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Literature summary for 1.14.13.5 extracted from

  • Maki, Y.; Yamamoto, S.; Nozaki, M.; Hayaishi, O.
    Crystallization of imidazolacetate monooxygenase and its characterization as flavoprotein (1966), Biochem. Biophys. Res. Commun., 25, 609-614.
No PubMed abstract available
Search for more literature for 1.14.13.5

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 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.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using protamine sulfate treatment, ammonium sulfate fractionation, chromatography on TEAE-cellulose column, calcium phosphate gel treatment and chromatography on DEAE-Sephadex column Pseudomonas sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
25
-
-
 Pseudomonas sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 cannot be replaced by FMN or riboflavin Pseudomonas sp.
NADH
-
 Pseudomonas sp.