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Literature summary for 1.14.99.54 extracted from

  • Kracher, D.; Andlar, M.; Furtmueller, P.; Ludwig, R.
    Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability (2018), J. Biol. Chem., 293, 1676-1687 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Neurospora crassa

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ the reduction of the mononuclear active-site copper by ascorbic acid increases the affinity and the maximum binding capacity of LPMO for cellulose Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cellulose + ascorbic acid + O2
-
Neurospora crassa ? + dehydroascorbic acid + H2O
-
?
soluble beta-glucan + ascorbic acid + O2
-
Neurospora crassa ? + dehydroascorbic acid + H2O
-
?

Synonyms

Synonyms Comment Organism
LPMO9C
-
Neurospora crassa

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35
-
midpoint transition temperature, pH 4.0, citrate buffer, oxidized enzyme Neurospora crassa
44
-
midpoint transition temperature, pH 4.0, acetate buffer, oxidized enzyme Neurospora crassa
48.8
-
midpoint transition temperature, pH 6.0, phosphate buffer, presence of ascorbic acid Neurospora crassa
53
-
midpoint transition temperature, pH 6.0, phosphate buffer, presence of EDTA Neurospora crassa
61.5
-
midpoint transition temperature, pH 6.0, phosphate buffer, oxidized enzyme Neurospora crassa

General Information

General Information Comment Organism
metabolism substrates cellulose and xyloglucan show a stabilizing effect on the apparent transition midpoint temperature of the reduced, catalytically active enzyme. Oxidative auto-inactivation and destabilization are observed in the absence of a suitable substrate Neurospora crassa