Lopez, C.; Alvaro, G.; Lopez-Santin, J.
    A novel immobilized chloroperoxidase biocatalyst with improved stability for the oxidation of amino alcohols to amino aldehydes (2012), J. Mol. Catal. B, 84, 144-151.
No PubMed abstract available

General Stability

General Stability Organism
enzyme immobilized on monoaminoethyl-N-aminoethyl through carbodiimide-coupled method shows an increase in apparent half-life time of more than 500fold that of the soluble enzyme Leptoxyphium fumago

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibited by sodium cyanoborohydride in molar excess of 1:10 and 1:100 Leptoxyphium fumago
Sodium cyanoborohydride activity decreases in 38.2 and 92.6% for sodium cyanoborohydride molar excess of 1:1000 and 1:10000 Leptoxyphium fumago

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyl-N-(2-hydroxyethyl)-carbamate + tertbutyl hydroperoxide
-
Leptoxyphium fumago Cbz-glycinal + ?
-
?
monochlorodimedone + chloride + H2O2
-
Leptoxyphium fumago dichlorodimedone + H2O
-
?

Synonyms

Synonyms Comment Organism
chloroperoxidase
-
Leptoxyphium fumago
CPO
-
Leptoxyphium fumago

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 6.5 at pH 6.5 the soluble enzyme retains about 70% of initial activity after 3 days of incubation, while at both pH 6.0 and 5.0 the enzyme retains more than 95% Leptoxyphium fumago

Cofactor

Cofactor Comment Organism Structure
heme
-
Leptoxyphium fumago