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Literature summary for 1.14.15.6 extracted from

  • Nazarov, P.A.; Drutsa, V.L.; Miller, W.L.; Shkumatov, V.M.; Luzikov, V.N.; Novikova, L.A.
    Formation and functioning of fused cholesterol side-chain cleavage enzymes (2003), DNA Cell Biol., 22, 243-252.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information construction of fusion proteins of enzyme plus adrenodoxin plus adrenodoxin reductase, fusion in order bovine enzyme - adrenodoxin - adrenodoxin reductase gives 30-fold higher enzymatic activity than fusion in same order with human enzyme and 14-fold higher activity than fusion with human enzyme in order adrenodoxin reductase – adrenodoxin – enzyme. Dimers of enzyme with adrenodoxin in order enzyme – adrenodoxin or adrenodoxin – enzyme show minimal side chain cleavage activity. CO difference spectra reveal a denatured cytochrome P450 in dimer fusion proteins Homo sapiens
additional information construction of fusion proteins of enzyme plus adrenodoxin plus adrenodoxin reductase, fusion in order enzyme - adrenodoxin - adrenodoxin reductase gives 30-fold higher enzymatic activity than fusion in same order with human enzyme and 14-fold higher activity than fusion with human enzyme in order adrenodoxin reductase – adrenodoxin – enzyme. CO-difference spectra do not show the presence of a normally folded enzyme moiety Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
x * 120000, fusion protein of enzyme plus adrenodoxin reductase plus adrenodoxin Homo sapiens
120000
-
x * 120000, fusion protein of enzyme plus adrenodoxin reductase plus adrenodoxin Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
fusion protein with adrenodoxin and/or adrenodoxin reductase
-
Homo sapiens
-
fusion protein with adrenodoxin and/or adrenodoxin reductase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
22(R)-hydroxycholesterol + reduced adrenodoxin + O2
-
Homo sapiens pregnenolone + oxidized adrenodoxin + H2O
-
?
22(R)-hydroxycholesterol + reduced adrenodoxin + O2
-
Bos taurus pregnenolone + oxidized adrenodoxin + H2O
-
?

Subunits

Subunits Comment Organism
? x * 120000, fusion protein of enzyme plus adrenodoxin reductase plus adrenodoxin Homo sapiens
? x * 120000, fusion protein of enzyme plus adrenodoxin reductase plus adrenodoxin Bos taurus

Cofactor

Cofactor Comment Organism Structure
cytochrome P450
-
Homo sapiens
cytochrome P450
-
Bos taurus