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Literature summary for 1.14.13.241 extracted from

  • Nelson, M.J.K.; Snell, E.E.
    Enzymes of vitamin B6 degradation. Purification and properties of 5-pyridoxic-acid oxygenase from Arthrobacter sp (1986), J. Biol. Chem., 261, 15115-15120.
    View publication on PubMed
Search for more literature for 1.14.13.241

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 NADPH
-
 Arthrobacter sp.
0.036
-
 5-pyridoxate
-
 Arthrobacter sp.
0.125
-
 O2
-
 Arthrobacter sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Arthrobacter sp. 5737
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
 native enzyme, gel filtration Arthrobacter sp.
39200
-
 native enzyme, sedimentation velocity Arthrobacter sp.
40000
-
 4 * 40000, SDS-PAGE Pseudomonas sp.
51000
-
 SDS-PAGE Arthrobacter sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2 + H3O+ Pseudomonas sp. bacterial vitamin B6 degradation pathway 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Arthrobacter sp.
-
-
-
Arthrobacter sp. Cr7
-
-
-
Pseudomonas sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas sp.
-
 Arthrobacter sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
8.5
-
-
 Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-hydroxy-2-methylpyridine-5-carboxylic acid + NADH poorly utilized substrate analoge Arthrobacter sp. 2-[(acetylamino)methylene]succinate + NAD+ + H2O
-
 ?
3-hydroxy-2-methylpyridine-5-carboxylic acid + NADH poorly utilized substrate analoge Arthrobacter sp. Cr7 2-[(acetylamino)methylene]succinate + NAD+ + H2O
-
 ?
3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O2 + H3O+ bacterial vitamin B6 degradation pathway Pseudomonas sp. 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP+ + H2O
-
 ?
5-pyridoxic acid + NADPH + O2 + H3O+
-
 Pseudomonas sp. 2-(acetylaminomethylene)succinate + NADP+ + H2O
-
 ?
5-pyridoxic acid + NADPH + O2 + H3O+
-
 Arthrobacter sp. 2-(acetylaminomethylene)succinate + NADP+ + H2O
-
 ?
5-pyridoxic acid + NADPH + O2 + H3O+
-
 Arthrobacter sp. Cr7 2-(acetylaminomethylene)succinate + NADP+ + H2O
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 51000, SDS-PAGE Arthrobacter sp.
tetramer 4 * 40000, SDS-PAGE Pseudomonas sp.

Synonyms

Synonyms Comment Organism
5-pyridoxic-acid oxygenase
-
 Arthrobacter sp.
compound I oxygenase
-
 Pseudomonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8
-
 Arthrobacter sp.
7.5
-
-
 Arthrobacter sp.

pH Range

pH Minimum pH Maximum Comment Organism
5.8 8.6
-
 Arthrobacter sp.

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Pseudomonas sp.
FAD one FAD per subunit, FMN or riboflavin do not replace FAD as coenzyme Arthrobacter sp.
NADH
-
 Pseudomonas sp.
NADH
-
 Arthrobacter sp.
NADPH
-
 Pseudomonas sp.
NADPH
-
 Arthrobacter sp.