Isopenicillin N epimerase
(Redirected from Isopenicillin-N epimerase)
| isopenicillin N epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.1.1.17 | ||||||||
| CAS no. | 88201-43-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an isopenicillin N epimerase (EC 5.1.1.17) is an enzyme that catalyzes the chemical reaction
- isopenicillin N penicillin N
Hence, this enzyme has one substrate, isopenicillin N, and one product, penicillin N.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is penicillin N 5-amino-5-carboxypentanoyl-epimerase. This enzyme participates in penicillin and cephalosporin biosynthesis.
References[edit]
- Usui S, Yu CA (1989). "Purification and properties of isopenicillin N epimerase from Streptomyces clavuligerus". Biochim. Biophys. Acta. 999 (1): 78–85. doi:10.1016/0167-4838(89)90033-2. PMID 2804141.
- Laiz L, Liras P, Castro JM, Martin JF (1990). "Purification and characterization of the isopenicillin-N epimerase from Nocardia lactamdurans". J. Gen. Microbiol. 136 (4): 663–671. doi:10.1099/00221287-136-4-663. hdl:10261/63775.
- Cantwell C, Beckmann R, Whiteman P, Queener SW, Abraham EP (1992). "Isolation of deacetoxycephalosporin C from fermentation broths of Penicillium chrysogenum transformants: construction of a new fungal biosynthetic pathway". Proceedings of the Royal Society B. 248 (1323): 283–9. doi:10.1098/rspb.1992.0073. PMID 1354366.
- Yeh WK, Ghag SK, Queener SW (1992). "Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C Function, evolution, refolding, and enzyme engineering". Ann. N.Y. Acad. Sci. 672 (1 Enzyme Engine): 396–408. doi:10.1111/j.1749-6632.1992.tb32705.x.
