adrenodoxin

アドレノドキシン

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/30 09:10:10」(JST)

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Ferredoxin 1
PDB rendering based on 1ayf.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3N9Y, 3N9Z, 3NA0, 3NA1, 3P1M
Identifiers
Symbols	FDX1 ; ADX; FDX; LOH11CR1D
External IDs	OMIM: 103260 MGI: 103224 HomoloGene: 31216 GeneCards: FDX1 Gene
Gene ontology Molecular function • iron ion binding • electron carrier activity • 2 iron, 2 sulfur cluster binding Cellular component • mitochondrion • mitochondrial matrix Biological process • steroid biosynthetic process • cholesterol metabolic process • hormone biosynthetic process • small molecule metabolic process • oxidation-reduction process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2230	14148
Ensembl	ENSG00000137714	ENSMUSG00000032051
UniProt	P10109	P46656
RefSeq (mRNA)	NM_004109	NM_007996
RefSeq (protein)	NP_004100	NP_032022
Location (UCSC)	Chr 11: 110.3 – 110.34 Mb	Chr 9: 51.94 – 51.96 Mb
PubMed search	[1]	[2]

Adrenal ferredoxin also known as adrenodoxin or adrenodoxin, mitochondrial or hepatoredoxin or ferredoxin-1 (FDX1) is a protein that in humans is encoded by the FDX1 gene. In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.

Function

Ferredoxin-1 is a small iron-sulfur protein that transfers electrons from NADPH through ferredoxin reductase to a terminal cytochrome P450. This particular oxidation/reduction system is found in steroidogenic tissues, and is involved with the synthesis of bile acid and vitamin D. Ferredoxin-1 has been identified in a number of different tissues but all forms have been shown to be identical and are not tissue specific.

References

Further reading

• Grinberg AV, Hannemann F, Schiffler B et al. (2000). "Adrenodoxin: structure, stability, and electron transfer properties". Proteins 40 (4): 590–612. doi:10.1002/1097-0134(20000901)40:4<590::AID-PROT50>3.0.CO;2-P. PMID 10899784. 
• Wada A, Waterman MR (1992). "Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding". J. Biol. Chem. 267 (32): 22877–82. PMID 1429635. 
• Sparkes RS, Klisak I, Miller WL (1991). "Regional mapping of genes encoding human steroidogenic enzymes: P450scc to 15q23-q24, adrenodoxin to 11q22; adrenodoxin reductase to 17q24-q25; and P450c17 to 10q24-q25". DNA Cell Biol. 10 (5): 359–65. doi:10.1089/dna.1991.10.359. PMID 1863359. 
• Skjeldal L, Markley JL, Coghlan VM, Vickery LE (1991). "1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins". Biochemistry 30 (37): 9078–83. doi:10.1021/bi00101a024. PMID 1909889. 
• Coghlan VM, Vickery LE (1991). "Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc". J. Biol. Chem. 266 (28): 18606–12. PMID 1917982. 
• Chang CY, Wu DA, Mohandas TK, Chung BC (1990). "Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family". DNA Cell Biol. 9 (3): 205–12. doi:10.1089/dna.1990.9.205. PMID 2340092. 
• Chang CY, Wu DA, Lai CC et al. (1989). "Cloning and structure of the human adrenodoxin gene". DNA 7 (9): 609–15. doi:10.1089/dna.1988.7.609. PMID 3229285. 
• Voutilainen R, Picado-Leonard J, DiBlasio AM, Miller WL (1988). "Hormonal and developmental regulation of adrenodoxin messenger ribonucleic acid in steroidogenic tissues". J. Clin. Endocrinol. Metab. 66 (2): 383–8. doi:10.1210/jcem-66-2-383. PMID 3339111. 
• Picado-Leonard J, Voutilainen R, Kao LC et al. (1988). "Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells". J. Biol. Chem. 263 (7): 3240–4. PMID 3343244. 
• Martsev SP, Chashchin VL, Akhrem AA (1985). "[Reconstruction and study of a multi-enzyme system by 11 beta-hydroxylase steroids]". Biokhimiia 50 (2): 243–57. PMID 3872685. 
• Geren LM, Millett F (1981). "Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c". J. Biol. Chem. 256 (20): 10485–9. PMID 6270113. 
• Pikuleva IA, Cao C, Waterman MR (1999). "An additional electrostatic interaction between adrenodoxin and P450c27 (CYP27A1) results in tighter binding than between adrenodoxin and p450scc (CYP11A1)". J. Biol. Chem. 274 (4): 2045–52. doi:10.1074/jbc.274.4.2045. PMID 9890963. 
• Kostic M, Pochapsky SS, Obenauer J et al. (2002). "Comparison of functional domains in vertebrate-type ferredoxins". Biochemistry 41 (19): 5978–89. doi:10.1021/bi0200256. PMID 11993992. 
• Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
• Johnson D, Norman S, Tuckey RC, Martin LL (2004). "Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode". Bioelectrochemistry (Amsterdam, Netherlands) 59 (1–2): 41–7. doi:10.1016/s1567-5394(02)00188-3. PMID 12699818. 
• Araya Z, Hosseinpour F, Bodin K, Wikvall K (2003). "Metabolism of 25-hydroxyvitamin D3 by microsomal and mitochondrial vitamin D3 25-hydroxylases (CYP2D25 and CYP27A1): a novel reaction by CYP27A1". Biochim. Biophys. Acta 1632 (1–3): 40–7. doi:10.1016/S1388-1981(03)00062-3. PMID 12782149. 
• Gerhard DS, Wagner L, Feingold EA et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. 
• Derouet-Hümbert E, Roemer K, Bureik M (2005). "Adrenodoxin (Adx) and CYP11A1 (P450scc) induce apoptosis by the generation of reactive oxygen species in mitochondria". Biol. Chem. 386 (5): 453–61. doi:10.1515/BC.2005.054. PMID 15927889. 

UpToDate Contents

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• 1. 副腎ステロイド生合成 adrenal steroid biosynthesis

English Journal

• The cytochrome P450 24A1 interaction with adrenodoxin relies on multiple recognition sites that vary among species.

• Estrada DF1.
• The Journal of biological chemistry.J Biol Chem.2018 Mar 16;293(11):4167-4179. doi: 10.1074/jbc.RA117.001145. Epub 2018 Jan 25.
• PMID 29371396

• [Study specificity of isatin interactions with P450 cytochromes].

• Ershov PV1, Mezentsev YV1, Yablokov EO1, Kalushskiy LA1, Florinskaya AV1, Svirid AV2, Gilep AA2, Usanov SA2, Medvedev AE1, Ivanov AS1.
• Biomeditsinskaia khimiia.Biomed Khim.2018 Jan;64(1):61-65. doi: 10.18097/PBMC20186401061.
• PMID 29460836

• Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme.

• Hanukoglu I1.
• Journal of molecular evolution.J Mol Evol.2017 Dec;85(5-6):205-218. doi: 10.1007/s00239-017-9821-9. Epub 2017 Nov 24.
• PMID 29177972

Japanese Journal

• Replacement of Alanine with Asparagic Acid at Position 203 in Human Steroidogenic Acute Regulatory Protein Impairs the Ability to Enhance Steroidogenesis in vitro

• KATSUMATA Noriyuki,HORIKAWA Reiko,TANAKA Toshiaki
• Endocrine Journal 53(3), 427-431, 2006
• … The A203 StAR caused a twelve-fold increase in pregnenolone secretion over COS-1 cells transfected with an NH2-cholesterol side-chain cleavage enzyme (P450scc)-adrenodoxin reductase-adrenodoxin-COOH fusion protein expressing plasmid (F2) and an empty vector, whereas the D203 StAR increased pregnenolone production no more than threefold. …
• NAID 130004443241

• 副腎皮質ミトコンドリアにおけるチオレドキシン・ペルオキシダーゼ酵素系

• 渡部 省二
• 山口医学 51(2), 29-38, 2002-04-30
• … Adrenocortical mitochondria contain several hydroxylases for steroids and an electron-donating system for them (adrnodoxin and adrenodoxin reductase). …
• NAID 110002774216

• Adrenodoxin-Cytochrome P45Oscc Interaction as Revealed by EPR Spectroscopy : Comparison with the Putidaredoxin-Cytochrome P45Ocam System

• Takeuchi Kohji,Tsubaki Motonari,Futagawa Junya [他],MASUYA Futoshi,HORI Hiroshi
• The journal of biochemistry 130(6), 789-797, 2001-12-01
• NAID 10007860238

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リンク元	「アドレノドキシン」
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adrenodoxin

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フェレドキシン

「NADPH-adrenodoxin reductase」

　　[★] フェレドキシン-NADP+還元酵素。NADPH-アドレノドキシン還元酵素