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Literature summary for 1.1.99.29 extracted from

  • Krondorfer, I.; Brugger, D.; Paukner, R.; Scheiblbrandner, S.; Pirker, K.F.; Hofbauer, S.; Furtmueller, P.G.; Obinger, C.; Haltrich, D.; Peterbauer, C.K.
    Agaricus meleagris pyranose dehydrogenase: influence of covalent FAD linkage on catalysis and stability (2014), Arch. Biochem. Biophys., 558, 111-119.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
H103Y the mutant is still able to bind FAD (non-covalently) and perform catalysis but steady-state kinetic parameters for several substrates are negatively affected Leucoagaricus meleagris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
1 * 75000, SDS-PAGE Leucoagaricus meleagris

Organism

Organism UniProt Comment Textmining
Leucoagaricus meleagris
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Leucoagaricus meleagris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + ferrocenium ion
-
Leucoagaricus meleagris 2-dehydro-D-glucose + ferrocene
-
?

Subunits

Subunits Comment Organism
monomer 1 * 75000, SDS-PAGE Leucoagaricus meleagris

Synonyms

Synonyms Comment Organism
PDH
-
Leucoagaricus meleagris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Leucoagaricus meleagris

Cofactor

Cofactor Comment Organism Structure
FAD
-
Leucoagaricus meleagris