BRENDA - Enzyme Database show
show all sequences of 1.14.11.B11

Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide

Strieker, M.; Kopp, F.; Mahlert, C.; Essen, L.O.; Marahiel, M.A.; ACS Chem. Biol. 2, 187-196 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli BL21
Streptomyces coelicolor
Crystallization (Commentary)
Crystallization
Organism
crystals of AsnO are grown at 18°C by the sitting-drop vapor diffusion method. 1.45, 1.92, and 1.66 A crystal structures of AsnO as apoprotein, Fe2+ complex, and product complex, respectively, with (2S,3S)-3-hydroxyasparagine and succinate
Streptomyces coelicolor
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.479
-
L-asparagine
pH 7.5, 25°C
Streptomyces coelicolor
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
no activity without Fe2+
Streptomyces coelicolor
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-asparagine + 2-oxoglutarate + O2
Streptomyces coelicolor
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
?
L-asparagine + 2-oxoglutarate + O2
Streptomyces coelicolor A3(2)
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptomyces coelicolor
Q9Z4Z5
-
-
Purification (Commentary)
Commentary
Organism
-
Streptomyces coelicolor
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-asparagine + 2-oxoglutarate + O2
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
721127
Streptomyces coelicolor
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
in presence of Fe2+ and 2-oxoglutarate, hydroxylation activity is observed exclusively with the L-enantiomer of the free amino acid
721127
Streptomyces coelicolor
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
721127
Streptomyces coelicolor A3(2)
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
in presence of Fe2+ and 2-oxoglutarate, hydroxylation activity is observed exclusively with the L-enantiomer of the free amino acid
721127
Streptomyces coelicolor A3(2)
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Streptomyces coelicolor
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.98
-
L-asparagine
pH 7.5, 25°C
Streptomyces coelicolor
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Streptomyces coelicolor
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli BL21
Streptomyces coelicolor
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystals of AsnO are grown at 18°C by the sitting-drop vapor diffusion method. 1.45, 1.92, and 1.66 A crystal structures of AsnO as apoprotein, Fe2+ complex, and product complex, respectively, with (2S,3S)-3-hydroxyasparagine and succinate
Streptomyces coelicolor
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.479
-
L-asparagine
pH 7.5, 25°C
Streptomyces coelicolor
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
no activity without Fe2+
Streptomyces coelicolor
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-asparagine + 2-oxoglutarate + O2
Streptomyces coelicolor
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
?
L-asparagine + 2-oxoglutarate + O2
Streptomyces coelicolor A3(2)
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Streptomyces coelicolor
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-asparagine + 2-oxoglutarate + O2
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
721127
Streptomyces coelicolor
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
in presence of Fe2+ and 2-oxoglutarate, hydroxylation activity is observed exclusively with the L-enantiomer of the free amino acid
721127
Streptomyces coelicolor
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
721127
Streptomyces coelicolor A3(2)
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
in presence of Fe2+ and 2-oxoglutarate, hydroxylation activity is observed exclusively with the L-enantiomer of the free amino acid
721127
Streptomyces coelicolor A3(2)
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Streptomyces coelicolor
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.98
-
L-asparagine
pH 7.5, 25°C
Streptomyces coelicolor
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Streptomyces coelicolor
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
Streptomyces coelicolor
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of (2S,3S)-3-hydroxyasparagine, a component of the lipopeptide lactone calcium-dependent antibiotic
Streptomyces coelicolor
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
10.3
-
L-asparagine
pH 7.5, 25°C
Streptomyces coelicolor
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
10.3
-
L-asparagine
pH 7.5, 25°C
Streptomyces coelicolor
Other publictions for EC 1.14.11.B11
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
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)
741694
Hara
One-Pot Production of L-threo ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
Appl. Environ. Microbiol.
81
3648-3654
2015
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1
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2
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1
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2
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42
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1
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1
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2
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1
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1
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2
1
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-
-
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-
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-
-
-
721127
Strieker
Mechanistic and structural bas ...
Streptomyces coelicolor
ACS Chem. Biol.
2
187-196
2007
-
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1
1
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1
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1
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2
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1
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1
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4
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1
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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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1
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2
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1
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4
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1
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1
1
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1
1
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1
1