Literature summary for 1.4.3.21 extracted from

Chiu, Y.C.; Okajima, T.; Murakawa, T.; Uchida, M.; Taki, M.; Hirota, S.; Kim, M.; Yamaguchi, H.; Kawano, Y.; Kamiya, N.; Kuroda, S.; Hayashi, H.; Yamamoto, Y.; Tanizawa, K.
Kinetic and structural studies on the catalytic role of the aspartic acid residue conserved in copper amine oxidase (2006), Biochemistry, 45, 4105-4120.

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Protein Variants

Protein Variants	Comment	Organism
D298A	Km-value for 2-phenylethylamine is 85% of the wild-type enzyme, kcat for 2-phenylethylamine is 360000fold lower than wild-type enzyme	Arthrobacter globiformis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0021	-	2-Phenylethylamine	pH 6.8, 30°C, mutant enzyme D298A	Arthrobacter globiformis
0.0025	-	2-Phenylethylamine	pH 6.8, 30°C, wild-type enzyme	Arthrobacter globiformis

Organism

Organism	UniProt	Comment	Textmining
Arthrobacter globiformis	P46881	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-phenylethylamine + H2O + O2	-	Arthrobacter globiformis	2-phenylethanal + NH3 + H2O2	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.00021	-	2-Phenylethylamine	pH 6.8, 30°C, mutant enzyme D298A	Arthrobacter globiformis
76	-	2-Phenylethylamine	pH 6.8, 30°C, wild-type enzyme	Arthrobacter globiformis

pH Range

pH Minimum	pH Maximum	Comment	Organism
additional information	-	-	Arthrobacter globiformis

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Release 2023.1 (January 2023)