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

BRENDA support

Literature summary extracted from

  • Matsumura, K.; Yamada, M.; Yamashita, T.; Muto, H.; Nishiyama, K.I.; Shimoi, H.; Isobe, K.
    Expression of alcohol oxidase gene from Ochrobactrum sp. AIU 033 in recombinant Escherichia coli through the twin-arginine translocation pathway (2019), J. Biosci. Bioeng., 128, 13-21 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.13 expression in Escherichia coli. The OcAOD productivity of the recombinant E. coli is 24fold higher than that of Ochrobactrum sp. AIU 033, and it is further enhanced by 1.2 times by the coexpression of additional tatABC from E. coli BL21 Ochrobactrum sp. AIU 033
1.1.3.15 expression in Escherichia coli. The OcAOD productivity of the recombinant E. coli is 24fold higher than that of Ochrobactrum sp. AIU 033, and it is further enhanced by 1.2 times by the coexpression of additional tatABC from E. coli BL21 Ochrobactrum sp. AIU 033

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.13 periplasm recombinant protein in Escherichia coli Ochrobactrum sp. AIU 033
-
-
1.1.3.15 periplasm recombinant protein in Escherichia coli Ochrobactrum sp. AIU 033
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.13 Ochrobactrum sp. AIU 033
-
-
-
1.1.3.15 Ochrobactrum sp. AIU 033
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.13 1-butanol + O2
-
 Ochrobactrum sp. AIU 033 butanal + H2O2
-
 ?
1.1.3.13 1-hexanol + O2
-
 Ochrobactrum sp. AIU 033 hexanal + H2O2
-
 ?
1.1.3.13 1-octanol + O2
-
 Ochrobactrum sp. AIU 033 octanal + H2O2
-
 ?
1.1.3.13 1-pentanol + O2
-
 Ochrobactrum sp. AIU 033 pentanal + H2O2
-
 ?
1.1.3.13 1-propanol + O2
-
 Ochrobactrum sp. AIU 033 propanal + H2O2
-
 ?
1.1.3.13 ethanol + O2
-
 Ochrobactrum sp. AIU 033 acetaldehyde + H2O2
-
 ?
1.1.3.13 additional information enzyme also catalyzes the oxidation of glycolate to glyoxylate, reaction of EC 1.1.3.15. No substrate: glyoxylate Ochrobactrum sp. AIU 033 ?
-
-
1.1.3.15 glycolate + O2
-
 Ochrobactrum sp. AIU 033 glyoxylate + H2O2
-
 ?
1.1.3.15 additional information no substrate: glyoxylate. Enzyme also catalyzes the oxidation of short-chain alcohols, reaction of EC 1.1.3.13 Ochrobactrum sp. AIU 033 ?
-
-

Subunits

EC Number Subunits Comment Organism
1.1.3.13 ? x * 52000, alpha-subunit, x * 14000, beta-subunit, SDS-PAGE Ochrobactrum sp. AIU 033
1.1.3.15 ? x * 52000, alpha-subunit, x * 14000, beta-subunit, SDS-PAGE Ochrobactrum sp. AIU 033

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.13 30
-
 20 min, more than 80% residual activity, recombinant protein Ochrobactrum sp. AIU 033
1.1.3.13 50
-
 20 min, more than 40% residual activity for recombinant protein, complete loss of activity for native protein Ochrobactrum sp. AIU 033
1.1.3.15 30
-
 20 min, more than 80% residual activity, recombinant protein Ochrobactrum sp. AIU 033
1.1.3.15 50
-
 20 min, more than 40% residual activity for recombinant protein, complete loss of activity for native protein Ochrobactrum sp. AIU 033

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.3.13 5 6 20 min, 25°C, more than 80% residual activity, recombinant protein Ochrobactrum sp. AIU 033
1.1.3.15 5 6 20 min, 25°C, more than 80% residual activity, recombinant protein Ochrobactrum sp. AIU 033