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Literature summary extracted from

  • Kishore, G.M.; Snell, E.E.
    Interaction of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase with FAD, substrates, and analogues. Spectral and fluorescence investigations (1981), J. Biol. Chem., 256, 4234-4240.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.242 1-deaza-FAD
-
 Pseudomonas sp.
1.14.13.242 5-pyridoxic acid competitive Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.242 43000
-
 4 * 43000, SDS-PAGE Pseudomonas sp.
1.14.13.242 160000
-
 equilibrium sedimentation Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.242 Pseudomonas sp.
-
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.14.13.242 the enzyme is very sensitive to oxidation, it loses activity rapidly in absence of mercaptoethanol even at 4°C, it is further stabilized in presence of high concentrations of glycerol or by serum albumin Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.242 3-hydroxy-2-methylpyridine-5-carboxylate + NADH + O2
-
 Pseudomonas sp. 2-(acetamidomethylene)succinate + NAD(P)+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.242 tetramer 4 * 43000, SDS-PAGE Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.242 FAD contains 2 mol of FAD per mol of tetrameric enzyme. 412 nM Pseudomonas sp.
1.14.13.242 NADH interacts with the holoenzyme in a slow catalytically irrelevant manner Pseudomonas sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.14.13.242 0.00046
-
 1-deaza-FAD
-
 Pseudomonas sp.
1.14.13.242 0.023
-
 5-pyridoxic acid
-
 Pseudomonas sp.