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Literature summary for 1.14.99.54 extracted from

  • Phillips, C.; Beeson, W.; Cate, J.; Marletta, M.
    Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa (2011), ACS Chem. Biol., 6, 1399-1406.
    View publication on PubMed
Search for more literature for 1.14.99.54

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ 1 mol of copper per mol of proein Neurospora crassa
Cu2+ 1 mol of copper per mol of protein Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa Q1K8B6 isoform endoglucanase II
-
Neurospora crassa Q7RWN7 isoform endoglucanase II
-
Neurospora crassa Q7SA19 isoform endoglucanase IV
-
Neurospora crassa ATCC 24698 Q1K8B6 isoform endoglucanase II
-
Neurospora crassa ATCC 24698 Q7RWN7 isoform endoglucanase II
-
Neurospora crassa ATCC 24698 Q7SA19 isoform endoglucanase IV
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 1-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose Neurospora crassa ?
-
 ?
additional information mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 4-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose Neurospora crassa ?
-
 ?
additional information mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 4-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose Neurospora crassa ATCC 24698 ?
-
 ?
additional information mechanism may follow one electron reduction of PMO-Cu(II) to PMO-Cu(I) by the cellobiose dehydrogenase heme domain followed by oxygen binding and internal electron transfer to form a copper superoxo intermediate. Hydrogen atom abstraction by the copper superoxo at the 1-position of an internal carbohydrate then takes place, generating a copper hydroperoxo intermediate and a substrate radical. The second electron from cellobiose dehydrogenase then facilitates O-O bond cleavage releasing water and generating a copper oxo radical that couples with the substrate radical, thereby hydroxylating the polysaccharide. The additional oxygen atom destabilizes the glycosidic bond leading to elimination of the adjacent glucan and formation of a sugar lactone or ketoaldose Neurospora crassa ATCC 24698 ?
-
 ?
phosphoric acid swollen cellulose + AH2 + O2
-
 Neurospora crassa ? + dehydroascorbate + H2O in presence of cellobiose dehydrogenase, products include doubly oxidized cellodextrin ?
phosphoric acid swollen cellulose + AH2 + O2
-
 Neurospora crassa ATCC 24698 ? + dehydroascorbate + H2O in presence of cellobiose dehydrogenase, products include doubly oxidized cellodextrin ?

Synonyms

Synonyms Comment Organism
endoglucanase II
-
 Neurospora crassa
endoglucanase IV
-
 Neurospora crassa
gh61-4
-
 Neurospora crassa
gh61-5
-
 Neurospora crassa
NCU07898
-
 Neurospora crassa
PMO
-
 Neurospora crassa
polysaccharide monoxygenase
-
 Neurospora crassa

General Information

General Information Comment Organism
physiological function cellobiose dehydrogenase enhances cellulose degradation by coupling the oxidation of cellobiose to the reductive activation of copper-dependent polysaccharide monooxygenase that catalyzes the insertion of oxygen into C-H bonds adjacent to the glycosidic linkage Neurospora crassa