Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.21 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.21 0.0021
-
 2-Phenylethylamine pH 6.8, 30°C, mutant enzyme D298A Arthrobacter globiformis
1.4.3.21 0.0025
-
 2-Phenylethylamine pH 6.8, 30°C, wild-type enzyme Arthrobacter globiformis

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.21 Arthrobacter globiformis P46881
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.21 2-phenylethylamine + H2O + O2
-
 Arthrobacter globiformis 2-phenylethanal + NH3 + H2O2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.21 0.00021
-
 2-Phenylethylamine pH 6.8, 30°C, mutant enzyme D298A Arthrobacter globiformis
1.4.3.21 76
-
 2-Phenylethylamine pH 6.8, 30°C, wild-type enzyme Arthrobacter globiformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.4.3.21 additional information
-
-
 Arthrobacter globiformis