EC 1.1.3.41 - Alditol oxidase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.1.3.41

Names

Accepted name:
alditol oxidase
Other names:
xylitol oxidase
xylitol:oxygen oxidoreductase
AldO
Systematic name:
alditol:oxygen oxidoreductase

Reactions

Cofactor

Comments:

The enzyme from Streptomyces sp. IKD472 is a monomeric oxidase containing one molecule of FAD per molecule of protein [1,2]. While xylitol (five carbons) and sorbitol (6 carbons) are the preferred substrates, other alditols, including L-threitol (four carbons), D-arabinitol (five carbons), D-galactitol (six carbons) and D-mannitol (six carbons) can also act as substrates, but more slowly [1,2]. Belongs in the vanillyl-alcohol-oxidase family of enzymes [2].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00674
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050582
UniProtKB/Swiss-Prot:

References

  1. Yamashita, M., Omura, H., Okamoto, E., Furuya, Y., Yabuuchi, M., Fukahi, K. and Murooka, Y.
    Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472.
    J. Biosci. Bioeng. 89: 350-360 (2000). [PMID: 16232758]
  2. Heuts, D.P.H.M., van Hellemond, E.W., Janssen, D.B. and Fraaije, M.W.
    Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolor.
    J. Biol. Chem. 282: 20283-20291 (2007). [PMID: 17517896]
  3. Forneris, F., Heuts, D.P.H.M., Delvecchio, M., Rovida, S., Fraaije, M. W. and Mattevi, A.
    Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase.
    Biochemistry 47: 978-985 (2008). [PMID: 18154360]

[EC 1.1.3.41 created 2002, modified 2008]