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Literature summary for 1.14.15.1 extracted from

  • Gunsalus, I.C.; Wagner, G.C.
    Bacterial P-450cam methylene monooxygenase components: cytochrome m, putidaredoxin, and putidaredoxin reductase (1978), Methods Enzymol., 52, 166-188.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
Pseudomonas putida PpG786, cytochrome m Pseudomonas putida

General Stability

General Stability Organism
2-mercaptoethanol retards loss of FeS-chromophore from putidaredoxin during purification Pseudomonas putida
glycerol, minimizes loss of FMN during purification of putidaredoxin reductase Pseudomonas putida
multiple freezing and thawing, at -20°C, cytochrome m accumulates an equally active, heme-containing component of higher molecular weight, DTT reconverts it to native cytochrome m at 25°C Pseudomonas putida

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
K+ increase of activity, selective effector of enhanced substrate affinity to cytochrome m Pseudomonas putida

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
putidaredoxin reductase: MW 45000 Da, putidaredoxin: MW 11000 Da, cytochrome m: MW 44000 Da, Pseudomonas putida PpG786, gel filtration Pseudomonas putida
additional information
-
putidaredoxin reductase, MW 43500 Da, putidaredoxin, MW 11594 Da, cytochrome m, MW 45000 Da, Pseudomonas putida PpG786, analytical data Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(+)-camphor + putidaredoxin + O2 Pseudomonas putida
-
(R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O i.e. (+)-exo-5-hydroxycamphor ?

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
PpG786, mutant derived from PpG1
-
Pseudomonas putida
-
Accession Number PC00183
-

Purification (Commentary)

Purification (Comment) Organism
PpG786 Pseudomonas putida

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
30.26
-
putidaredoxin reductase Pseudomonas putida

Storage Stability

Storage Stability Organism
-196°C, no loss of activity of putidaredoxin reductase after repeated freeze-thaw cycles Pseudomonas putida
0°C, putidaredoxin slowly loses its prosthetic group, 2-mercaptoethanol retards apoprotein formation Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(+)-camphor + putidaredoxin + O2
-
Pseudomonas putida (R)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O i.e. (+)-exo-5-hydroxycamphor ?

Subunits

Subunits Comment Organism
More multi-component mixed function monooxygenase consisting of putidaredoxin reductase, MW 47000, putidaredoxin, MW 11700, cytochrome m, MW 50500, Pseudomonas putida PpG786, SDS-PAGE Pseudomonas putida

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas putida

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2
-
putidaredoxin constituent protein of the multi-component oxygenase Pseudomonas putida
34
-
cytochrome m P-450cam, constituent part of the multi-component enzyme Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
cytochrome m cytochrome P-450cam, essential, b-type heme-thiolate protein of P-450-class Pseudomonas putida
FMN
-
Pseudomonas putida
NADH
-
Pseudomonas putida
putidaredoxin essential, iron-sulfur redox protein, Fe2S2*Cys4-class, e-transfer agent to and effector of cytochrome P450cam Pseudomonas putida