BRENDA - Enzyme Database
show all sequences of 1.14.13.154

Identification of a Saccharopolyspora erythraea gene required for the final hydroxylation step in erythromycin biosynthesis

Stassi, D.; Donadio, S.; Staver, M.J.; Katz, L.; J. Bacteriol. 175, 182-189 (1993)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
-
Saccharopolyspora erythraea
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
43759
-
x * 43759, calculated from sequence
Saccharopolyspora erythraea
Organism
Organism
UniProt
Commentary
Textmining
Saccharopolyspora erythraea
P48635
-
-
Subunits
Subunits
Commentary
Organism
?
x * 43759, calculated from sequence
Saccharopolyspora erythraea
Synonyms
Synonyms
Commentary
Organism
EryK
-
Saccharopolyspora erythraea
erythromycin C-12 hydroxylase
-
Saccharopolyspora erythraea
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P-450
a heme-thiolate protein (P-450)
Saccharopolyspora erythraea
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Saccharopolyspora erythraea
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P-450
a heme-thiolate protein (P-450)
Saccharopolyspora erythraea
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
43759
-
x * 43759, calculated from sequence
Saccharopolyspora erythraea
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 43759, calculated from sequence
Saccharopolyspora erythraea
General Information
General Information
Commentary
Organism
malfunction
an Saccharopolyspora erythraea strain disrupted in eryK no longer produces erythromycin A but accumulates the B and D forms of the antibiotic
Saccharopolyspora erythraea
physiological function
the enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis
Saccharopolyspora erythraea
General Information (protein specific)
General Information
Commentary
Organism
malfunction
an Saccharopolyspora erythraea strain disrupted in eryK no longer produces erythromycin A but accumulates the B and D forms of the antibiotic
Saccharopolyspora erythraea
physiological function
the enzyme is responsible for the C-12 hydroxylation of the macrolactone ring, one of the last steps in erythromycin biosynthesis
Saccharopolyspora erythraea
Other publictions for EC 1.14.13.154
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
714227
Montemiglio
Azole drugs trap cytochrome P4 ...
Saccharopolyspora erythraea
Biochemistry
49
9199-9206
2010
-
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1
1
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2
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715499
Savino
Investigating the structural p ...
Saccharopolyspora erythraea
J. Biol. Chem.
284
29170-29179
2009
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1
1
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1
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1
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1
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713821
Chen
Genetic modulation of the over ...
Saccharopolyspora erythraea
Appl. Environ. Microbiol.
74
1820-1828
2008
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1
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716845
Savino
Cloning, expression, purificat ...
Saccharopolyspora erythraea
Protein Pept. Lett.
15
1138-1141
2008
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1
1
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2
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1
1
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714405
Lee
The role of erythromycin C-12 ...
Saccharopolyspora erythraea
Bioorg. Chem.
32
549-559
2004
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3
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1
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1
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1
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1
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714134
Lambalot
Overproduction and characteriz ...
Saccharopolyspora erythraea
Biochemistry
34
1858-1866
1995
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1
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1
1
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1
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3
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1
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3
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1
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1
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1
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2
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3
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1
1
715331
Stassi
Identification of a Saccharopo ...
Saccharopolyspora erythraea
J. Bacteriol.
175
182-189
1993
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1
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