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Literature summary for 1.11.2.4 extracted from

  • Lee, D.-S.; Yamada, A.; Sugimoto, H.; Matsunaga, I.; Ogura, H.; Ichihara, K.; Adachi, S.-i.; Park, S.-Y.; Shiro, Y.
    Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis: Crystallographic, spectroscopic, and mutational studies (2003), J. Biol. Chem., 278, 9761-9767.
    View publication on PubMed
Search for more literature for 1.11.2.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli M15 (pREP4) cells Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
ferric P450BSbeta in the substrate-bound form, sitting drop vapor diffusion method, using 10% (w/v) polyethylene glycol 3350 and 50 mM MES at pH 6.8, at 20°C Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
F79L the specific activity is reduced by half compared to the wild type enzyme Bacillus subtilis
F79L/V170F the double mutant exhibits 10% of the activity of the wild type enzyme Bacillus subtilis
V170F the mutant exhibits 30% of the activity of the wild type enzyme Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus subtilis P450BSbeta produces both the beta-OH (60%) and the alpha-OH (40%) fatty acids. Ferredoxin, ferredoxin reductase, and P450 reductase systems do not appear to function in P450BSbeta reactions. P450BSbeta does not require any electrons and protons for catalytic activity, because it utilizes H2O2 as an oxidant instead of O2/2e-/2H+. This enzyme requires neither a reductase nor a proton delivery system ?
-
 ?
myristic acid + H2O2 Bacillus subtilis
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O31440
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information P450BSbeta produces both the beta-OH (60%) and the alpha-OH (40%) fatty acids. Ferredoxin, ferredoxin reductase, and P450 reductase systems do not appear to function in P450BSbeta reactions. P450BSbeta does not require any electrons and protons for catalytic activity, because it utilizes H2O2 as an oxidant instead of O2/2e-/2H+. This enzyme requires neither a reductase nor a proton delivery system Bacillus subtilis ?
-
 ?
myristic acid + H2O2
-
 Bacillus subtilis ?
-
 ?
palmitic acid + H2O2
-
 Bacillus subtilis ?
-
 ?

Synonyms

Synonyms Comment Organism
CYP152A1
-
 Bacillus subtilis
P450BSbeta
-
 Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
heme
-
 Bacillus subtilis