Erythromycin 12 hydroxylase

Erythromycin 12 hydroxylase
Identifiers
EC number	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
Search PMC articles PubMed articles NCBI proteins

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 D + NADPH + H⁺ + O₂ $\rightleftharpoons$ erythromycin C + NADP⁺ + H₂O

Erythromycin 12 hydroxylase is responsible for the C-12 hydroxylation of the macrolactone ring.

References

1. Lambalot, R.H., Cane, D.E., Aparicio, J.J. and Katz, L. (1995). "Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK". Biochemistry 34 (6): 1858–1866. doi:10.1021/bi00006a006. PMID 7849045.
2. Savino, C., Montemiglio, L.C., Sciara, G., Miele, A.E., Kendrew, S.G., Jemth, P., Gianni, S. and Vallone, B. (2009). "Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate". J. Biol. Chem. 284 (42): 29170–29179. doi:10.1074/jbc.M109.003590. PMC 2781461. PMID 19625248.
3. Montemiglio, L.C., Gianni, S., Vallone, B. and Savino, C. (2010). "Azole drugs trap cytochrome P450 EryK in alternative conformational states". Biochemistry 49 (43): 9199–9206. doi:10.1021/bi101062v. PMID 20845962.

External links

• Erythromycin 12 hydroxylase at the US National Library of Medicine Medical Subject Headings (MeSH)