6-deoxyerythronolide B hydroxylase (EryF)

6-deoxyerythronolide B hydroxylase, also known as EryF or CYP113A1, is a bacterial cytochrome P450 enzyme derived from Saccharopolyspora erythraea [1]. It plays a critical role in the biosynthesis of the macrolide antibiotic erythromycin by catalyzing the regiospecific and stereospecific hydroxylation of 6-deoxyerythronolide B at the C-6 position to produce erythronolide B [2]. This enzymatic step is essential for the formation of the active antibiotic structure. EryF has served as a primary model for understanding the structural biology and catalytic mechanisms of P450 enzymes due to its high substrate specificity and well-defined crystal structure [3]. While it is not a direct therapeutic target for treating human diseases, it is a vital component in the industrial production of erythromycin and a target for metabolic engineering to create novel macrolide derivatives [4]. Understanding its function has facilitated the development of semi-synthetic antibiotics with improved pharmacological properties.

Other names

EryFCytochrome P450 113A1CYP113A16-deoxyerythronolide B 6-monooxygenase6-deoxyerythronolide B 6-hydroxylase

The enzyme catalyzes the regiospecific and stereospecific hydroxylation of 6-deoxyerythronolide B at the C-6 position, utilizing molecular oxygen and electrons from a ferredoxin/ferredoxin reductase system [1, 2].