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Literature summary extracted from

  • Mast, N.; Annalora, A.; Lodowski, D.; Palczewski, K.; Stout, C.; Pikuleva, I.
    Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1 (2011), J. Biol. Chem., 286, 5607-5613.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.6 recombinant expression of C-terminally His4-tagged CYP11A1 Bos taurus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.15.6 CYP11A1 in complex with (22R)-22-hydroxycholesterol, sitting drop vapour diffusion methdo, mixing of 0.001 ml of 23 mg/ml protein in 50 mM potassium phosphate, pH 7.2, 20% glycerol, 0.1 M NaCl, 0.1% octyl pentaethylene glycol ether, 1 mM EDTA, and 0.05 mM (22R)-22-hydroxycholesterol, with 0.001 ml of precipitant solution containing 14% PEG 1000, 20% glycerol, 12% JEFFAMINE ED-2001, 0.1 M MES, pH 7.0, and 10% isopropyl alcohol, 18°C, overnight, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement using rat mitochondrial CYP24A1 Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.15.6 mitochondrion
-
 Bos taurus 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.6 (20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2 Bos taurus
-
 pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O
-
 ?
1.14.15.6 (22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O2 Bos taurus
-
 (20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H2O
-
 ?
1.14.15.6 cholesterol + 2 reduced adrenodoxin + O2 Bos taurus
-
 (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
-
 ?
1.14.15.6 cholesterol + 6 reduced adrenodoxin + 3 O2 Bos taurus overall reaction pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.6 Bos taurus P00189
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.6 recombinant C-terminally His4-tagged CYP11A1 by anion exchange, nickel affinity, hydroxylapatite, adrenodoxin affinity chromatography, and gel filtration Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.6 (20R,22R)-20,22-dihydroxy-cholesterol + 2 reduced adrenodoxin + O2
-
 Bos taurus pregnenolone + 4-methylpentanal + 2 oxidized adrenodoxin + 2 H2O
-
 ?
1.14.15.6 (22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O2
-
 Bos taurus (20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H2O
-
 ?
1.14.15.6 (22R)-22-hydroxycholesterol + 2 reduced adrenodoxin + O2 product binding structure analysis, detailed overview Bos taurus (20R,22R)-20,22-dihydroxycholesterol + 2 oxidized adrenodoxin + H2O
-
 ?
1.14.15.6 cholesterol + 2 reduced adrenodoxin + O2
-
 Bos taurus (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H2O
-
 ?
1.14.15.6 cholesterol + 6 reduced adrenodoxin + 3 O2 overall reaction Bos taurus pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.15.6 cholesterol side chain cleavage enzyme
-
 Bos taurus
1.14.15.6 CYP11A1
-
 Bos taurus
1.14.15.6 cytochrome P450 11A1
-
 Bos taurus
1.14.15.6 P450 11A1
-
 Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.6 adrenodoxin
-
 Bos taurus
1.14.15.6 cytochrome P450
-
 Bos taurus
1.14.15.6 heme site of catalysis Bos taurus

General Information

EC Number General Information Comment Organism
1.14.15.6 additional information the active site cavity in CYP11A1 represents a long curved tube that extends from the protein surface to the heme group, the site of catalysis. Shuttling of the sterol intermediates between the active site entrance and the heme group during the three-step reaction. Structural basis of the strict substrate specificity and high catalytic efficiency of the enzyme, overview Bos taurus