Erythromycin 12 hydroxylase (EC 1.14.13.154, EryK) is an enzyme with systematic name erythromycin-D,NADPH:oxygen oxidoreductase (12-hydroxylating) .[1][2][3] This enzyme catalyses the following chemical reaction
| Erythromycin 12 hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.154 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- erythromycin D + NADPH + H+ + O2 erythromycin C + NADP+ + H2O
Erythromycin 12 hydroxylase is responsible for the C-12 hydroxylation of the macrolactone ring.
References
edit- ^ Lambalot RH, Cane DE, Aparicio JJ, Katz L (February 1995). "Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK". Biochemistry. 34 (6): 1858–66. doi:10.1021/bi00006a006. PMID 7849045.
- ^ Savino C, Montemiglio LC, Sciara G, Miele AE, Kendrew SG, Jemth P, Gianni S, Vallone B (October 2009). "Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate". The Journal of Biological Chemistry. 284 (42): 29170–9. doi:10.1074/jbc.M109.003590. PMC 2781461. PMID 19625248.
- ^ Montemiglio LC, Gianni S, Vallone B, Savino C (November 2010). "Azole drugs trap cytochrome P450 EryK in alternative conformational states". Biochemistry. 49 (43): 9199–206. doi:10.1021/bi101062v. PMID 20845962.
External links
edit- Erythromycin+12+hydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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