1.14.13.154: erythromycin 12-hydroxylase
This is an abbreviated version!
For detailed information about erythromycin 12-hydroxylase, go to the full flat file.

Word Map on EC 1.14.13.154
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1.14.13.154
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editing
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inosine
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a-to-i
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deaminases
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deamination
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symmetrica
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hereditaria
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dyschromatosis
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rna-editing
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rna-specific
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adenosine-to-inosine
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interferon-inducible
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ifn-inducible
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glur-b
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site-selective
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zalpha
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left-handed
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adar2-mediated
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hypopigmented
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dsrbds
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recoding
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hyperediting
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synthesis
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macules
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z-dna-binding
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genodermatosis
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dsrna-binding
- 1.14.13.154
-
editing
- inosine
-
a-to-i
- deaminases
-
deamination
-
symmetrica
-
hereditaria
-
dyschromatosis
-
rna-editing
-
rna-specific
-
adenosine-to-inosine
-
interferon-inducible
-
ifn-inducible
-
glur-b
-
site-selective
-
zalpha
-
left-handed
-
adar2-mediated
-
hypopigmented
-
dsrbds
-
recoding
-
hyperediting
- synthesis
-
macules
-
z-dna-binding
-
genodermatosis
-
dsrna-binding
Reaction
Synonyms
CYP113A1, EryK, erythromycin C-12 hydroxylase
ECTree
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Results
in table
51
Substrates Products
Substrates Products on EC 1.14.13.154 - erythromycin 12-hydroxylase
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REACTION DIAGRAM
erythromycin B + NADPH + H+ + O2
erythromycin A + NADP+ + H2O
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1200-1900-fold preference for erythromycin D over the alternative C-12 hydroxylase substrate erythromycin B
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?
erythromycin C + NADP+ + H2O
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?
erythromycin D + NADPH + H+ + O2
erythromycin C + NADP+ + H2O
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1200-1900-fold preference for erythromycin D over the alternative C-12 hydroxylase substrate erythromycin B
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?
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in a Saccharopolyspora venezuelae pikC deletion mutant, EryK can catalyze the hydroxylation of YC-17 and narbomycin to generate methymycin/neomethymycin and pikromycin, respectively. EryK is flexible toward some alternative polyketides and can be useful for structural diversification of macrolides by post-polyketide synthase hydroxylation
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additional information
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in a Saccharopolyspora venezuelae pikC deletion mutant, EryK can catalyze the hydroxylation of YC-17 and narbomycin to generate methymycin/neomethymycin and pikromycin, respectively. EryK is flexible toward some alternative polyketides and can be useful for structural diversification of macrolides by post-polyketide synthase hydroxylation
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?