Literature summary for 1.14.15.6 extracted from

Kubeil, C.; Yeung, J.; Tuckey, R.; Rodgers, R.; Martin, L.
Membrane-mediated protein-protein interactions of cholesterol side-chain cleavage cytochrome P450 with its associated electron transport proteins (2016), ChemPlusChem, 81, 995-1002 .

No PubMed abstract available

Search for more literature for 1.14.15.6

Application

Application	Comment	Organism
analysis	examination of protein-membrane interactions between P450scc and its redox partners on 1,2-dimyristoyl-sn-glycero-3-phosphocholine membranes containing cholesterol (20%), using a quartz crystal microbalance with dissipation monitoring	Bos taurus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Bos taurus	16020	-
mitochondrion	-	Bos taurus	5739	-

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P00189	-	-

Synonyms

Synonyms	Comment	Organism
P450scc	-	Bos taurus

General Information

General Information	Comment	Organism
physiological function	the activity of P450scc is dependent upon electron delivery from NADPH-dependent adrenodoxin reductase (AdR), via adrenodoxin (Adx). The lipid membrane assists in the assembly of electron transport proteins and the activity of P450scc by providing a surface for the localized concentration of proteins. Using sequential deposition with P450scc first (to saturation), there is effectively no further binding of AdR or Adx. When premixing the three proteins, P450scc, Adx and AdR, all bind the membrane in a two-stage process	Bos taurus

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Release 2023.1 (January 2023)