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Literature summary extracted from

  • Fukiya, K.; Itoh, K.; Yamaguchi, S.; Kishiba, A.; Adachi, M.; Watanabe, N.; Tanaka, Y.
    A single amino acid substitution confers high cinchonidine oxidation activity comparable with that of rabbit to monkey aldehyde oxidase 1 (2010), Drug Metab. Dispos., 38, 302-307.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.3.1 expressed in Escherichia coli M15 cells Oryctolagus cuniculus
1.2.3.1 expressed in Escherichia coli M15 cells Macaca fascicularis

Protein Variants

EC Number Protein Variants Comment Organism
1.2.3.1 A1023Y the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 A1081V the mutant completely loses the high cinchonidine oxidation activity of the wild type enzyme Oryctolagus cuniculus
1.2.3.1 A1083T the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 A1083T/V1085A the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 I1032V the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 K1004Q the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 K1004Q/K1005R the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 K1004Q/K1005R/M1009I/V1010I the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y/I1032V the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y/I1032V/G1064K/I1067M the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 M1009I the mutant shows increased Km towards (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine compared to the wild type enzyme Macaca fascicularis
1.2.3.1 V1085A the mutant acquires high cinchonidine oxidation activity Macaca fascicularis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.3.1 0.0074
-
cinchonidine wild type enzyme, in 80 mM phosphate buffer, pH 7.4, at 37°C Oryctolagus cuniculus
1.2.3.1 0.0109
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine wild type enzyme, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.012
-
cinchonidine mutant enzyme V1085A, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.0157
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y/I1032V/G1064K/I1067M, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.0244
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y/I1032V, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.0264
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme A1023Y, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.027
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme M1009I, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.0334
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme I1032V, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.0352
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine mutant enzyme A1081V, in 80 mM phosphate buffer, pH 7.4, at 37°C Oryctolagus cuniculus
1.2.3.1 0.036
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme K1004Q/K1005R, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.0366
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme K1004Q, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.0521
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme K1004Q/K1005R/M1009I/V1010I, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.0965
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.128
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme A1083T/V1085A, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.131
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine mutant enzyme V1085A, in 80 mM phosphate buffer, pH 7.4, at 37°C Macaca fascicularis
1.2.3.1 0.147
-
(+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine wild type enzyme, in 80 mM phosphate buffer, pH 7.4, at 37°C Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
1.2.3.1 Macaca fascicularis
-
-
-
1.2.3.1 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.3.1 Ni affinity column chromatography Oryctolagus cuniculus
1.2.3.1 Ni affinity column chromatography Macaca fascicularis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.3.1 (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta-[d]-pyrimidine + H2O + O2 i.e. (S)-RS-8359 Macaca fascicularis ?
-
?
1.2.3.1 (+)-4-(4-cyanoanilino)-5,6-dihydro-7-hydroxy-7H-cyclopenta[d]-pyrimidine + H2O + O2 i.e. (S)-RS-8359 Oryctolagus cuniculus ?
-
?
1.2.3.1 cinchonidine + H2O + O2 rabbit AOX1 has an extremely high Vmax value toward cinchonidine Oryctolagus cuniculus ?
-
?
1.2.3.1 cinchonidine + H2O + O2 wild type monkey AOX1 is not able to oxidize chinchonidine, but mutant enzyme V1085A does Macaca fascicularis ?
-
?
1.2.3.1 zonisamide + H2O + O2
-
Oryctolagus cuniculus ?
-
?
1.2.3.1 zonisamide + H2O + O2
-
Macaca fascicularis ?
-
?

Synonyms

EC Number Synonyms Comment Organism
1.2.3.1 aldehyde oxidase 1
-
Oryctolagus cuniculus
1.2.3.1 aldehyde oxidase 1
-
Macaca fascicularis
1.2.3.1 AOX1
-
Oryctolagus cuniculus
1.2.3.1 AOX1
-
Macaca fascicularis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.3.1 FAD
-
Oryctolagus cuniculus
1.2.3.1 FAD
-
Macaca fascicularis