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Literature summary for 1.14.13.5 extracted from

  • Flashner, M.S.; Massey, V.
    Flavoprotein oxygenases (1974), Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York, , 245-283.
No PubMed abstract available
Search for more literature for 1.14.13.5

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Pseudomonas sp.

Inhibitors

Inhibitors Comment Organism Structure
p-chloromercuribenzoate
-
 Pseudomonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
87000 90000 sedimentation equilibrium, gel filtration Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-imidazoleacetate + NADH + O2 Pseudomonas sp. the enzyme is part of the histidine catabolic pathway in which imidazaloneacetate is converted to aspartic acid by way of formiminoaspartic acid 5-hydroxy-4-imidazoleacetate + NAD+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-imidazoleacetate + NAD(P)H + O2 + H+
-
 Pseudomonas sp. 5-hydroxy-4-imidazoleacetate + NAD(P)+ + H2O
-
 ?
4-imidazoleacetate + NADH + O2 the enzyme is part of the histidine catabolic pathway in which imidazaloneacetate is converted to aspartic acid by way of formiminoaspartic acid Pseudomonas sp. 5-hydroxy-4-imidazoleacetate + NAD+ + H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
FAD 1 mol per mol enzyme Pseudomonas sp.
FAD FAD is the only prosthetic group Pseudomonas sp.
NADH
-
 Pseudomonas sp.
NADPH less efficient than NADH Pseudomonas sp.