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Literature summary for 1.4.3.3 extracted from

  • Mora, M.F.; Giacomelli, C.E.; Garcia, C.D.
    Interaction of D-amino acid oxidase with carbon nanotubes: implications in the design of biosensors (2009), Anal. Chem., 81, 1016-1022.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information immobilization of the enzyme, interaction of D-amino acid oxidase with single-walled carbon nanotubes, analysis by spectroscopic ellipsometry. DAAO can adopt multiple orientations on the surface, which are ultimately responsible for significant differences in catalytic activity, highest enzymatic activity by adsorbing the protein at pH 5.7 and 0.1 mg/ml, adsorption kinetics at different pH values, overview Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation from kidney Sus scrofa
-
kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information DAAO is a flavoprotein that catalyzes the dehydrogenation of different D-amino acids to their imino counterparts via a reduced flavin product complex. The reduced flavin is then reoxidized by O2 to yield H2O2, whereas the imino acid spontaneously hydrolyzes to the corresponding keto acid and NH4+. DAAO is strictly stereospecific and oxidizes a variety of D-amino acids, with a preference for those having small hydrophobic side chains, followed by those bearing polar, aromatic, and basic groups Sus scrofa ?
-
?

Synonyms

Synonyms Comment Organism
DAAO
-
Sus scrofa

Cofactor

Cofactor Comment Organism Structure
flavin flavoenzyme Sus scrofa

pI Value

Organism Comment pI Value Maximum pI Value
Sus scrofa
-
-
6.37