| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| In an in vitro reconstituted system consisting of both mat COX / ADX and mat ADR containing fractions , bovine P450scc converted cholesterol into pregnenolone . ^^^ Thus mat COX / ADX and mat ADR produced in the yeast can transfer electrons from NADPH to P450scc . . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| Rat adrenal mitochondria contain approximately equal levels of P450scc and P 45011 beta , each reduced by NADPH through adrenodoxin reductase ( ADX reductase ) and adrenodoxin ( ADX ) . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| The content of the side chain cleavage ( SCC ) enzymes cytochrome P450scc and adrenodoxin ( ADX ) and the steady state availability of their mRNAs were determined and compared to P 4 production in each of the luteal cell types . ^^^ Moreover , 8 days after stimulant removal , LLC retained their P 4 production capacity , expressed P450scc and ADX mRNAs , and contained these proteins . ^^^ In the SLC , P 4 production , P450scc and ADX content , and their mRNAs showed a much stronger dependence on chronic cAMP ( and insulin ) stimulation . ^^^ In SLC , stimulant removal was accompanied by a sharp decrease ( 95 % reduction ) in P 4 production , P450scc and ADX enzyme content ( 57 % and 90 % reduction , respectively ) , and their mRNAs ( 90 % and 95 % reduction , respectively ) . ^^^ Interestingly , P 4 production by both luteal cells types was reflected better in ADX than in P450scc content . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| The conversion of cholesterol to pregnenolone , the rate limiting step in steroid hormone synthesis , occurs on mitochondrial cytochrome P450scc , which catalyzes this reaction by receiving electrons from NADPH via a flavoprotein [ adrenodoxin reductase ( AdRed ) ] and an iron sulfur protein [ adrenodoxin ( Adx ) ] . ^^^ In JEG 3 cells , 8Br cAMP increased and PMA / A23187 slightly decreased the abundance of P450scc and Adx , but neither treatment had a detectable effect on AdRed . ^^^ In Y 1 cells , 8Br cAMP increased the abundance of all three proteins , while PMA / A23187 decreased the abundance of P450scc and Adx . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| We constructed expression vectors for three fusion proteins : NH 2 P450scc AdRed COOH , P 450 AdRed Adx , and P450scc Adx AdRed . ^^^ Triple transfection of three individual vectors expressing P450scc , AdRed , and Adx yielded more pregnenolone than did transfection with P450scc alone . ^^^ The P450scc AdRed and P450scc Adx AdRed fusion proteins produced levels of pregnenolone similar to the control triple transfection . ^^^ However , the P450scc AdRed Adx fusion produced substantially more pregnenolone , having an apparent Vmax of 9 . 1 ng of pregnenolone produced per milliliter of medium per 24 hr , compared to a Vmax of 1 . 7 ng / ml per day for the triple transfection . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| Expression of the electron carrier adrenodoxin ( ADX ) , which is a part of the cytochrome P450scc enzyme system , was very low in nonstimulated cells but was dramatically elevated in FK and 8 Br cAMP stimulated cells , whereas no reduction of ADX was evident in cells costimulated with FK and TPA . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| The activity increased 17 or 25 fold when sonicated mitochondria were supplemented with an excess of purified P450scc or a mixture of adrenodoxin ( Adx ) and adrenodoxin reductase ( AdxRed ) , respectively . ^^^ These data suggest that , at least in yeast mitochondria , the interactions of the catalytic domains of P450scc , Adx , and AdxRed in the common polypeptide chain are restricted . . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| We studied the properties of various fused combinations of the components of the mitochondrial cholesterol side chain cleavage system including cytochrome P450scc , adrenodoxin ( Adx ) , and adrenodoxin reductase ( AdR ) . ^^^ To understand the assembly of the catalytic domains in the fused molecules , we analyzed the catalytic properties of three two component fusions : P450scc Adx , Adx P450scc , and AdR Adx . ^^^ Our data suggest that when fusion proteins containing P450scc , Adx , and AdR undergo protein folding , the corresponding catalytic domains are not formed independently of each other . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| It is able to transfer electrons to horse heart cytochrome c and to bovine cytochromes P 450 ( scc ) ( CYP11A1 ) and P 450 ( 11 beta ) ( CYP11B1 ) , thereby receiving electrons from bovine NADPH dependent Adx reductase . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| Adrenodoxin ( Adx ) , a [ 2Fe 2S ] vertebrate type ferredoxin , transfers electrons from the NADPH dependent flavoprotein Adx reductase ( AdR ) to mitochondrial cytochrome P 450 enzymes of the CYP11A and CYP11B families , which catalyze key reactions in steroid hormone biosynthesis . ^^^ Here , we show for the first time that bovine Adx is a substrate of protein kinase CK 2 , whereas bovine CYP11A1 , CYP11B1 , and AdR are not phosphorylated by this kinase . ^^^ Substrate conversion assays catalyzed by CYP11A1 showed an increase in product formation when Adx T71E or CK 2 phosphorylated Adx were used as electron carrier instead of Adx WT , whereas the activity toward CYP11B1 was not altered using these Adx species . ^^^ Additionally , Adx T71E represents the only full length Adx mutant which leads to an increase in CYP11A1 product formation . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| The present study was undertaken to evaluate the role of positively charged amino acid residues proposed to reside on the proximal surface of bovine cytochrome P 450 cholesterol side chain cleavage ( P450scc , CYP11A1 ) and to determine which residues may be involved in protein protein interactions with the electron carrier adrenodoxin ( Adx ) . ^^^ Independently , a homology model of P450scc was constructed and docked with the structure of Adx . ^^^ Four potential sites of interaction were identified : P450scc : K 403 with Adx : D 76 , P450scc : K 405 with Adx : D 72 ; P450scc : R 426 with Adx : E 73 , and P450scc : K 267 with Adx : E 47 . ^^^ Thus , the biochemical and molecular modeling studies together support the hypothesis that K 267 , K 403 , K 405 , and R 426 participate in the electrostatic interaction of P450scc with Adx . . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| The adrenodoxin ( Adx ) concentration in mitochondria from term placentae is near saturating for P450scc and under these conditions , we found that decreasing AR reduces the K ( m ) of P450scc for adrenodoxin . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| Biosynthesis involves eight mammalian proteins ( mature forms of CYP11A1 , adrenodoxin ( ADX ) , and adrenodoxin reductase ( ADR ) ; mitochondrial forms of ADX and CYP11B1 ; 3beta HSD , CYP17A1 , and CYP21A1 ) . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| Cytochrome P450scc , mitochondrial adrenodoxin ( Adx ) , and adrenodoxin reductase ( AdR ) are an essential components in a steroid hydroxylation system . ^^^ In order to study the effect of single mutations on the Adx binding a model of bovine cytochrome P450scc , previously optimized by molecular modeling , was utilized . ^^^ The apparent dissociation constant values for Asp405Ile and Glu124Ile cytochrome P450scc show that the mutated residues seem to be at the interaction domain with Adx or at least close to it , as predicted by molecular modeling study . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| Adrenodoxin ( Adx ) and CYP11A1 ( P450scc ) induce apoptosis by the generation of reactive oxygen species in mitochondria . ^^^ Mitochondrial cytochrome P 450 systems are an indispensable component of mammalian steroid biosynthesis ; they catalyze regio and stereo specific steroid hydroxylations and consist of three protein entities : adrenodoxin reductase ( AdR ) , adrenodoxin ( Adx ) , and a mitochondrial cytochrome P 450 enzyme , e . g . , CYP11A1 ( P 450 side chain cleavage , P450scc ) . ^^^ |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P10109 and P05108 |
Pubmed |
SVM Score :0.0 |
| NA |
|