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Literature summary for 1.1.3.4 extracted from

  • Forneris, F.; Heuts, D.; Delvecchio, M.; Rovida, S.; Fraaije, M.; Mattevi, A.
    Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase (2008), Biochemistry, 47, 978-985.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
native wild-type enzyme, hanging-drop vapor diffusion method at 4 °C by mixing equal volumes of 14 mg/mL AldO solution in 50 mM potassium phosphate buffer, pH 7.5, with reservoir solutions containing 0.1 M MES/HCl, pH 6.5, 0.2 M MgCl2 and 18-20% w/v PEG4000, 3-4 days, substrate incorporation by soaking the wild-type AldO crystals in a solution consisting of 0.1 M MES/HCl, pH 6.5, 0.2 M MgCl2, 25% w/v PEG 4000, 17.5% sucrose, and 25 mM substrate for 3 h, X-ray diffraction structure determination and analysis at 1.1-1.9 A resolution Streptomyces coelicolor

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Reaction

Reaction Comment Organism Reaction ID
beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2 catalytic mechanism and stereoselectivity, substrate binding occurs through a lock-and-key mechanism and does not induce conformational changes with respect to the ligand-free protein, overview Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-mannitol + O2
-
Streptomyces coelicolor ?
-
?
D-mannitol + O2
-
Streptomyces coelicolor A3(2) ?
-
?
D-sorbitol + O2
-
Streptomyces coelicolor ?
-
?
D-sorbitol + O2
-
Streptomyces coelicolor A3(2) ?
-
?

Subunits

Subunits Comment Organism
More AldO shares the same folding topology of the members of the vanillyl-alcohol oxidase family of flavoenzymes, three-dimensional structure analysis, overview Streptomyces coelicolor

Synonyms

Synonyms Comment Organism
AldO
-
Streptomyces coelicolor

Cofactor

Cofactor Comment Organism Structure
FAD flavin-dependent oxidase with covalently linked FAD which is located at the bottom of a funnel-shaped pocket that forms the active site Streptomyces coelicolor