PROSITE documentation PDOC00674Oxygen oxidoreductases covalent FAD-binding site
Description
Some oxygen-dependent oxidoreductases are flavoproteins that contains a covalently bound FAD group which is attached to a histidine via an 8-α-(N3-histidyl)-riboflavin linkage. These proteins are:
- (R)-6-hydroxynicotine oxidase (EC 1.5.3.6) (6-HDNO) [1], a bacterial enzyme that catalyzes the oxygen-dependent degradation of 6-hydroxynicotine into 6-hydroxypyrid-N-methylosmine.
- Plant reticuline oxidase (EC 1.21.3.3) [2] (berberine-bridge-forming enzyme), an enzyme that catalyzes the oxidation of (S)-reticuline into (S)- scoulerine in the pathway leading to benzophenanthridine alkaloids.
- L-gulonolactone oxidase (EC 1.1.3.8) (l-gulono-γ-lactone oxidase) [3], a mammalian enzyme which catalyzes the oxidation of L-gulono-1,4-lactone to L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate.
- D-arabinono-1,4-lactone oxidase (EC 1.1.3.24) (L-galactonolactone oxidase), a yeast enzyme involved in the biosynthesis of D-erythroascorbic acid [4].
- Mitomycin radical oxidase [5], a bacterial protein involved in mitomycin resistance and that probably oxidizes the reduced form of mitomycins.
- Cytokinin oxidase (EC 1.4.3.18), a plant enzyme.
- Rhodococcus fascians fasciation locus protein fas5.
The region around the histidine that binds the FAD group is conserved in these enzymes and can be used as a signature pattern.
Last update:April 2006 / Pattern revised.
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Technical section
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References
| 1 | Authors | Brandsch R. Hinkkanen A.E. Mauch L. Nagursky H. Decker K. |
| Title | 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase. | |
| Source | Eur. J. Biochem. 167:315-320(1987). | |
| PubMed ID | 3622516 |
| 2 | Authors | Dittrich H. Kutchan T.M. |
| Title | Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 88:9969-9973(1991). | |
| PubMed ID | 1946465 |
| 3 | Authors | Koshizaka T. Nishikimi M. Ozawa T. Yagi K. |
| Title | Isolation and sequence analysis of a complementary DNA encoding rat liver L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis. | |
| Source | J. Biol. Chem. 263:1619-1621(1988). | |
| PubMed ID | 3338984 |
| 4 | Authors | Huh W.-K. Lee B.-H. Kim S.-T. Kim Y.-R. Rhie G.-E. Baek Y.-W. Hwang C.-S. Lee J.-S. Kang S.-O. |
| Title | D-erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae. | |
| Source | Mol. Microbiol. 30:895-903(1998). | |
| PubMed ID | 10094636 |
| 5 | Authors | August P.R. Flickinger M.C. Sherman D.H. |
| Title | Cloning and analysis of a locus (mcr) involved in mitomycin C resistance in Streptomyces lavendulae. | |
| Source | J. Bacteriol. 176:4448-4454(1994). | |
| PubMed ID | 7517396 |
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