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Literature summary extracted from

  • Usanov, S.A.; Graham, S.E.; Lepesheva, G.I.; Azeva, T.N.; Strushkevich, N.V.; Gilep, A.A.; Estabrook, R.W.; Peterson, J.
    Probing the interaction of bovine cytochrome P450scc (CYP11A1) with adrenodoxin: evaluating site-directed mutations by molecular modeling (2002), Biochemistry, 41, 8310-8320.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.6 mutants and wild-type expressed in Escherichia coli Bos taurus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.6 K103Q expression similar to wild-type, decreased stability or an altered heme or substrate pocket, B'-C loop, no change in interaction of P-450scc and adrenodoxin Bos taurus
1.14.15.6 K104Q decreased expression, B'-C loop, no change in interaction of P-450scc and adrenodoxin Bos taurus
1.14.15.6 K109Q change in folding, thus, an inability of heme to be retained, helix C, no change in interaction of P-450scc and adrenodoxin Bos taurus
1.14.15.6 K110Q expression similar to wild-type, helix C, does not appear to play a role in adrenodoxin binding because it shows no change in interaction of P-450scc and adrenodoxin Bos taurus
1.14.15.6 K145Q expression similar to wild-type, helix D Bos taurus
1.14.15.6 K148Q extremely unstable, helix D Bos taurus
1.14.15.6 K338Q removed from heme group but still very important for interaction with adrenodoxin, K helix Bos taurus
1.14.15.6 K342Q removed from heme group but still very important for interaction with adrenodoxin, K helix Bos taurus
1.14.15.6 K394Q expression similar to wild-type, "meander", involved in the interaction of P-450scc with its electron-transfer partners Bos taurus
1.14.15.6 K403Q expression similar to wild-type, located between the meander and the heme-binding region, important role in electrostatic interactions with adrenodoxin, ability to bind adrenodoxin affected to lower extent than K405Q Bos taurus
1.14.15.6 K405Q expression similar to wild-type, 4fold decrease in efficiency of enzymatic reduction by adrenodoxin and adrenodoxin reductase, and a 3.3fold decrease of cholesterol side chain cleavage activity, located between the meander and the heme-binding region, important role in electrostatic interactions with adrenodoxin Bos taurus
1.14.15.6 additional information site directed mutagenesis. complex stabilizing salt bridges: K403 of P-450scc with D76 of adrenodoxin, K405 with D72, R426 with E73 and K267 with E47, multiple electrostatic interactions between the negatively charged residues of adrenodoxin and positively charged groups of P-450scc Bos taurus
1.14.15.6 R425Q most harmful substitution, L helix, heme-binding region Bos taurus
1.14.15.6 R425Q/R426C double mutant, most harmful substitution Bos taurus
1.14.15.6 R425Q/R426Q double mutant, most harmful substitution Bos taurus
1.14.15.6 R426Q expression similar to wild-type, serious changes in proteine folding and ability to insert and bind heme correctly, unable to catalyze cholesterol side chain cleavage reaction, although it is able to bind cholesterol, L helix, heme-binding region, important role in electrostatic interactions with adrenodoxin Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.15.6 mitochondrial inner membrane inner membrane Bos taurus 5743
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.6 cholesterol + 6 reduced adrenodoxin + 3 O2 Bos taurus
-
 pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O precursor of all steroid hormones ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.6 precipitation with polyethylene glycol, affinity chromatography Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.15.6 adrenal cortex
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.6 cholesterol + 6 reduced adrenodoxin + 3 O2
-
 Bos taurus pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O precursor of all steroid hormones ?
1.14.15.6 cholesterol + reduced adrenodoxin + O2
-
 Bos taurus pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O
-
 ?
1.14.15.6 additional information 2 interaction processes with 2 different sensitivities to ionic strength Bos taurus ?
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.15.6 7.2
-
 assay at Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.6 adrenodoxin electron shuttle Bos taurus
1.14.15.6 NADPH
-
 Bos taurus