Adrenodoxin: An iron-sulfur protein which serves as an electron carrier in enzymatic steroid hydroxylation reactions in adrenal cortex mitochondria. The electron transport system which catalyzes this reaction consists of adrenodoxin reductase, NADP, adrenodoxin, and cytochrome P-450.Ferredoxin-NADP Reductase: An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.Cholesterol Side-Chain Cleavage Enzyme: A mitochondrial cytochrome P450 enzyme that catalyzes the side-chain cleavage of C27 cholesterol to C21 pregnenolone in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP11A1 gene, catalyzes the breakage between C20 and C22 which is the initial and rate-limiting step in the biosynthesis of various gonadal and adrenal steroid hormones.Adrenal Cortex: The outer layer of the adrenal gland. It is derived from MESODERM and comprised of three zones (outer ZONA GLOMERULOSA, middle ZONA FASCICULATA, and inner ZONA RETICULARIS) with each producing various steroids preferentially, such as ALDOSTERONE; HYDROCORTISONE; DEHYDROEPIANDROSTERONE; and ANDROSTENEDIONE. Adrenal cortex function is regulated by pituitary ADRENOCORTICOTROPIN.Steroid 11-beta-Hydroxylase: A mitochondrial cytochrome P450 enzyme that catalyzes the 11-beta-hydroxylation of steroids in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP11B1 gene, is important in the synthesis of CORTICOSTERONE and HYDROCORTISONE. Defects in CYP11B1 cause congenital adrenal hyperplasia (ADRENAL HYPERPLASIA, CONGENITAL).NADH, NADPH Oxidoreductases: A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.Pregnenolone: A 21-carbon steroid, derived from CHOLESTEROL and found in steroid hormone-producing tissues. Pregnenolone is the precursor to GONADAL STEROID HORMONES and the adrenal CORTICOSTEROIDS.Ethyldimethylaminopropyl Carbodiimide: Carbodiimide cross-linking reagent.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Ferredoxins: Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Cytochrome P-450 Enzyme System: A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.Nuclear Physics: The study of the characteristics, behavior, and internal structures of the atomic nucleus and its interactions with other nuclei. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Electron Transport: The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)Polysorbates: Sorbitan mono-9-octadecanoate poly(oxy-1,2-ethanediyl) derivatives; complex mixtures of polyoxyethylene ethers used as emulsifiers or dispersing agents in pharmaceuticals.Steroid Hydroxylases: Cytochrome P-450 monooxygenases (MIXED FUNCTION OXYGENASES) that are important in steroid biosynthesis and metabolism.Mitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)NADP: Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)Cytochrome c Group: A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)CarbodiimidesElectromagnetic Phenomena: Characteristics of ELECTRICITY and magnetism such as charged particles and the properties and behavior of charged particles, and other phenomena related to or associated with electromagnetism.Cholestanetriol 26-Monooxygenase: An NAPH-dependent cytochrome P450 enzyme that catalyzes the oxidation of the side chain of sterol intermediates such as the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol.Kinetics: The rate dynamics in chemical or physical systems.Electron Spin Resonance Spectroscopy: A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.Adrenal Glands: A pair of glands located at the cranial pole of each of the two KIDNEYS. Each adrenal gland is composed of two distinct endocrine tissues with separate embryonic origins, the ADRENAL CORTEX producing STEROIDS and the ADRENAL MEDULLA producing NEUROTRANSMITTERS.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Ferricyanides: Inorganic salts of the hypothetical acid, H3Fe(CN)6.
(1/164) Luteinization and proteolysis in ovarian follicles of Meishan and Large White gilts during the preovulatory period.

This experiment was conducted to determine why follicles luteinize faster in the Meishan breed than in the Large White breed of pig. Follicles were recovered during the late follicular phase from ovaries of both breeds before and after administration of hCG given to mimic the LH surge. First, the patterns of cholesterol transporters (high and low density lipoproteins: HDL and LDL) were compared. Cholesterol transporters detected in follicular fluid consisted of HDL only. Similar amounts of Apolipoprotein A-I were found in all samples. There was no obvious breed effect on minor lipoproteins found in the HDL-rich fraction, and this pattern was altered similarly by hCG in the two breeds. The LDL-rich samples of serum from both breeds contained similar amounts of protein. Second, three steroidogenic enzymes, adrenodoxin, 17 alpha-hydroxylase-lyase (P450(17) alpha) and 3 beta-hydroxysteroid-dehydrogenase (3 beta-HSD) were detected by immunohistochemistry and quantified by image analysis on sections of the two largest follicles. Before hCG treatment, theca interna cells demonstrated immunoreactivities for adrenodoxin (strong), P450(17) alpha and 3 beta-HSD (very strong), whereas granulosa cells displayed immunoreactivities for adrenodoxin only. After hCG treatment, the localization of the enzymes was unchanged but the staining intensity of adrenodoxin on granulosa cells and 3 beta-HSD on theca cells increased (P < 0.01 and P < 0.05, respectively). Breed effects were detected for the amounts of adrenodoxin in theca cells (Meishan > Large White; P < 0.05) and of 17 alpha-hydroxylase (Large White > Meishan, P < 0.01). Breed x treatment interactions were never detected. Finally, gelatinases, plasminogen activator, plasminogen activator inhibitor, tissue inhibitors of metalloproteases (TIMP-1 and TIMP-2) were visualized by direct or reverse zymography or western blotting. Whatever the stage relative to LH administration, follicular fluid from Large White gilts contained more TIMP-1, and TIMP-2 (P < 0.02 and P < 0.01, respectively). No breed effect was detected for the amounts of gelatinases and plasminogen activator inhibitor 1. However, for these parameters, a significant breed x time interaction was obvious, as the Meishan follicles had a greater response to hCG (P < 0.01). Since proteolysis plays a key role in the bioavailability of growth factors such as insulin-like growth factor 1, fibroblast growth factor and transforming growth factor beta, which have the ability to alter gonadotrophin-induced progesterone production in pigs, the differences observed in its control in the present study may explain, at least in part, the different patterns of luteinization observed in Meishan and Large White follicles.  (+info)

(2/164) Enzymatic properties of vesicle-reconstituted human cytochrome P450SCC (CYP11A1) differences in functioning of the mitochondrial electron-transfer chain using human and bovine adrenodoxin and activation by cardiolipin.

The recently reported heterologous expression and purification of both human cytochrome P450SCC and adrenodoxin [Woods, S.T., Sadleir, J., Downs, T., Triantopoulos, T., Haedlam, M.J. & Tuckey, R.C. (1998) Arch. Biochem. Biophys. 353, 109-115] has enabled us to perform studies with the membrane-reconstituted human enzymes to better understand the side-chain cleavage reaction in humans. Human P450SCC was successfully reconstituted into dioleoylphosphatidylcholine vesicles with and without cardiolipin and its enzymatic properties characterized in the membrane-bound state. Enhancement of the P450SCC activity and significant activation by cardiolipin were observed when human adrenodoxin instead of bovine adrenodoxin was used as electron donor. In the absence of cardiolipin, Km for cholesterol was decreased twice in the case of human adrenodoxin indicating enhanced cholesterol binding. On the other hand, in the presence of cardiolipin in the membrane both Km and V for cholesterol were decreased with human adrenodoxin as electron donor. Kinetic analysis of the interaction between human P450SCC and its redox partners provided evidence for enhanced binding of the human electron donor to human P450SCC indicated by both an increased V and decreased Kd for human adrenodoxin compared with the values with bovine adrenodoxin. Because no similar effects were observed in Tween 20 micelles, these results suggest that the phospholipid membrane may play an important role in the interaction of human adrenodoxin with human P450SCC.  (+info)

(3/164) Interaction of CYP11B1 (cytochrome P-45011 beta) with CYP11A1 (cytochrome P-450scc) in COS-1 cells.

The interactions of CYP11B1 (cytochrome P-45011beta), CYP11B2 (cytochrome P-450aldo) and CYP11A1 (cytochrome P-450scc) were investigated by cotransfection of their cDNA into COS-1 cells. The effect of CYP11A1 on CYP11B isozymes was examined by studying the conversion of 11-deoxycorticosterone to corticosterone, 18-hydroxycorticosterone and aldosterone. It was shown that when human or bovine CYP11B1 and CYP11A1 were cotransfected they competed for the reducing equivalents from the limiting source contained in COS-1 cells; this resulted in a decrease of the CYP11B activities without changes in the product formation patterns. The competition of human CYP11A1 with human CYP11B1 and CYP11B2 could be diminished with excess expression of bovine adrenodoxin. However, the coexpression of bovine CYP11B1 and CYP11A1 in the presence of adrenodoxin resulted in a stimulation of 11beta-hydroxylation activity of CYP11B1 and in a decrease of the 18-hydroxycorticosterone and aldosterone formation. These results suggest that the interactions of CYP11A1 with CYP11B1 and CYP11B2 do not have an identical regulatory function in human and in bovine adrenal tissue.  (+info)

(4/164) Modulation of aldosterone biosynthesis by adrenodoxin mutants with different electron transport efficiencies.

Aldosterone biosynthesis is highly regulated on different levels by hormones, potassium, lipid composition of the membrane and the molecular structure of its gene. Here, the influence of the electron transport efficiency from adrenodoxin (Adx) to CYP11B1 on the activities of bovine CYP11B1 has been investigated using a liposomal reconstitution system with truncated mutants of Adx. It could be clearly demonstrated that Adx mutants Adx 4-114 and Adx 4-108, possessing enhanced electron transfer abilities, produce increases in corticosterone and aldosterone biosynthesis. Based on the Vmax values of corticosterone and aldosterone formation, Adx 4-108 and Adx 4-114 enhance corticosterone synthesis 1.3-fold and aldosterone formation threefold and twofold, respectively. The production of 18-hydroxycorticosterone was changed only slightly in these Adx mutants. The effect of Adx 1-108 on the product patterns of bovine CYP11B1, human CYP11B1 and human CYP11B2 was confirmed in COS-1 cells by cotransfection of CYP11B- and Adx-containing expression vectors. It could be shown that Adx 1-108 enhances the formation of aldosterone by bovine CYP11B1 and by human CYP11B2, and stimulates the production of corticosterone by bovine CYP11B1 and human CYP11B1 and CYP11B2 also.  (+info)

(5/164) Enzymatic properties of human 25-hydroxyvitamin D3 1alpha-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli.

We have cloned human 25-hydroxyvitamin D3 1alpha-hydroxylase cDNAs from normal subjects and patients with pseudovitamin D-deficient rickets (PDDR), and expressed the cDNAs in Escherichia coli JM109 cells. Kinetic analysis of normal 1alpha-hydroxylase in the reconstituted system revealed that Km values for 25(OH)D3 and (24R), 25(OH)2D3 were 2.7 and 1.1 microM, respectively. The lower Km value and higher Vmax/Km value for (24R),25(OH)2D3 indicated that it is a better substrate than 25(OH)D3 for 1alpha-hydroxylase. These results are quite similar to those of mouse 1alpha-hydroxylase. To establish a highly sensitive in vivo system, 1alpha-hydroxylase, adrenodoxin and NADPH-adrenodoxin reductase were coexpressed in E. coli cells. The recombinant E. coli cells showed remarkably high 1alpha-hydroxylase activity, suggesting that the electrons were efficiently transferred from NADPH-adrenodoxin reductase through adrenodoxin to 1alpha-hydroxylase in E. coli cells. Using this system, the activities of four mutants of 1alpha-hydroxylase, R107H, G125E, R335P and P382S, derived from patients with PDDR were examined. Although no significant reduction in expression of these mutants was observed, none showed detectable activity. These results strongly suggest that the mutations found in the patients with PDDR completely abolished 1alpha-hydroxylase activity by replacement of one amino acid residue.  (+info)

(6/164) A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins.

Iron-sulfur (Fe/S) cluster-containing proteins catalyze a number of electron transfer and metabolic reactions. The components and molecular mechanisms involved in the assembly of the Fe/S clusters have been identified only partially. In eukaryotes, mitochondria have been proposed to execute a crucial task in the generation of intramitochondrial and extramitochondrial Fe/S proteins. Herein, we identify the essential ferredoxin Yah1p of Saccharomyces cerevisiae mitochondria as a central component of the Fe/S protein biosynthesis machinery. Depletion of Yah1p by regulated gene expression resulted in a 30-fold accumulation of iron within mitochondria, similar to what has been reported for other components involved in Fe/S protein biogenesis. Yah1p was shown to be required for the assembly of Fe/S proteins both inside mitochondria and in the cytosol. Apparently, at least one of the steps of Fe/S cluster biogenesis within mitochondria requires reduction by ferredoxin. Our findings lend support to the idea of a primary function of mitochondria in the biosynthesis of Fe/S proteins outside the organelle. To our knowledge, Yah1p is the first member of the ferredoxin family for which a function in Fe/S cluster formation has been established. A similar role may be predicted for the bacterial homologs that are encoded within iron-sulfur cluster assembly (isc) operons of prokaryotes.  (+info)

(7/164) Construction and characterization of a catalytic fusion protein system: P-450(11beta)-adrenodoxin reductase-adrenodoxin.

Cortisol is an important intermediate for the production of steroidal drugs and can only be synthesized chemically by rather complicated multi-step procedures. The most critical step is the 11beta-hydroxylation of 11-deoxycortisol, which is catalyzed by a mitochondrial enzyme, P-450(11beta). Various fusion constructs of P-450(11beta) with its electron transfer components, adrenodoxin and adrenodoxin reductase, were produced by cDNA manipulation and were successfully expressed in COS-1 cells from which the hydroxylation activities were assayed. It was demonstrated that the fusion protein required both adrenodoxin reductase and adrenodoxin for its activity and was not able to receive electrons from an external source. The fusion protein with all three components had less activity than P-450(11beta) alone, receiving electrons from coexpressed or internal electron transfer components. The activities of the fusion proteins were determined mainly by the fusion sequence. The fusion protein with a sequence of P-450(11beta)-adrenodoxin reductase-adrenodoxin was more active than that of P-450(11beta)-adrenodoxin-adrenodoxin reductase, 1.5- and 3-fold for bovine and human P-450(11beta), respectively. Modification of the linker region by extending the size of the linker with various peptide sequences in the bovine P-450(11beta)-adrenodoxin reductase-adrenodoxin fusion protein indicated that the linker did not have significant effect on the P-450 activity. Taken together, the fusion protein obtained here can serve as a model for the investigation of electron transfer in P-450 systems and is of potential importance for biotechnological steroid production.  (+info)

(8/164) Dual metabolic pathway of 25-hydroxyvitamin D3 catalyzed by human CYP24.

Human 25-hydroxyvitamin D3 (25(OH)D3) 24-hydroxylase (CYP24) cDNA was expressed in Escherichia coli, and its enzymatic and spectral properties were revealed. The reconstituted system containing the membrane fraction prepared from recombinant E. coli cells, adrenodoxin and adrenodoxin reductase was examined for the metabolism of 25(OH)D3, 1alpha,25(OH)2D3 and their related compounds. Human CYP24 demonstrated a remarkable metabolism consisting of both C-23 and C-24 hydroxylation pathways towards both 25(OH)D3 and 1alpha,25(OH)2D3, whereas rat CYP24 showed almost no C-23 hydroxylation pathway [Sakaki, T. Sawada, N. Nonaka, Y. Ohyama, Y. & Inouye, K. (1999) Eur. J. Biochem. 262, 43-48]. HPLC analysis and mass spectrometric analysis revealed that human CYP24 catalyzed all the steps of the C-23 hydroxylation pathway from 25(OH)D3 via 23S, 25(OH)2D3, 23S,25,26(OH)3D3 and 25(OH)D3-26,23-lactol to 25(OH)D3-26, 23-lactone in addition to the C-24 hydroxylation pathway from 25(OH)D3 via 24R,25(OH)2D3, 24-oxo-25(OH)D3, 24-oxo-23S,25(OH)2D3 to 24,25,26,27-tetranor-23(OH)D3. On 1alpha,25(OH)2D3 metabolism, similar results were observed. These results strongly suggest that the single enzyme human CYP24 is greatly responsible for the metabolism of both 25(OH)D3 and 1alpha,25(OH)2D3. We also succeeded in the coexpression of CYP24, adrenodoxin and NADPH-adrenodoxin reductase in E. coli. Addition of 25(OH)D3 to the recombinant E. coli cell culture yielded most of the metabolites in both the C-23 and C-24 hydroxylation pathways. Thus, the E. coli expression system for human CYP24 appears quite useful in predicting the metabolism of vitamin D analogs used as drugs.  (+info)

*  Adrenodoxin reductase
... (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine ... Müller JJ, Lapko A, Bourenkov G, Ruckpaul K, Heinemann U (Jan 2001). "Adrenodoxin reductase-adrenodoxin complex structure ... It catalyzes the following reaction: NADPH + 2 oxidized adrenodoxin -→ 2 reduced adrenodoxin + NADP+ + H+ The cDNA for ... Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ...
*  Adrenodoxin-NADP+ reductase
... (EC 1.18.1.6, adrenodoxin reductase, nicotinamide adenine dinucleotide phosphate-adrenodoxin ... Hanukoglu, I.; Hanukoglu, Z. (1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ... 2 oxidized adrenodoxin + NADPH + H+ Adrenodoxin-NADP+ reductase is a flavoprotein (FAD). Omura, T.; Sanders, E.; Estabrook, R.W ... Adrenodoxin-NADP reductase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...
*  Rossmann fold
Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous ... Phylogenetic analysis of the NADP binding enzyme adrenodoxin reductase revealed that from prokaryotes, through metazoa and up ... Hanukoglu I, Gutfinger T (March 1989). "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in ...
*  Adrenal ferredoxin
... (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that ... adrenodoxin to 11q22; adrenodoxin reductase to 17q24-q25; and P450c17 to 10q24-q25". DNA Cell Biol. 10 (5): 359-65. doi:10.1089 ... 1988). "Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells". J. Biol. Chem. 263 (7): 3240-4 ... 2000). "Adrenodoxin: structure, stability, and electron transfer properties". Proteins. 40 (4): 590-612. doi:10.1002/1097-0134( ...
*  Israel Hanukoglu
Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ... "Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) ... His lab was the first to clone the cDNAs and the gene coding for adrenodoxin reductase - the first enzyme in the electron ... Cholesterol and adrenodoxin interactions at equilibrium and during turnover". The Journal of Biological Chemistry. 256 (9): ...
*  Ferredoxin
Adrenodoxin (adrenal ferredoxin) is expressed in mammals including humans. The human variant of adrenodoxin is referred to as ... In mitochondrial monooxygenase systems, adrenodoxin transfers an electron from NADPH:adrenodoxin reductase to membrane-bound ... It also transfers electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450. FDX-1 has the ... Despite low sequence similarity between adrenodoxin-type and plant-type ferredoxins, the two classes have a similar folding ...
*  Nicotinamide adenine dinucleotide phosphate
Adrenodoxin reductase: This enzyme is present ubiquitously in most organisms. It transfers two electrons from NADPH to FAD. In ... Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous ...
*  Cytochrome c
Geren LM, Millett F (Oct 1981). "Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c ...
*  Cholesterol side-chain cleavage enzyme
In the adrenal cortex, the concentration of adrenodoxin is similar to that of P450scc, but adrenodoxin reductase is expressed ... The electrons are transferred from NADPH to P450scc via two electron transfer proteins: adrenodoxin reductase and adrenodoxin. ... P450scc is associated with the inner mitochondrial membrane, facing the interior (matrix). Adrenodoxin and adrenodoxin ... Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ...
*  Corpus luteum
The mitochondrial P450 system electron transport chain including adrenodoxin reductase and adrenodoxin has been shown to leak ... "Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) ... plasma levels of progesterone increase in parallel to the levels of P450scc and its electron donor adrenodoxin, indicating that ...
*  Peripheral membrane protein
They include cytochrome c, cupredoxins, high potential iron protein, adrenodoxin reductase, some flavoproteins, and others. ...
*  Cytochrome P450
... which employ adrenodoxin reductase and adrenodoxin to transfer electrons from NADPH to P450. Bacterial P450 systems, which ...
*  Flavin adenine dinucleotide
The reductase of the mitochondrial P450 systems Adrenodoxin reductase contains FAD that is embedded in the FAD-binding domain ... Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous ...
*  Aldosterone
They are located within the mitochondria and require adrenodoxin as a cofactor (except 21-hydroxylase and 17α-hydroxylase). ...
*  P450-containing systems
In mitochondrial monooxygenase systems, adrenodoxin functions as a soluble electron carrier between NADPH:adrenodoxin reductase ... The general scheme of electron flow in the P450 systems containing adrenodoxin-type ferredoxins is: Eukaryotic microsomal P450 ...
*  Adrenocortical hormone
A coenzyme system called adrenodoxin reductase transfers electrons to the P450 enzyme which initiates the oxidation-reduction ...
*  Index of biochemistry articles
... adrenodoxin - aequorin - aerobic respiration - agonist - alanine - albumin - alcohol - alcoholic fermentation - alicyclic ...
*  ADR
... a surgical procedure Adrenodoxin-NADP+ reductase, an enzyme ADR (treaty), a treaty governing transport of hazardous materials ...
*  List of MeSH codes (D12.776)
... adrenodoxin MeSH D12.776.556.579.374.375.150 - ferredoxin-nitrite reductase MeSH D12.776.556.579.374.375.275 - ferredoxins MeSH ...
*  Inner mitochondrial membrane
HtrA serine peptidase 2 Adrenodoxin reductase Heme biosynthesis Protoporphyrinogen oxidase Ferrochelatase Uncoupling protein ...
*  Steroid 11β-hydroxylase
... adrenodoxin reductase and adrenodoxin that transfer 2 electrons from NADPH to the P450 for each monooxygenase reaction ...
*  25-Hydroxyvitamin D3 1-alpha-hydroxylase
2 reduced adrenodoxin + 2 H+ + O2 ⇌ {\displaystyle \rightleftharpoons } calcitriol + 2 oxidized adrenodoxin + H2O Calcidiol ...
*  Ferredoxin-NADP(+) reductase
Other names in common use include: adrenodoxin reductase, ferredoxin-NADP+ reductase, ferredoxin-NADP+ oxidoreductase, ... reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin, reductase, and TPNH-ferredoxin reductase During photosynthesis ...
*  List of EC numbers (EC 1)
... adrenodoxin-NADP+ reductase EC 1.18.2.1: now EC 1.18.6.1 EC 1.18.3.1: now EC 1.18.99.1 EC 1.18.6.1: nitrogenase EC 1.18.96.1: ...
Recombinant Human Adrenodoxin protein (ab87670) Protocols  Recombinant Human Adrenodoxin protein (ab87670) Protocols
There are no specific protocols for Recombinant Human Adrenodoxin protein (ab87670). Please download our general protocols ...
more infohttp://www.abcam.com/recombinant-human-adrenodoxin-protein-ab87670-protocols.html
Polycistronic expression of mitochondrial steroidogenic P450scc system in the HEK293T cell line - статья  | ИСТИНА -...  Polycistronic expression of mitochondrial steroidogenic P450scc system in the HEK293T cell line - статья | ИСТИНА -...
Аннотация: Abstract The cholesterol hydroxylase/lyase (CHL) system, which consists of cytochrome P450scc, adrenodoxin (Adx) and ... Abstract The cholesterol hydroxylase/lyase (CHL) system, which consists of cytochrome P450scc, adrenodoxin (Adx) and ... adrenodoxin reductase (AdR), initiates mammalian steroidogenesis, converting cholesterol to pregnenolone. The FMDV 2A-based ... adrenodoxin reductase (AdR), initiates mammalian steroidogenesis, converting cholesterol to pregnenolone. The FMDV 2A-based ...
more infohttps://istina.msu.ru/publications/article/140605694/
adrenodoxin (human)  adrenodoxin (human)
The 'lollipop plot' above illustrates recurrent (observed in 3 or more out of 4440 TCGA tumor samples from 15 cancer types) and therefore potentially oncogenic missense mutations (click on 'Show Cancer Mutations'). The bar plot below shows the proportion of tumor samples that have any kind of altering mutation(s) in the given protein. ...
more infohttps://www.phosphosite.org/proteinAction.action?id=7398&showAllSites=true
Fdx1 - Adrenodoxin, mitochondrial precursor - Mus musculus (Mouse) - Fdx1 gene & protein  Fdx1 - Adrenodoxin, mitochondrial precursor - Mus musculus (Mouse) - Fdx1 gene & protein
Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage. ... Does not form a ternary complex with adrenodoxin reductase and CYP11A1 but shuttles between the two enzymes to transfer ... IPR001055 Adrenodoxin. IPR018298 Adrenodoxin_Fe-S_BS. IPR012675 Beta-grasp_dom_sf. ... IPR001055 Adrenodoxin. IPR018298 Adrenodoxin_Fe-S_BS. IPR012675 Beta-grasp_dom_sf. ...
more infohttps://www.uniprot.org/uniprot/P46656
RCSB PDB 









- 1L6V: STRUCTURE OF REDUCED BOVINE ADRENODOXIN Literature Report Page  RCSB PDB - 1L6V: STRUCTURE OF REDUCED BOVINE ADRENODOXIN Literature Report Page
... transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin. ... Adrenodoxin 1 A 128 Bos taurus Gene Name(s): FDX1 Gene View ADX ... STRUCTURE OF REDUCED BOVINE ADRENODOXIN. *DOI: 10.2210/pdb1l6v/ ...
more infohttp://www.rcsb.org/pdb/explore/litView.do?structureId=1L6V
Adrenodoxin reductase - Wikipedia  Adrenodoxin reductase - Wikipedia
Adrenodoxin reductase (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine ... Müller JJ, Lapko A, Bourenkov G, Ruckpaul K, Heinemann U (Jan 2001). "Adrenodoxin reductase-adrenodoxin complex structure ... It catalyzes the following reaction: NADPH + 2 oxidized adrenodoxin -→ 2 reduced adrenodoxin + NADP+ + H+ The cDNA for ... Hanukoglu I, Hanukoglu Z (May 1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ...
more infohttps://en.wikipedia.org/wiki/Adrenodoxin_reductase
Adrenodoxin-NADP+ reductase - Wikipedia  Adrenodoxin-NADP+ reductase - Wikipedia
Adrenodoxin-NADP+ reductase (EC 1.18.1.6, adrenodoxin reductase, nicotinamide adenine dinucleotide phosphate-adrenodoxin ... Hanukoglu, I.; Hanukoglu, Z. (1986). "Stoichiometry of mitochondrial cytochromes P-450, adrenodoxin and adrenodoxin reductase ... 2 oxidized adrenodoxin + NADPH + H+ Adrenodoxin-NADP+ reductase is a flavoprotein (FAD). Omura, T.; Sanders, E.; Estabrook, R.W ... Adrenodoxin-NADP reductase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular ...
more infohttps://en.wikipedia.org/wiki/Adrenodoxin-NADP+_reductase
RCSB PDB 









- 1E1M: ADRENODOXIN REDUCTASE in complex with NADPH obtained by a soaking experiment Methods Report Page  RCSB PDB - 1E1M: ADRENODOXIN REDUCTASE in complex with NADPH obtained by a soaking experiment Methods Report Page
Crystal Structures of Adrenodoxin Reductase in Complex with Nadp+ and Nadph Suggesting a Mechanism for the Electron Transfer of ...
more infohttp://www.rcsb.org/pdb/explore/materialsAndMethods.do?structureId=1E1M
Nitroreductase reactions of the NADPH: adrenodoxin reductase a...  Nitroreductase reactions of the NADPH: adrenodoxin reductase a...
... adrenodoxin reductase (E.C. 1.18.1.2) and its complex with adr ... NADPH: adrenodoxin reductase (E.C. 1.18.1.2) and its complex ... Nitroreductase reactions of the NADPH: adrenodoxin reductase and the adrenodoxin complex.. Authors * Marcinkeviciene, J ... The reactivity of adrenodoxin reductase is two orders of magnitude lower than that of adrenodoxin. ... The rate constants of adrenodoxin oxidation by nitrocompounds vary from 4 x 10(5) to 3 x 10(2) M-1 s-1. A linear correlation ...
more infohttps://www.mysciencework.com/publication/show/nitroreductase-reactions-nadph-adrenodoxin-reductase-adrenodoxin-complex-e1ab1d04
Adrenodoxin, mitochondrial  Adrenodoxin, mitochondrial
Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage. ... Results present the crystal structure of the complex of human adrenodoxin and CYP11A1--the first of a complex between a ...
more infohttps://pharos.nih.gov/idg/targets/P10109
Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis  - MDC Repository  Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis - MDC Repository
Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis ... Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis. ... Adrenodoxin, Binding Sites, Electron Transport, Electrostatics, Ferredoxin-NADP Reductase, Flavin-Adenine Dinucleotide, ... The steroid hydroxylating system of adrenal cortex mitochondria consists of the membrane-attached NADPH-dependent adrenodoxin ...
more infohttp://edoc.mdc-berlin.de/4746/
C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function...  C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function...
... was accelerated up to 4.5-fold by the adrenodoxin mutants. The results suggest that the C-terminal peptide of adrenodoxin, ... The role of the C-terminal region of adrenodoxin was studied by analyzing deletion mutants 4-114 and 4-108 lacking amino acids ... Absorption spectra of these mutants were found to be identical to that of wild type adrenodoxin. However, EPR and CD studies ... Adrenal Glands, Adrenodoxin, Affinity Chromatography, Base Sequence, Circular Dichroism, Cytochrome P-450 Enzyme System, DNA ...
more infohttp://edoc.mdc-berlin.de/1477/
1cje - Proteopedia, life in 3D  1cje - Proteopedia, life in 3D
Transfers electrons from adrenodoxin reductase to cytochrome P450 cholesterol side-chain cleavage enzyme. reductase to the ... The three-dimensional X-ray crystal structure of full-length oxidized bovine adrenodoxin (Adx) has been determined at 2.5 A ... The tertiary structure of full-length bovine adrenodoxin suggests functional dimers.,Pikuleva IA, Tesh K, Waterman MR, Kim Y ... Pikuleva IA, Tesh K, Waterman MR, Kim Y. The tertiary structure of full-length bovine adrenodoxin suggests functional dimers. ...
more infohttp://proteopedia.org/wiki/index.php/1cje
Nicotinamide adenine dinucleotide phosphate - Wikipedia  Nicotinamide adenine dinucleotide phosphate - Wikipedia
Adrenodoxin reductase: This enzyme is present ubiquitously in most organisms.[5] It transfers two electrons from NADPH to FAD. ... Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous ...
more infohttps://en.wikipedia.org/wiki/NADP+
KAKEN - Research Projects | Studies on the Reaction Mechanisms of Flavoenzymes by Multi-Nuclear NMR (KAKENHI-PROJECT-01480525)  KAKEN - Research Projects | Studies on the Reaction Mechanisms of Flavoenzymes by Multi-Nuclear NMR (KAKENHI-PROJECT-01480525)
Publications] 山野俊雄: 'Rate enhancement of the electron transfer of the adrenodoxin-adrenodoxin reductase system by inorganic and ... Publications] 山野俊雄: 'Rate enhancement of the electron transfer of the adrenodoxin-adrenodoxin reductase system by dicarboxylic ... Publications] Toshio Yamano: 'Rate enhancement of the electron transfer of the adrenodoxin-adrenodoxin reductase system by ... Publications] Toshio Yamano: 'Rate enhancement of the electron transfer of the adrenodoxin-adrenodoxin reductase system by ...
more infohttps://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-01480525/
Beta-grasp domain superfamily (IPR012675) | InterPro | EMBL-EBI  Beta-grasp domain superfamily (IPR012675) | InterPro | EMBL-EBI
... including putidaredoxin and adrenodoxin) [PMID: 15755454], the 2Fe-2S ferredoxin-related family (including aldehyde reductase, ...
more infohttp://www.ebi.ac.uk/interpro/entry/IPR012675
New Arabidopsis DNA 08-Aug-1998  New Arabidopsis DNA 08-Aug-1998
... adrenodoxin - like protein; F7J7.40; UV-damaged DNA-binding protein- like; F7J7.50; G10 - like protein; F7J7.60; amino acid ...
more infohttp://www.bio.net/bionet/mm/arab-gen/1998-August/006547.html
Journal of Basic and Clinical Physiology and Pharmacology  Journal of Basic and Clinical Physiology and Pharmacology
Structure and function of the mitochondrial P450 system electron transfer proteins, adrenodoxin reductase and adrenodoxin. ...
more infohttps://www.degruyter.com/view/j/jbcpp.1992.3.s1/issue-files/jbcpp.1992.3.s1.xml
  • However, EPR and CD studies indicated that the structure of deletion mutants 4-114 and 4-108 differs from that of wild type adrenodoxin. (mdc-berlin.de)