BRENDA - Enzyme Database
show all sequences of 1.14.11.39

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)
Cloned (Commentary)
Organism
expressed in Escherichia coli as His7-tagged fusion
Streptomyces coelicolor
Crystallization (Commentary)
Crystallization (Commentary)
Organism
crystals are grown at 18°C by the sitting-drop vapordiffusion method, 1.45 A, 1.92 A 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+
non-heme Fe2+ enzyme
Streptomyces coelicolor
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-asparagine + 2-oxoglutarate + O2
Streptomyces coelicolor
the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
?
L-asparagine + 2-oxoglutarate + O2
Streptomyces coelicolor A3(2)
the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Streptomyces coelicolor
Q9Z4Z5
-
-
Streptomyces coelicolor A3(2)
Q9Z4Z5
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Streptomyces coelicolor
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-asparagine + 2-oxoglutarate + O2
the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone
721127
Streptomyces coelicolor
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
the enzyme exclusively acts on free L-asparagine. It is not active toward D-asparagine
721127
Streptomyces coelicolor
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone
721127
Streptomyces coelicolor A3(2)
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
the enzyme exclusively acts on free L-asparagine. It is not active toward D-asparagine
721127
Streptomyces coelicolor A3(2)
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
AsnO
-
Streptomyces coelicolor
L-asparagine 3-hydroxylase
-
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
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli as His7-tagged fusion
Streptomyces coelicolor
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystals are grown at 18°C by the sitting-drop vapordiffusion method, 1.45 A, 1.92 A 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+
non-heme Fe2+ enzyme
Streptomyces coelicolor
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-asparagine + 2-oxoglutarate + O2
Streptomyces coelicolor
the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
?
L-asparagine + 2-oxoglutarate + O2
Streptomyces coelicolor A3(2)
the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone
(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
ID
L-asparagine + 2-oxoglutarate + O2
the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone
721127
Streptomyces coelicolor
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
the enzyme exclusively acts on free L-asparagine. It is not active toward D-asparagine
721127
Streptomyces coelicolor
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
the beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone
721127
Streptomyces coelicolor A3(2)
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
L-asparagine + 2-oxoglutarate + O2
the enzyme exclusively acts on free L-asparagine. It is not active toward D-asparagine
721127
Streptomyces coelicolor A3(2)
(2S,3S)-3-hydroxyasparagine + succinate + CO2
-
-
-
?
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
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
10.4
-
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
10.4
-
L-asparagine
pH 7.5, 25°C
Streptomyces coelicolor
Other publictions for EC 1.14.11.39
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)
721127
Strieker
Mechanistic and structural bas ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
ACS Chem. Biol.
2
187-196
2007
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1
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1
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1
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725895
Neary
An asparagine oxygenase (AsnO) ...
Streptomyces coelicolor, Streptomyces coelicolor A3(2)
Microbiology
153
768-776
2007
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2
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