Literature summary for 1.4.3.3 extracted from

Molla, G.; Porrini, D.; Job, V.; Motteran, L.; Vegezzi, C.; Campaner, S.; Pilone, M.S.; Pollegioni, L.
Role of arginine 285 in the active site of Rhodotorula gracilis D-amino acid oxidase. A site-directed mutagenesis study (2000), J. Biol. Chem., 275, 24715-24721.

Search for more literature for 1.4.3.3

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Rhodotorula toruloides

Protein Variants

Protein Variants	Comment	Organism
R285A	decreased activity with D-amino acids	Rhodotorula toruloides
R285D	decreased activity with D-amino acids	Rhodotorula toruloides
R285K	decreased activity with D-amino acids	Rhodotorula toruloides
R285Q	decreased activity with D-amino acids	Rhodotorula toruloides

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.06	-	O2	mutant R285K	Rhodotorula toruloides
0.08	-	O2	mutant R285A	Rhodotorula toruloides
2.3	-	O2	wild-type	Rhodotorula toruloides
2.6	-	D-alanine	wild-type	Rhodotorula toruloides
310	-	D-alanine	mutant R285A	Rhodotorula toruloides
800	-	D-alanine	mutant R285K	Rhodotorula toruloides

Organism

Organism	UniProt	Comment	Textmining
Rhodotorula toruloides	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Storage Stability

Storage Stability	Organism
-20°C, several months	Rhodotorula toruloides

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.05	-	D-alanine	mutant R285A	Rhodotorula toruloides
0.8	-	D-alanine	mutant R285K	Rhodotorula toruloides
350	-	D-alanine	wild-type	Rhodotorula toruloides

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Rhodotorula toruloides

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)