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Literature summary for 1.14.15.1 extracted from

  • Tsai, R.L.; Gunsalus, I.C.; Dus, K.
    Composition and structure of camphor hydroxylase components and homology between putidaredoxin and adrenodoxin (1971), Biochem. Biophys. Res. Commun., 45, 1300-1306.
    View publication on PubMed
Search for more literature for 1.14.15.1

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Pseudomonas putida 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ requirement, enzyme complex with two FeS-protein components Pseudomonas putida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 FMN-containing NADH-reductase, MW 43500 Da, putidaredoxin, MW 12500 Da, cytochrome P-450cam, MW 45000 Da, Pseudomonas putida C1, ultracentrifugal analysis, gel filtration, end group analysis and quantification of prosthetic group material Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-
Pseudomonas putida
-
 Accession Number PC00183
-
Pseudomonas putida C1 / ATCC 17453
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein small amount of carbohydrate in putidaredoxin and in cytochrome P-450cam Pseudomonas putida

Purification (Commentary)

Purification (Comment) Organism
C1 Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
cytochrome m
-
 Pseudomonas putida
FAD increase of activity, can replace FMN Pseudomonas putida
FMN requirement, prosthetic group of putidaredoxin reductase Pseudomonas putida
NADPH
-
 Pseudomonas putida
putidaredoxin
-
 Pseudomonas putida