Literature summary for 1.4.3.3 extracted from

Arroyo, M.; Menendez, M.; Garcia, J.L.; Campillo, N.; Hormigo, D.; De la Mata, I.; Castillon, M.P.; Acebal, C.
The role of cofactor binding in tryptophan accessibility and conformational stability of His-tagged D-amino acid oxidase from Trigonopsis variabilis (2007), Biochim. Biophys. Acta, 1774, 556-565.

Search for more literature for 1.4.3.3

Cloned(Commentary)

Cloned (Comment)	Organism
the His-tagged enzyme is expressed in Escherichia coli	Trigonopsis variabilis

General Stability

General Stability	Organism
His-tagged DAAO loses its flavin cofactor upon dilution or prolonged dialysis against FAD-free solvents leading to the catalytic inactivation	Trigonopsis variabilis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
5.5	-	D-alanine	apparent value, reconstituted holoenzyme at pH 8.0 and 30°C	Trigonopsis variabilis

Organism

Organism	UniProt	Comment	Textmining
Trigonopsis variabilis	Q99042	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Trigonopsis variabilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
cephalosporin C + H2O + O2	-	Trigonopsis variabilis	7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2	-	?
D-alanine + H2O + O2	-	Trigonopsis variabilis	pyruvate + NH3 + H2O2	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Trigonopsis variabilis

Synonyms

Synonyms	Comment	Organism
D-amino acid oxidase	-	Trigonopsis variabilis
DAAO	-	Trigonopsis variabilis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
30	45	loss of secondary structure and inactivation occurs over a range of 30°C to 45°C, the melting temperature is at 41.4°C	Trigonopsis variabilis

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
95	-	D-alanine	apparent value, reconstituted holoenzyme at pH 8.0 and 30°C	Trigonopsis variabilis

Cofactor

Cofactor	Comment	Organism	Structure
FAD	contains non-covalently bound FAD	Trigonopsis variabilis

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Release 2023.1 (January 2023)