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Literature summary for 1.14.14.19 extracted from

  • Nakajin, S.; Hall, P.F.
    Microsomal cytochrome P-450 from neonatal pig testis. Purification and properties of A C21 steroid side-chain cleavage system (17alpha-hydroxylase-C17,20 lyase) (1981), J. Biol. Chem., 256, 3871-3876.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
progesterone
-
Sus scrofa
0.0024
-
17alpha-hydroxyprogesterone
-
Sus scrofa

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome membrane-bound Sus scrofa
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Fe3+ 8 nM per mg protein Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
59000
-
SDS-PAGE and denaturating gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Sus scrofa
phospholipoprotein 40 nmol phospholipid per mg of protein Sus scrofa

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.008
-
lyase activity Sus scrofa
0.023
-
hydroxylase activity Sus scrofa

Storage Stability

Storage Stability Organism
-70°C, 0.2% Emulgen 913 v/v and 20% glycerol v/v, 6 months, no detectable loss of activity Sus scrofa

Subunits

Subunits Comment Organism
monomer alpha, 1 * 59000 Sus scrofa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Sus scrofa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Sus scrofa