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

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 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.; 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.; 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 2781461Freely accessible. PMID 19625248.
  3. Montemiglio, L.C.; Gianni, S.; Vallone, B.; 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

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