The Enzyme Database

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EC 1.14.13.154     
Accepted name: erythromycin 12-hydroxylase
Reaction: erythromycin D + NADPH + H+ + O2 = erythromycin C + NADP+ + H2O
For diagram of erythromycin biosynthesis, click here
Other name(s): EryK
Systematic name: erythromycin-D,NADPH:oxygen oxidoreductase (12-hydroxylating)
Comments: The enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis. It shows 1200-1900-fold preference for erythromycin D over the alternative substrate erythromycin B [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Lambalot, R.H., Cane, D.E., Aparicio, J.J. and Katz, L. Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK. Biochemistry 34 (1995) 1858–1866. [PMID: 7849045]
2.  Savino, C., Montemiglio, L.C., Sciara, G., Miele, A.E., Kendrew, S.G., Jemth, P., Gianni, S. and Vallone, B. Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate. J. Biol. Chem. 284 (2009) 29170–29179. [PMID: 19625248]
3.  Montemiglio, L.C., Gianni, S., Vallone, B. and Savino, C. Azole drugs trap cytochrome P450 EryK in alternative conformational states. Biochemistry 49 (2010) 9199–9206. [PMID: 20845962]
[EC 1.14.13.154 created 2012]
 
 


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