+ NADPH
+ H+
Erythromycin 12 hydroxylase
| Erythromycin 12 hydroxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.154 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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
The enzyme characterised from Saccharopolyspora erythraea converts erythromycin D into erythromycin C by introduction of a hydroxy group at the C-12 position of the macrocycle. It uses reduced nicotinamide adenine dinucleotide phosphate (NADPH) and oxygen as cofactors.[4] Erythromycin C is subsequently converted to the antibiotic, erythromycin A, by the enzyme erythromycin 3''-O-methyltransferase.[5]
References
- ↑ 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.
- ↑ Enzyme 1.14.13.154 at KEGG Pathway Database.
- ↑ Summers RG, Donadio S, Staver MJ, Wendt-Pienkowski E, Hutchinson CR, Katz L (October 1997). "Sequencing and mutagenesis of genes from the erythromycin biosynthetic gene cluster of Saccharopolyspora erythraea that are involved in L-mycarose and D-desosamine production". Microbiology. 143 (10): 3251–62. doi:10.1099/00221287-143-10-3251. PMID 9353926.
External links
- Erythromycin+12+hydroxylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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