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Literature summary extracted from

  • Cammack, R.
    Assay, purification and properties of mammalian D-2-hydroxy acid dehydrogenase (1969), Biochem. J., 115, 55-64.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.5.10 oxalate
-
 Oryctolagus cuniculus
1.1.5.10 oxaloacetate
-
 Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.10 mitochondrion
-
 Oryctolagus cuniculus 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.5.10 95000
-
 combination of gel filtration data and the sedimentation coefficient Oryctolagus cuniculus
1.1.5.10 102000
-
 gel filtration Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.10 Oryctolagus cuniculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.10
-
 Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.5.10 kidney cortex Oryctolagus cuniculus
-

Storage Stability

EC Number Storage Stability Organism
1.1.5.10 4°C, 50 mM Tris-chloride buffer, pH 8-0, in the dark, stable for several weeks Oryctolagus cuniculus
1.1.5.10 4°C, as a precipitate in 32% (w/v) ammonium sulfate solution in 50 mM Tris-chloride buffer, pH 8.0, stable for several months Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.10 D-lactate + oxidized 2,6-dichloroindophenol
-
 Oryctolagus cuniculus pyruvate + reduced 2,6-dichloroindophenol
-
 ?
1.1.5.10 D-lactate + ubiquinone the rate with 0.06 mM ubiquinone is 72% of the rate with 2,6-dichloroindophenol Oryctolagus cuniculus pyruvate + ubiquinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.10 (R)-2-hydroxy acid dehydrogenase
-
 Oryctolagus cuniculus
1.1.5.10 (R)-2-hydroxy-acid:(acceptor) 2-oxidoreductase
-
 Oryctolagus cuniculus
1.1.5.10 D-lactate dehydrogenase ambiguous Oryctolagus cuniculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.5.10 30
-
 assay at Oryctolagus cuniculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.5.10 20
-
 pH 5.5-10, 30 min, stable Oryctolagus cuniculus
1.1.5.10 62
-
 pH 7.3, activity decreases by 79% in 10 min, in the presence of 1 mM oxalate the decrease is 5% Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.10 8.6
-
 assay at Oryctolagus cuniculus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.5.10 4.8
-
 20°C, 30 min, stable above pH 10.5 or below pH 4.8 Oryctolagus cuniculus
1.1.5.10 5.5 10 20°C, 30 min, stable Oryctolagus cuniculus
1.1.5.10 7.3
-
 unstable above 55°C Oryctolagus cuniculus
1.1.5.10 10.5
-
 20°C, 30 min, stable above pH 10.5 or below pH 4.8 Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.10 FAD the purified enzyme has a spectrum typical of a flavoprotein. The change induced in the spectrum on addition of D-malate or D-lactate suggests the formation of a flavin semiquinone. Flavin can be removed by treatment with acid ammonium sulfate, and activity can be restored to the inactive apoenzyme by addition of FAD, but not of FMN or riboflavin Oryctolagus cuniculus