2xfh | pdb_00002xfh
From Proteopedia
STRUCTURE OF CYTOCHROME P450 ERYK COCRYSTALLIZED WITH INHIBITOR CLOTRIMAZOLE.
Template:ABSTRACT PUBMED 20845962
Function
[CPXQ_SACEN] Responsible for the C-12 hydroxylation of the macrolactone ring of erythromycin. Thus, EryK catalyzes the hydroxylation of erythromycin D (ErD) at the C-12 position to produce erythromycin C (ErC). Erythromycin B (ErB) is not a substrate for this enzyme.[1] [2]
About this Structure
2xfh is a 1 chain structure with sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.
Reference
- Montemiglio LC, Gianni S, Vallone B, Savino C. Azole drugs trap cytochrome P450 EryK in alternative conformational states. Biochemistry. 2010 Sep 16. PMID:20845962 doi:10.1021/bi101062v
- ↑ Stassi D, Donadio S, Staver MJ, Katz L. Identification of a Saccharopolyspora erythraea gene required for the final hydroxylation step in erythromycin biosynthesis. J Bacteriol. 1993 Jan;175(1):182-9. PMID:8416893
- ↑ Lambalot RH, Cane DE, Aparicio JJ, Katz L. Overproduction and characterization of the erythromycin C-12 hydroxylase, EryK. Biochemistry. 1995 Feb 14;34(6):1858-66. PMID:7849045
