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Literature summary for 1.1.5.13 extracted from

  • Kalliri, E.; Mulrooney, S.; Hausinger, R.
    Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase (2008), J. Bacteriol., 190, 3793-3798 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli C41(DE3) cells Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.095
-
L-2-hydroxyglutarate at pH 7.0 and 25┬░C Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-2-hydroxyglutarate + O2 Escherichia coli
-
2-oxoglutarate + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA-Sepharose 6 column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2-hydroxyglutarate + O2
-
Escherichia coli 2-oxoglutarate + H2O2
-
?
additional information no activity with dimethylglycine, sarcosine, butyraldehyde or 3-hydroxybutyric acid. Most 2-hydroxy acids are ineffective as substrates, including L-malic acid, DL-malic acid, DL-lactic acid, L-mandelic acid, D-mandelic acid, and 2-hydroxycaproic acid Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
? x * 47640, His-tagged protein, calculated from amino acid sequence Escherichia coli

Synonyms

Synonyms Comment Organism
L-2-hydroxyglutarate oxygenase
-
Escherichia coli
lhgO
-
Escherichia coli
YgaF
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.08
-
L-2-hydroxyglutarate at pH 7.0 and 25┬░C Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme contains a noncovalently bound FAD Escherichia coli
additional information not affected by NAD+ or NADP+ Escherichia coli