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Literature summary extracted from

  • Quaye, J.A.; Gadda, G.
    Kinetic and bioinformatic characterization of D-2-hydroxyglutarate dehydrogenase from Pseudomonas aeruginosa PAO1 (2020), Biochemistry, 59, 4833-4844 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.99.39 expression in Escherichia coli strain Rosetta(DE3)pLysS Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.99.39 0.06
-
(S)-2-hydroxyglutarate pH 7.4, 25°C Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.99.39 (S)-2-hydroxyglutarate + acceptor Pseudomonas aeruginosa necessary step in the serine biosynthetic pathway 2-oxoglutarate + reduced acceptor
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.39 Pseudomonas aeruginosa Q9I6H4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.99.39
-
Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.39 (R)-2-hydroxyglutarate + phenazine methosulfate
-
Pseudomonas aeruginosa 2-oxoglutarate + reduced phenazine methosulfate
-
?
1.1.99.39 (S)-2-hydroxyglutarate + acceptor necessary step in the serine biosynthetic pathway Pseudomonas aeruginosa 2-oxoglutarate + reduced acceptor
-
?
1.1.99.39 D-malate + phenazine methosulfate
-
Pseudomonas aeruginosa ? + reduced phenazine methosulfate
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.99.39 D2HGDH
-
Pseudomonas aeruginosa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.99.39 11
-
(S)-2-hydroxyglutarate pH 7.4, 25°C Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.99.39 FAD
-
Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
1.1.99.39 drug target the dependence of Pseudomonas aeruginosa on PaD2HGDH makes the enzyme a potential therapeutic target against Pseudomonas aeruginosa Pseudomonas aeruginosa
1.1.99.39 evolution a phylogenetic tree analysis of D-2-hydroxyglutarate dehydrogenase from Pseudomonas aeruginosa, vanillyl alcohol oxidase, and human D-2-hydroxyglutarate dehydrogenase establishes genetic diversity among these enzymes Pseudomonas aeruginosa
1.1.99.39 physiological function the enzyme catalyzes a necessary step in the serine biosynthetic pathway Pseudomonas aeruginosa