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Literature summary for 1.14.13.242 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

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Oxidation Stability

Oxidation Stability Organism
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)

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

Subunits

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

Cofactor

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

Ki Value [mM]

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