BRENDA - Enzyme Database
show all sequences of 1.14.11.49

Characterization of LipL as a non-heme, Fe(II)-dependent alpha-ketoglutarate:UMP dioxygenase that generates uridine-5-aldehyde during A-90289 biosynthesis

Yang, Z.; Chi, X.; Funabashi, M.; Baba, S.; Nonaka, K.; Pahari, P.; Unrine, J.; Jacobsen, J.M.; Elliott, G.I.; Rohr, J.; Van Lanen, S.G.; J. Biol. Chem. 286, 7885-7892 (2011)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ascorbate
1 mM activates
Streptomyces sp.
Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli BL21(DE3) cells
Streptomyces sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
Co2+
less than 15% activity at 1 mM
Streptomyces sp.
Cu2+
less than 5% activity at 1 mM
Streptomyces sp.
Fe3+
less than 10% activity at 1 mM
Streptomyces sp.
Mn2+
less than 15% activity at 1 mM
Streptomyces sp.
Ni2+
20% residual activity at 1 mM
Streptomyces sp.
Zn2+
less than 1% activity at 1 mM
Streptomyces sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0075
-
2-oxoglutarate
at pH 7.5 and 30°C
Streptomyces sp.
0.014
-
UMP
at pH 7.5 and 30°C
Streptomyces sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
dependent on, optimal activity in the range of 0.002-0.1 mM FeCl2, 0.02 mM used in assay conditions
Streptomyces sp.
additional information
not influenced by Ca2+, K+ and Mg2+
Streptomyces sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38000
-
x * 38000, His6-tagged enzyme, SDS-PAGE
Streptomyces sp.
38200
-
x * 38200, His6-tagged enzyme, calculated from amino acid sequence
Streptomyces sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Streptomyces sp.
in the absence of the prime substrate UMP, the enzyme is able to catalyze oxidative decarboxylation of 2-oxoglutarate, although at a significantly reduced rate
?
-
-
?
additional information
Streptomyces sp.
uridine and UDP, pyruvate, 2-oxoadipate, 2-oxobutyrate, 2-oxovalerate, and oxaloacetate are not recognized as substrates. The enzyme is unable to catalyze dephosphorylation and aldehyde formation using the remaining canonical, monophosphorylated ribo- or deoxyribonucleotides
?
-
-
?
additional information
Streptomyces sp. SANK60405
in the absence of the prime substrate UMP, the enzyme is able to catalyze oxidative decarboxylation of 2-oxoglutarate, although at a significantly reduced rate
?
-
-
?
additional information
Streptomyces sp. SANK60405
uridine and UDP, pyruvate, 2-oxoadipate, 2-oxobutyrate, 2-oxovalerate, and oxaloacetate are not recognized as substrates. The enzyme is unable to catalyze dephosphorylation and aldehyde formation using the remaining canonical, monophosphorylated ribo- or deoxyribonucleotides
?
-
-
?
UMP + 2-oxoglutarate + O2
Streptomyces sp.
-
5'-dehydrouridine + succinate + CO2 + phosphate
-
-
?
UMP + 2-oxoglutarate + O2
Streptomyces sp. SANK60405
-
5'-dehydrouridine + succinate + CO2 + phosphate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Streptomyces sp.
-
-
-
Streptomyces sp. SANK60405
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
nickel-nitrilotriacetic acid-agarose column chromatography
Streptomyces sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
in the absence of the prime substrate UMP, the enzyme is able to catalyze oxidative decarboxylation of 2-oxoglutarate, although at a significantly reduced rate
734171
Streptomyces sp.
?
-
-
-
?
additional information
uridine and UDP, pyruvate, 2-oxoadipate, 2-oxobutyrate, 2-oxovalerate, and oxaloacetate are not recognized as substrates. The enzyme is unable to catalyze dephosphorylation and aldehyde formation using the remaining canonical, monophosphorylated ribo- or deoxyribonucleotides
734171
Streptomyces sp.
?
-
-
-
?
additional information
in the absence of the prime substrate UMP, the enzyme is able to catalyze oxidative decarboxylation of 2-oxoglutarate, although at a significantly reduced rate
734171
Streptomyces sp. SANK60405
?
-
-
-
?
additional information
uridine and UDP, pyruvate, 2-oxoadipate, 2-oxobutyrate, 2-oxovalerate, and oxaloacetate are not recognized as substrates. The enzyme is unable to catalyze dephosphorylation and aldehyde formation using the remaining canonical, monophosphorylated ribo- or deoxyribonucleotides
734171
Streptomyces sp. SANK60405
?
-
-
-
?
UMP + 2-oxoglutarate + O2
-
734171
Streptomyces sp.
5'-dehydrouridine + succinate + CO2 + phosphate
-
-
-
?
UMP + 2-oxoglutarate + O2
-
734171
Streptomyces sp. SANK60405
5'-dehydrouridine + succinate + CO2 + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 38000, His6-tagged enzyme, SDS-PAGE
Streptomyces sp.
?
x * 38200, His6-tagged enzyme, calculated from amino acid sequence
Streptomyces sp.
Synonyms
Synonyms
Commentary
Organism
alpha-ketoglutarate:UMP dioxygenase
-
Streptomyces sp.
alpha-KG:UMP dioxygenase
-
Streptomyces sp.
LIPL
-
Streptomyces sp.
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.27
-
UMP
at pH 7.5 and 30°C
Streptomyces sp.
1.53
-
2-oxoglutarate
at pH 7.5 and 30°C
Streptomyces sp.
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
does not contain heme
Streptomyces sp.
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ascorbate
1 mM activates
Streptomyces sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL21(DE3) cells
Streptomyces sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
does not contain heme
Streptomyces sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Co2+
less than 15% activity at 1 mM
Streptomyces sp.
Cu2+
less than 5% activity at 1 mM
Streptomyces sp.
Fe3+
less than 10% activity at 1 mM
Streptomyces sp.
Mn2+
less than 15% activity at 1 mM
Streptomyces sp.
Ni2+
20% residual activity at 1 mM
Streptomyces sp.
Zn2+
less than 1% activity at 1 mM
Streptomyces sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0075
-
2-oxoglutarate
at pH 7.5 and 30°C
Streptomyces sp.
0.014
-
UMP
at pH 7.5 and 30°C
Streptomyces sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
dependent on, optimal activity in the range of 0.002-0.1 mM FeCl2, 0.02 mM used in assay conditions
Streptomyces sp.
additional information
not influenced by Ca2+, K+ and Mg2+
Streptomyces sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38000
-
x * 38000, His6-tagged enzyme, SDS-PAGE
Streptomyces sp.
38200
-
x * 38200, His6-tagged enzyme, calculated from amino acid sequence
Streptomyces sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
additional information
Streptomyces sp.
in the absence of the prime substrate UMP, the enzyme is able to catalyze oxidative decarboxylation of 2-oxoglutarate, although at a significantly reduced rate
?
-
-
?
additional information
Streptomyces sp.
uridine and UDP, pyruvate, 2-oxoadipate, 2-oxobutyrate, 2-oxovalerate, and oxaloacetate are not recognized as substrates. The enzyme is unable to catalyze dephosphorylation and aldehyde formation using the remaining canonical, monophosphorylated ribo- or deoxyribonucleotides
?
-
-
?
additional information
Streptomyces sp. SANK60405
in the absence of the prime substrate UMP, the enzyme is able to catalyze oxidative decarboxylation of 2-oxoglutarate, although at a significantly reduced rate
?
-
-
?
additional information
Streptomyces sp. SANK60405
uridine and UDP, pyruvate, 2-oxoadipate, 2-oxobutyrate, 2-oxovalerate, and oxaloacetate are not recognized as substrates. The enzyme is unable to catalyze dephosphorylation and aldehyde formation using the remaining canonical, monophosphorylated ribo- or deoxyribonucleotides
?
-
-
?
UMP + 2-oxoglutarate + O2
Streptomyces sp.
-
5'-dehydrouridine + succinate + CO2 + phosphate
-
-
?
UMP + 2-oxoglutarate + O2
Streptomyces sp. SANK60405
-
5'-dehydrouridine + succinate + CO2 + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
nickel-nitrilotriacetic acid-agarose column chromatography
Streptomyces sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
in the absence of the prime substrate UMP, the enzyme is able to catalyze oxidative decarboxylation of 2-oxoglutarate, although at a significantly reduced rate
734171
Streptomyces sp.
?
-
-
-
?
additional information
uridine and UDP, pyruvate, 2-oxoadipate, 2-oxobutyrate, 2-oxovalerate, and oxaloacetate are not recognized as substrates. The enzyme is unable to catalyze dephosphorylation and aldehyde formation using the remaining canonical, monophosphorylated ribo- or deoxyribonucleotides
734171
Streptomyces sp.
?
-
-
-
?
additional information
in the absence of the prime substrate UMP, the enzyme is able to catalyze oxidative decarboxylation of 2-oxoglutarate, although at a significantly reduced rate
734171
Streptomyces sp. SANK60405
?
-
-
-
?
additional information
uridine and UDP, pyruvate, 2-oxoadipate, 2-oxobutyrate, 2-oxovalerate, and oxaloacetate are not recognized as substrates. The enzyme is unable to catalyze dephosphorylation and aldehyde formation using the remaining canonical, monophosphorylated ribo- or deoxyribonucleotides
734171
Streptomyces sp. SANK60405
?
-
-
-
?
UMP + 2-oxoglutarate + O2
-
734171
Streptomyces sp.
5'-dehydrouridine + succinate + CO2 + phosphate
-
-
-
?
UMP + 2-oxoglutarate + O2
-
734171
Streptomyces sp. SANK60405
5'-dehydrouridine + succinate + CO2 + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 38000, His6-tagged enzyme, SDS-PAGE
Streptomyces sp.
?
x * 38200, His6-tagged enzyme, calculated from amino acid sequence
Streptomyces sp.
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.27
-
UMP
at pH 7.5 and 30°C
Streptomyces sp.
1.53
-
2-oxoglutarate
at pH 7.5 and 30°C
Streptomyces sp.
Other publictions for EC 1.14.11.49
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)
734626
Yang
Fe(II)-dependent, uridine-5-mo ...
Streptomyces sp., Streptomyces sp. SANK 60405
Methods Enzymol.
516
153-168
2012
-
-
1
-
-
-
-
-
-
1
2
2
-
3
-
-
1
-
-
-
-
-
2
2
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
2
2
-
-
-
1
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
734171
Yang
Characterization of LipL as a ...
Streptomyces sp., Streptomyces sp. SANK60405
J. Biol. Chem.
286
7885-7892
2011
1
-
1
-
-
-
6
2
-
2
2
6
-
2
-
-
1
-
-
-
-
-
6
2
3
-
-
-
2
-
-
-
1
-
-
-
1
-
1
1
-
-
-
-
6
-
2
-
2
2
6
-
-
-
1
-
-
-
-
6
2
-
-
-
2
-
-
-
-
-
-
-
-
-
-