Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Phizackerley, P.J.; Francis, M.J.
    Cofactor requirements of the L-malate dehydrogenase of Pseudomonas ovalis Chester (1966), Biochem. J., 101, 524-535.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.5.4 Phospholipid the nature of the phospholipid required to activate the enzyme depends on the nature of the quinone used in the assay system. When 2-methyl-1,4-naphthoquinone is used, a wide variety of phospholipids, including all these isolated from the organism, will activate the enzyme, but when coenzyme Q9 is used the phospholipid specificity of the enzyme is much more restricted, and the most effective activator is the unsaturated phosphatidylethanolamine isolated from the organism Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.4 0.0024
-
 ubiquinone 9 pH 7.0, 20°C Pseudomonas putida
1.1.5.4 0.45
-
 (S)-malate pH 7.0, 20°C Pseudomonas putida

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.5.4 membrane bound to the cell-wall membrane Pseudomonas putida 16020
-

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.4 Pseudomonas putida
-
 Chester
-
1.1.5.4 Pseudomonas putida Chester
-
 Chester
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.4 partial Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.4 (S)-malate + oxidized 2,6-dichlorophenol indophenol
-
 Pseudomonas putida oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
 ?
1.1.5.4 (S)-malate + oxidized 2,6-dichlorophenol indophenol
-
 Pseudomonas putida Chester oxaloacetate + reduced 2,6-dichlorophenol indophenol
-
 ?
1.1.5.4 (S)-malate + ubiquinone-9 in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor Pseudomonas putida oxaloacetate + ubiquinol-9
-
 ?
1.1.5.4 (S)-malate + ubiquinone-9 in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to these obtained with 2,6-dichlorophenol-indophenol as terminal acceptor Pseudomonas putida Chester oxaloacetate + ubiquinol-9
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.5.4 L-malate-quinone oxidoreductase
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.5.4 20
-
 assay at Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.4 7
-
 assay at Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.4 FAD triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. Km-value for FAD is 0.0004 mM Pseudomonas putida
1.1.5.4 menadione triple cofactor requirement for FAD, quinone and phospholipid. Maximum rate when phosphatidylethanolamine is added to the enzyme before the quinone Pseudomonas putida
1.1.5.4 ubiquinone-0 triple cofactor requirement for FAD, quinone and phospholipid. Maximum activation rate when phosphatidylethanolamine is added to the enzyme before the quinone Pseudomonas putida
1.1.5.4 ubiquinone-9 triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. The quinone is identified as ubiquinone 9. Km-value for ubiquinone 9 is 0.0024 mM Pseudomonas putida
1.1.5.4 vitamin K1 with both vitamin K1 and ubiquinone-9, maximum rates are obtained by exposing the enzyme to phospholipid and quinone simultaneously, but, when phosphatidylethanolamine is added to the enzyme before either of these quinones, the rates are much lower Pseudomonas putida