Literature summary for 1.4.3.3 extracted from

Caldinelli, L.; Molla, G.; Pilone, M.S.; Pollegioni, L.
Tryptophan 243 affects interprotein contacts, cofactor binding and stability in D-amino acid oxidase from Rhodotorula gracilis (2006), FEBS J., 273, 504-512.

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Protein Variants

Protein Variants	Comment	Organism
W243I	mutant ezyme with a significantly lower content of flavin cofactor. Loss of the tertiary structure elements and of the flavin cofactor occurs at lower temperatures in mutant than in the dimeric wild-type enzyme. The midpoint concentration of urea required for unfolding is significanlty lower than for the wild-type enzyme	Rhodotorula toruloides
W243Y	mutant enzyme retains the FAD coenzyme. Loss of the tertiary structure elements and of the flavin cofactor occurs at lower temperatures in mutant than in the dimeric wild-type enzyme	Rhodotorula toruloides

General Stability

General Stability	Organism
the midpoint contration of urea required for unfolding is 1.4-1.8 M for wild-type enzyme and 0.8-1.1 M for mutant enzyme W243Y	Rhodotorula toruloides

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.4	-	D-alanine	mutant enzyme W243Y	Rhodotorula toruloides
1.6	-	D-alanine	mutant enzyme W243I, assay in presence of a large excess of free FAD (0.2 mM) in assay mixture	Rhodotorula toruloides

Organism

Organism	UniProt	Comment	Textmining
Rhodotorula toruloides	P80324	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-alanine + H2O + O2	-	Rhodotorula toruloides	pyruvate + NH3 + H2O2	-	?

Subunits

Subunits	Comment	Organism
homodimer	-	Rhodotorula toruloides

Synonyms

Synonyms	Comment	Organism
DAAO	-	Rhodotorula toruloides

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Rhodotorula toruloides

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Release 2023.1 (January 2023)