| Entry |
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| Symbol |
eryK, CYP113A
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| Name |
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| Pathway |
| map00522 | Biosynthesis of 12-, 14- and 16-membered macrolides |
| map01110 | Biosynthesis of secondary metabolites |
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| Module |
| M00774 | Erythromycin biosynthesis, propanoyl-CoA + methylmalonyl-CoA => deoxyerythronolide B => erythromycin A/B |
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| Reaction |
| R05521 | erythromycin-B,NADPH:oxygen oxidoreductase (12-hydroxylating) |
| R05522 | erythromycin-D,NADPH:oxygen oxidoreductase (12-hydroxylating) |
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| Brite |
KEGG Orthology (KO) [BR:ko00001]
09100 Metabolism
09109 Metabolism of terpenoids and polyketides
01052 Type I polyketide structures
K14370 eryK, CYP113A; erythromycin 12 hydroxylase
00522 Biosynthesis of 12-, 14- and 16-membered macrolides
K14370 eryK, CYP113A; erythromycin 12 hydroxylase
09180 Brite Hierarchies
09181 Protein families: metabolism
01008 Polyketide biosynthesis proteins
K14370 eryK, CYP113A; erythromycin 12 hydroxylase
00199 Cytochrome P450
K14370 eryK, CYP113A; erythromycin 12 hydroxylase
Enzymes [BR:ko01000]
1. Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
1.14.13.154 erythromycin 12-hydroxylase
K14370 eryK, CYP113A; erythromycin 12 hydroxylase
Polyketide biosynthesis proteins [BR:ko01008]
Polyketide tailoring proteins
Oxygenase
K14370 eryK, CYP113A; erythromycin 12 hydroxylase
Cytochrome P450 [BR:ko00199]
Cytochrome P450, bacteria type
CYP113 family
K14370 eryK, CYP113A; erythromycin 12 hydroxylase
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| Other DBs |
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| Genes |
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| Reference |
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| Authors |
Stassi D, Donadio S, Staver MJ, Katz L |
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| Title |
Identification of a Saccharopolyspora erythraea gene required for the final hydroxylation step in erythromycin biosynthesis. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Savino C, Montemiglio LC, Sciara G, Miele AE, Kendrew SG, Jemth P, Gianni S, Vallone B |
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| Title |
Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate. |
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| Journal |
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| LinkDB |
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