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| isopenicillin N synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.21.3.1 | ||||||||
| CAS no. | 78642-31-6 | ||||||||
| 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 | ||||||||
| |||||||||
Isopenicillin N synthase (IPNS) is a non-heme iron protein belonging to the 2-oxoglutarate (2OG)-dependent dioxygenases oxidoreductase family. This enzyme catalyzes the formation of isopenicillin N from δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (LLD-ACV).
- N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 isopenicillin N + 2 H2O
This reaction is a key step in the biosynthesis of penicillin and cephalosporin antibiotics.[1]
The active sites of most isopenicillin N synthases contain an iron ion.[2]
This enzyme is also called isopenicillin N synthetase.
- ^ Cohen G, Shiffman D, Mevarech M, Aharonowitz Y (April 1990). "Microbial isopenicillin N synthase genes: structure, function, diversity and evolution". Trends Biotechnol. 8 (4): 105–11. doi:10.1016/0167-7799(90)90148-Q. PMID 1366527.
- ^ Roach PL, Clifton IJ, Hensgens CM, Shibata N, Schofield CJ, Hajdu J, Baldwin JE (June 1997). "Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation". Nature. 387 (6635): 827–30. doi:10.1038/42990. PMID 9194566. S2CID 205032251.