L-saccharopine oxidase
| L-saccharopine oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.3.18 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
L-saccharopine oxidase (EC 1.5.3.18, FAP2) is an enzyme with systematic name L-saccharopine:oxygen oxidoreductase (L-glutamate forming).[1] This enzyme catalyses the following chemical reaction
The enzyme is involved in pipecolic acid biosynthesis in Rhizoctonia leguminicola.[2][3]
References
- ^ Yoshida N, Akazawa S, Katsuragi T, Tani Y (2004). "Characterization of two fructosyl-amino acid oxidase homologs of Schizosaccharomyces pombe". Journal of Bioscience and Bioengineering. 97 (4): 278–80. doi:10.1016/S1389-1723(04)70204-2. PMID 16233628.
- ^ Enzyme 1.5.3.18 at KEGG Pathway Database.
- ^ Wickwire BM, Wagner C, Broquist HP (September 1990). "Pipecolic acid biosynthesis in Rhizoctonia leguminicola. II. Saccharopine oxidase: a unique flavin enzyme involved in pipecolic acid biosynthesis". The Journal of Biological Chemistry. 265 (25): 14748–53. doi:10.1016/S0021-9258(18)77176-7. PMID 2394693.
External links
- L-saccharopine+oxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)