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Literature summary for 1.1.3.4 extracted from

  • van Bloois, E.; Winter, R.T.; Janssen, D.B.; Fraaije, M.W.
    Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysis (2009), Appl. Microbiol. Biotechnol., 83, 679-687.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.1.3.4

Application

Application Comment Organism
synthesis utilization of recombinant enzyme expressed in the periplasm or on the cell surface of Escherichia coli as biocatalyst in a non-laborious and non-costly whole-cell application for reacting on towards different polyols such as xylitol and sorbitol Streptomyces coelicolor

Cloned(Commentary)

Cloned (Comment) Organism
recombinant enzyme expression in the periplasm or on the cell surface of Escherichia coli cells of different strains. The enzyme is differently tagged, i.e. expressed as Tat-AldO or INP-AldO, and exported to the periplasm or to the cell surface of the transformed cells, overview. AldO is successfully displayed at the surface of E. coli using a truncated INP variant, it contains covalently bound FAD, thus has attained a correctly folded and active conformation Streptomyces coelicolor

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Streptomyces coelicolor
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45100
-
 1 * 45100 Streptomyces coelicolor

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sorbitol + O2 Streptomyces coelicolor
-
 ?
-
 ?
sorbitol + O2 Streptomyces coelicolor A3(2)
-
 ?
-
 ?
xylitol + O2 Streptomyces coelicolor
-
 ?
-
 ?
xylitol + O2 Streptomyces coelicolor A3(2)
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
-
-
-
Streptomyces coelicolor A3(2)
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information AldO catalyzes the C1 oxidation of several polyols Streptomyces coelicolor ?
-
 ?
additional information AldO catalyzes the C1 oxidation of several polyols Streptomyces coelicolor A3(2) ?
-
 ?
sorbitol + O2
-
 Streptomyces coelicolor ?
-
 ?
sorbitol + O2
-
 Streptomyces coelicolor A3(2) ?
-
 ?
xylitol + O2
-
 Streptomyces coelicolor ?
-
 ?
xylitol + O2
-
 Streptomyces coelicolor A3(2) ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 45100 Streptomyces coelicolor

Synonyms

Synonyms Comment Organism
AldO
-
 Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
FAD a flavoprotein, the flavin cofactor is covalently linked to the polypeptide chain, covalent anchoring of the FAD cofactor is an autocatalytic process and that only occurs upon correct folding of the polypeptide chain Streptomyces coelicolor