Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ascorbate | 1 mM activates | Streptomyces sp. |
Cloned (Comment) | Organism |
---|---|
expressed in Escherichia coli BL21(DE3) cells | Streptomyces sp. |
Inhibitors | Comment | 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 Maximum [mM] | Substrate | Comment | 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 | Comment | 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 Maximum [Da] | Comment | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces sp. | - |
- |
- |
Streptomyces sp. SANK60405 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
nickel-nitrilotriacetic acid-agarose column chromatography | Streptomyces sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | 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 | 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 | 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 | Streptomyces sp. SANK60405 | ? | - |
? | |
UMP + 2-oxoglutarate + O2 | - |
Streptomyces sp. | 5'-dehydrouridine + succinate + CO2 + phosphate | - |
? | |
UMP + 2-oxoglutarate + O2 | - |
Streptomyces sp. SANK60405 | 5'-dehydrouridine + succinate + CO2 + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 38000, His6-tagged enzyme, SDS-PAGE | Streptomyces sp. |
? | x * 38200, His6-tagged enzyme, calculated from amino acid sequence | Streptomyces sp. |
Synonyms | Comment | Organism |
---|---|---|
alpha-ketoglutarate:UMP dioxygenase | - |
Streptomyces sp. |
alpha-KG:UMP dioxygenase | - |
Streptomyces sp. |
LIPL | - |
Streptomyces sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | 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 | Comment | Organism | Structure |
---|---|---|---|
additional information | does not contain heme | Streptomyces sp. |