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Literature summary for 1.14.11.49 extracted from

  • 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.
    Characterization of LipL as a non-heme, Fe(II)-dependent alpha-ketoglutarate:UMP dioxygenase that generates uridine-5-aldehyde during A-90289 biosynthesis (2011), J. Biol. Chem., 286, 7885-7892.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.49

Activating Compound

Activating Compound Comment Organism Structure
ascorbate 1 mM activates Streptomyces sp.

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Streptomyces sp.

Inhibitors

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 [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

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 [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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Streptomyces sp.
-
-
-
Streptomyces sp. SANK60405
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel-nitrilotriacetic acid-agarose column chromatography Streptomyces sp.

Substrates and Products (Substrate)

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

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

Synonyms Comment 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 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

Cofactor Comment Organism Structure
additional information does not contain heme Streptomyces sp.