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Protein found in humans
Adrenodoxin reductase (Enzyme Nomenclature name: adrenodoxin-NADP+ reductase, EC 1.18.1.6), was first isolated from bovine adrenal cortex where it functions
Adrenodoxin_reductase
Enzyme
Adrenodoxin-NADP+ reductase (EC 1.18.1.6, adrenodoxin reductase, nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase, ADR, NADPH:adrenal
Adrenodoxin-NADP+_reductase
Class of enzymes
adrenodoxin reductase, ferredoxin-NADP+ reductase, ferredoxin-NADP+ oxidoreductase, ferredoxin-nicotinamide adenine dinucleotide phosphate reductase,
Ferredoxin—NADP(+)_reductase
Mammalian protein found in humans
the adrenal cortex, the concentration of adrenodoxin is similar to that of P450scc, but adrenodoxin reductase is expressed at lower levels. Immunofluorescence
Cholesterol side-chain cleavage enzyme
Cholesterol_side-chain_cleavage_enzyme
Coenzyme acting as an electron carrier in biochemical redox reactions
of NADP. Therefore, it is also called an "ADP-binding βαβ fold". Adrenodoxin reductase: This enzyme is present ubiquitously in most organisms. It transfers
Nicotinamide adenine dinucleotide phosphate
Nicotinamide_adenine_dinucleotide_phosphate
Redox-active coenzyme
proteins: An FAD containing adrenodoxin reductase (AR) and a small iron-sulfur group containing protein named adrenodoxin. FAD is embedded in the FAD-binding
Flavin_adenine_dinucleotide
Temporary endocrine structure in ovaries
mitochondrial P450 system electron transport chain including adrenodoxin reductase and adrenodoxin has been shown to leak electrons leading to the formation
Corpus_luteum
Mammalian protein found in Homo sapiens
mitochondrial cytochrome P450 systems. The first enzyme in this system is adrenodoxin reductase that carries an FAD. FAD can be reduced by two electrons donated
Adrenal_ferredoxin
Iron–sulfur proteins that mediate electron transfer in metabolic reactions
monooxygenase systems, adrenodoxin transfers an electron from NADPH:adrenodoxin reductase to membrane-bound cytochrome P450. In bacteria, putidaredoxin and
Ferredoxin
Protein fold
integrated into ECOD. Phylogenetic analysis of the NADP binding enzyme adrenodoxin reductase revealed that from prokaryotes, through metazoa and up to primates
Rossmann_fold
Israeli biochemist
His lab was the first to clone the cDNAs and the gene coding for adrenodoxin reductase - the first enzyme in the electron transfer chain of the mitochondrial
Israel_Hanukoglu
Protein family
or as a cofactor. The flavin is generally tightly bound (as in adrenodoxin reductase, wherein the FAD is buried deeply). About 5-10% of flavoproteins
Flavoprotein
Class of enzymes
camphor-related substrates. Mitochondrial P450 systems which employ adrenodoxin reductase and adrenodoxin (a ferrodoxin) to transfer electrons from NADPH to P450
Cytochrome_P450
ferredoxin reductase (FR) and P450. In mitochondrial monooxygenase systems, adrenodoxin functions as a soluble electron carrier between NADPH:adrenodoxin reductase
P450-containing_systems
Cell structure
dehydrogenase Thymidylate synthase (FAD) HtrA serine peptidase 2 Adrenodoxin reductase Heme biosynthesis Protoporphyrinogen oxidase Ferrochelatase Uncoupling
Inner_mitochondrial_membrane
Highly reactive molecules formed from diatomic oxygen (O2)
(September 1993). "Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) system". Archives
Reactive_oxygen_species
Chemical compound
The reaction requires electron transfer from NADPH via adrenodoxin reductase and adrenodoxin, similar to other P450 systems. In adrenal tissue, testosterone
11β-Hydroxytestosterone
Hormones produced by the adrenal cortex
the family of cytochrome P450 enzymes. A coenzyme system called adrenodoxin reductase transfers electrons to the P450 enzyme which initiates the oxidation-reduction
Adrenocortical_hormone
Mammalian protein found in humans
25-hydroxyvitamin D3 1alpha-hydroxylase coexpression with adrenodoxin and NADPH-adrenodoxin reductase in Escherichia coli". European Journal of Biochemistry
25-Hydroxyvitamin D 1-alpha-hydroxylase
25-Hydroxyvitamin_D_1-alpha-hydroxylase
Non-protein chemical compound or metallic ion
"Conservation of the Enzyme–Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme". Journal of Molecular Evolution. 85 (5–6):
Cofactor_(biochemistry)
Physical interactions and constructions between multiple proteins
adrenodoxin to its reductase were identified as two basic Arg residues on the surface of the reductase and two acidic Asp residues on the adrenodoxin
Protein–protein_interaction
Membrane proteins that adhere temporarily to membranes with which they are associated
include cytochrome c, cupredoxins, high potential iron protein, adrenodoxin reductase, some flavoproteins, and others.[citation needed] Many hormones
Peripheral_membrane_protein
Group of cytochrome P450 enzymes
and absolute dependence on mitochondrial electron donors adrenodoxin reductase and adrenodoxin. Rabbit gene CYP8B1 was named CYP12 at the beginning of
CYP12_family
Protein found in mammals
P450c11 is dependent on two electron transfer proteins, adrenodoxin reductase and adrenodoxin that transfer 2 electrons from NADPH to the P450 for each
Steroid_11β-hydroxylase
Topics referred to by the same term
lodging industry statistic Adiabatic demagnetization refrigeration Adrenodoxin-NADP+ reductase, an enzyme Adverse drug reaction Artificial disc replacement
ADR
1.18.1.5: Putidaredoxin—NAD+ reductase EC 1.18.1.6: adrenodoxin-NADP+ reductase EC 1.18.1.7: ferredoxin—NAD(P)+ reductase (naphthalene dioxygenase ferredoxin-specific)
List_of_EC_numbers_(EC_1)
Polycyclic organic compound having sterane as a core structure
"Mitochondrial cytochrome P-450scc. Mechanism of electron transport by adrenodoxin". J Biol Chem. 255 (7): 3057–61. doi:10.1016/S0021-9258(19)85851-9. PMID 6766943
Steroid
Protein found in humans
respiration. It transfers electrons between Complexes III (Coenzyme Q – Cyt c reductase) and IV (Cyt c oxidase). Cytochrome c is highly water-soluble, unlike
Cytochrome_c
Protein-coding gene in the species Homo sapiens
follows: all-trans-retinol + 2 reduced adrenodoxin + 2 H+ + O2 = all-trans-3,4-didehydroretinol + 2 oxidized adrenodoxin + 2 H2O. The initial substrate for
CYP27C1
proteins MeSH D12.776.556.579.374.375.025 – adrenodoxin MeSH D12.776.556.579.374.375.150 – ferredoxin-nitrite reductase MeSH D12.776.556.579.374.375.275 – ferredoxins
List_of_MeSH_codes_(D12.776)
proteins MeSH D12.776.157.427.374.375.025 – adrenodoxin MeSH D12.776.157.427.374.375.150 – ferredoxin-nitrite reductase MeSH D12.776.157.427.374.375.275 – ferredoxins
List of MeSH codes (D12.776.157)
List_of_MeSH_codes_(D12.776.157)
ADRENODOXIN REDUCTASE
ADRENODOXIN REDUCTASE
ADRENODOXIN REDUCTASE
ADRENODOXIN REDUCTASE
ADRENODOXIN REDUCTASE
ADRENODOXIN REDUCTASE
ADRENODOXIN REDUCTASE
ADRENODOXIN REDUCTASE
ADRENODOXIN REDUCTASE