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Chemical Compound Review

ADP     [[(2R,3S,4R,5R)-5-(6- aminopurin-9-yl)-3,4...

Synonyms: a-ADP, H3adp, CHEMBL14830, AG-J-06224, CHEBI:16761, ...
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Disease relevance of Adenosine diphosphate

  • Human choroideremia protein contains a FAD-binding domain [1].
  • Human glutathione reductase serves as a reference molecule for FAD-dependent disulphide reductases and between its primary structure and that of MerA from Tn501 (Pseudomonas), Tn21 (Shigella), p1258 (Staphylococcus) and Bacillus, 25-30% of the residues have been conserved [2].
  • A novel FAD-binding domain, BLUF, exemplified by the N-terminus of the AppA protein from Rhodobacter sphaeroides, is present in various proteins, primarily from Bacteria [3].
  • In Escherichia coli photolyase, excitation of the FAD cofactor in its semireduced radical state (FADH*) induces an electron transfer over approximately 15 A from tryptophan W306 to the flavin [4].
  • Whereas 40% of the amino acid residues overall were identical between the pI258 merA polypeptide product and mercuric reductases from Gram-negative bacteria, the percentage identity in the active-site positions and those thought to be involved in NADPH and FAD contacts was above 90% [5].

Psychiatry related information on Adenosine diphosphate

  • Genetic linkage studies suggest that Alzheimer's disease is not a single homogeneous disorder. FAD Collaborative Study Group [6].
  • Lifetime risk of dementia in early-onset FAD kindreds is consistent with an autosomal dominant inheritance model [7].
  • The roles of the FAD 2'-OH group and the FAD N(5)-Arg431 hydrogen bond pair in regulating redox-dependent PutA-membrane associations were tested using FAD analogues and site-directed mutagenesis [8].
  • Competitive behavior is observed in reconstitution reactions containing both FAD and 8-(methylsulfonyl)FAD [9].
  • Univariate analysis showed that family dysfunction measured on the FAD is associated with thinking and planning suicide, deliberate self harm, suicide attempts, as well as severe depression (BDI > or = 22) [10].

High impact information on Adenosine diphosphate

  • The new work clarifies the molecular function of Mia40 and reveals Mia40 to be the first physiological substrate for the FAD-linked Erv1 [11].
  • Genetic map positions were recently reported for two more FA genes, FAA (16q24.3) and FAD (3p22-26) [12].
  • The only specific molecular defects that cause Alzheimer's disease which have been identified so far are missense mutations in the gene encoding the beta-amyloid precursor protein (beta-APP) in certain families with an autosomal dominant form of the disease (familial Alzheimer's disease, or FAD) [13].
  • These data establish a direct link between a FAD genotype and the clinicopathological phenotype [13].
  • Here we report that cultured cells which express a beta-APP complementary DNA bearing a double mutation (Lys to Asn at residue 595 plus Met to Leu at position 596) found in a Swedish FAD family produce approximately 6-8-fold more A beta than cells expressing normal beta-APP [13].

Chemical compound and disease context of Adenosine diphosphate

  • NO*-resistant mutants of Escherichia coli were isolated that rapidly consumed NO*. An NO*-converting activity was reconstituted in extracts that required NADPH, FAD, and O2, was cyanide-sensitive, and produced NO3-. This nitric oxide dioxygenase (NOD) contained 19 of 20 N-terminal amino acids identical to those of the E. coli flavohemoglobin [14].
  • Denaturation of DNA photolyase (deoxyribodipyrimidine photolyase, EC from Escherichia coli with guanidine hydrochloride or acidification to pH 2 released, in addition to FAD, a chromophore with the spectral and chromatographic properties of a reduced pterin [15].
  • Functional characterization of flavin-containing monooxygenase 1B1 expressed in Saccharomyces cerevisiae and Escherichia coli and analysis of proposed FAD- and membrane-binding domains [16].
  • We propose that the amino acid sequence similarity between E. coli flavodoxin-flavodoxin reductase and the putative FMN, FAD, and NAD(P)H binding regions of cytochrome P450 reductase provides the basis for the reconstitution of P450c17 activities by this bacterial system [17].
  • The Lactococcus lactis enzyme is a dimer of heterodimers containing FMN, FAD, and a 2Fe-2S center [18].

Biological context of Adenosine diphosphate

  • Cloning of a complementary DNA for brain nitric oxide synthase reveals recognition sites for NADPH, FAD, flavin mononucleotide and calmodulin as well as phosphorylation sites, indicating that the synthase is regulated by many different factors [19].
  • Here, we summarize the mechanisms by which members of the GDI superfamily might function to coordinate events leading to membrane fusion, and we discuss the unexpected, yet striking structural homology of GDI to FAD-binding proteins [20].
  • PPO forms a loosely associated dimer and folds into an FAD-binding domain of the p-hydroxybenzoate-hydrolase fold and a substrate-binding domain that enclose a narrow active site cavity beneath the FAD and an alpha-helical membrane-binding domain [21].
  • 0. An amino acid sequence motif indicative of FAD utilization is located at the N terminus of the polypeptide [22].
  • The NADPH-binding dinucleotide folds of the beta-ketoacyl reductase and the enoyl reductase sites were identified by comparison with a known consensus sequence for the NADP- and FAD-binding dinucleotide folds [23].

Anatomical context of Adenosine diphosphate

  • However, they must interact with each other to induce the subsequent transfer of electrons from FAD to cytochrome b heme and molecular oxygen.This two-step model of regulation by Rac GTPase may provide a means of more effectively controlling the inflammatory responses of phagocytic leukocytes [24].
  • The covalent attachment of heme to apocytochrome c, and therefore the import of cytochrome c into mitochondria, is dependent on both NADH plus a cytosolic cofactor that has been identified to be FMN or FAD [25].
  • In 1957, Bloch and colleagues identified a factor from rat liver cytosol termed "supernatant protein factor (SPF)," which promotes the squalene epoxidation catalyzed by rat liver microsomes with oxygen, NADPH, FAD, and phospholipid [Tchen, T. T. & Bloch, K. (1957) J. Biol. Chem. 226, 921-930] [26].
  • Compared with the classical single-domain b5 and b5R proteins localized on endoplasmic reticulum membrane, b5+b5R also has binding motifs for heme, FAD, and NAD(P)H prosthetic groups but no membrane anchor [27].
  • These include the bacterial proteins NIFL and AER, both of which bind FAD, and the phy3 photoreceptor from Adiantium capillus-veneris [28].

Associations of Adenosine diphosphate with other chemical compounds

  • The latter, a homodimer with homology to the FAD-dependent disulphide oxidoreductases, catalyses the reaction NADPH + Hg(II)----NADP+ + H+ + Hg(0), one of the very rare enzymic reactions with metal substrates [2].
  • Dihydropyrimidine dehydrogenase contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice [29].
  • In the absence of this binding site in QR2, the enzyme retains the essential catalytic machinery, including affinity for FAD, but cannot bind phosphorylated hydride donors [30].
  • Cloning of a cDNA for the FAD-linked glycerol-3-phosphate dehydrogenase from rat liver and its regulation by thyroid hormones [31].
  • In flavocytochrome c fumarate reductase, all redox centers are in van der Waals contact with one another, thus providing an efficient conduit of electrons from the hemes via the FAD to fumarate [32].

Gene context of Adenosine diphosphate

  • That PS1 is a constituent of the cadherin/catenin complex makes that complex a potential target for PS1 FAD mutations [33].
  • Importantly, the TLN accumulations are suppressed by adenoviral expression of wild-type, FAD-linked and D257A mutant PS1, indicating that this phenotype is independent from gamma-secretase activity [34].
  • Exon 12 codes for the covalent FAD-binding-site and is the most conserved exon; the MAOA and MAOB exon 12 products share 93.9% peptide identity [35].
  • The Fig1 cDNA sequence encodes a predicted 70-kDa flavoprotein with best homology to the monoamine oxidases, particularly in domains responsible for FAD binding [36].
  • Descriptions of phenotypic features were available for six additional recently defined 14q-linked FAD kindreds: the findings in four of them (FAD4, FAD2, A, B) indicated a relatively consistently shared 14qFAD phenotype, conforming closely with the specific clinical and neuropathological characteristics noted in the L family [37].

Analytical, diagnostic and therapeutic context of Adenosine diphosphate

  • The structure of Erv2p, determined by X-ray crystallography to 1.5 A resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases [38].
  • Dithionite and NADH titrations of the native FAD oxidase require 1.7 eq of reductant/FAD and follow spectral courses very similar to those previously reported for the purified holoenzyme [39].
  • The requirements for FAD-attachment to His71 of 6-hydroxy-D-nicotine oxidase (6-HDNO) were investigated by site-directed mutagenesis [40].
  • Size exclusion chromatography was employed to follow the state of association of enzyme and dissociation of FAD from GOD [41].
  • The prosthetic group of the enzyme was identified to be FAD by high-performance liquid chromatography [42].


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  2. Structure of the detoxification catalyst mercuric ion reductase from Bacillus sp. strain RC607. Schiering, N., Kabsch, W., Moore, M.J., Distefano, M.D., Walsh, C.T., Pai, E.F. Nature (1991) [Pubmed]
  3. BLUF: a novel FAD-binding domain involved in sensory transduction in microorganisms. Gomelsky, M., Klug, G. Trends Biochem. Sci. (2002) [Pubmed]
  4. Dissection of the triple tryptophan electron transfer chain in Escherichia coli DNA photolyase: Trp382 is the primary donor in photoactivation. Byrdin, M., Eker, A.P., Vos, M.H., Brettel, K. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  5. Nucleotide sequence and expression of the mercurial-resistance operon from Staphylococcus aureus plasmid pI258. Laddaga, R.A., Chu, L., Misra, T.K., Silver, S. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  6. Genetic linkage studies suggest that Alzheimer's disease is not a single homogeneous disorder. FAD Collaborative Study Group. St George-Hyslop, P.H., Haines, J.L., Farrer, L.A., Polinsky, R., Van Broeckhoven, C., Goate, A., McLachlan, D.R., Orr, H., Bruni, A.C., Sorbi, S. Nature (1990) [Pubmed]
  7. Transmission and age-at-onset patterns in familial Alzheimer's disease: evidence for heterogeneity. Farrer, L.A., Myers, R.H., Cupples, L.A., St George-Hyslop, P.H., Bird, T.D., Rossor, M.N., Mullan, M.J., Polinsky, R., Nee, L., Heston, L. Neurology (1990) [Pubmed]
  8. Redox-Induced Changes in Flavin Structure and Roles of Flavin N(5) and the Ribityl 2'-OH Group in Regulating PutA-Membrane Binding(,). Zhang, W., Zhang, M., Zhu, W., Zhou, Y., Wanduragala, S., Rewinkel, D., Tanner, J.J., Becker, D.F. Biochemistry (2007) [Pubmed]
  9. Affinity probing of flavin binding sites. 1. Covalent attachment of 8-(methylsulfonyl)FAD to pig heart lipoamide dehydrogenase. Raibekas, A.A., Jorns, M.S. Biochemistry (1994) [Pubmed]
  10. Adolescent suicide, depression and family dysfunction. Martin, G., Rozanes, P., Pearce, C., Allison, S. Acta psychiatrica Scandinavica. (1995) [Pubmed]
  11. A disulfide relay system in mitochondria. Tokatlidis, K. Cell (2005) [Pubmed]
  12. Expression cloning of a cDNA for the major Fanconi anaemia gene, FAA. Lo Ten Foe, J.R., Rooimans, M.A., Bosnoyan-Collins, L., Alon, N., Wijker, M., Parker, L., Lightfoot, J., Carreau, M., Callen, D.F., Savoia, A., Cheng, N.C., van Berkel, C.G., Strunk, M.H., Gille, J.J., Pals, G., Kruyt, F.A., Pronk, J.C., Arwert, F., Buchwald, M., Joenje, H. Nat. Genet. (1996) [Pubmed]
  13. Mutation of the beta-amyloid precursor protein in familial Alzheimer's disease increases beta-protein production. Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A.Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., Selkoe, D.J. Nature (1992) [Pubmed]
  14. Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Gardner, P.R., Gardner, A.M., Martin, L.A., Salzman, A.L. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  15. Identification of the second chromophore of Escherichia coli and yeast DNA photolyases as 5,10-methenyltetrahydrofolate. Johnson, J.L., Hamm-Alvarez, S., Payne, G., Sancar, G.B., Rajagopalan, K.V., Sancar, A. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  16. Functional characterization of flavin-containing monooxygenase 1B1 expressed in Saccharomyces cerevisiae and Escherichia coli and analysis of proposed FAD- and membrane-binding domains. Lawton, M.P., Philpot, R.M. J. Biol. Chem. (1993) [Pubmed]
  17. Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities. Jenkins, C.M., Waterman, M.R. J. Biol. Chem. (1994) [Pubmed]
  18. Lys-D48 is required for charge stabilization, rapid flavin reduction, and internal electron transfer in the catalytic cycle of dihydroorotate dehydrogenase B of Lactococcus lactis. Combe, J.P., Basran, J., Hothi, P., Leys, D., Rigby, S.E., Munro, A.W., Scrutton, N.S. J. Biol. Chem. (2006) [Pubmed]
  19. Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Bredt, D.S., Hwang, P.M., Glatt, C.E., Lowenstein, C., Reed, R.R., Snyder, S.H. Nature (1991) [Pubmed]
  20. Structural insights into the function of the Rab GDI superfamily. Wu, S.K., Zeng, K., Wilson, I.A., Balch, W.E. Trends Biochem. Sci. (1996) [Pubmed]
  21. Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis. Koch, M., Breithaupt, C., Kiefersauer, R., Freigang, J., Huber, R., Messerschmidt, A. EMBO J. (2004) [Pubmed]
  22. Molecular structure and enzymatic function of lycopene cyclase from the cyanobacterium Synechococcus sp strain PCC7942. Cunningham, F.X., Sun, Z., Chamovitz, D., Hirschberg, J., Gantt, E. Plant Cell (1994) [Pubmed]
  23. Homology analysis of the protein sequences of fatty acid synthases from chicken liver, rat mammary gland, and yeast. Chang, S.I., Hammes, G.G. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  24. Molecular basis for Rac2 regulation of phagocyte NADPH oxidase. Diebold, B.A., Bokoch, G.M. Nat. Immunol. (2001) [Pubmed]
  25. Import of cytochrome c into mitochondria: reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c. Nicholson, D.W., Neupert, W. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  26. Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis. Shibata, N., Arita, M., Misaki, Y., Dohmae, N., Takio, K., Ono, T., Inoue, K., Arai, H. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  27. Identification of a cytochrome b-type NAD(P)H oxidoreductase ubiquitously expressed in human cells. Zhu, H., Qiu, H., Yoon, H.W., Huang, S., Bunn, H.F. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  28. LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide. Christie, J.M., Salomon, M., Nozue, K., Wada, M., Briggs, W.R. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  29. Crystal structure of dihydropyrimidine dehydrogenase, a major determinant of the pharmacokinetics of the anti-cancer drug 5-fluorouracil. Dobritzsch, D., Schneider, G., Schnackerz, K.D., Lindqvist, Y. EMBO J. (2001) [Pubmed]
  30. Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase). Zhao, Q., Yang, X.L., Holtzclaw, W.D., Talalay, P. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  31. Cloning of a cDNA for the FAD-linked glycerol-3-phosphate dehydrogenase from rat liver and its regulation by thyroid hormones. Müller, S., Seitz, H.J. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  32. Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1. Leys, D., Tsapin, A.S., Nealson, K.H., Meyer, T.E., Cusanovich, M.A., Van Beeumen, J.J. Nat. Struct. Biol. (1999) [Pubmed]
  33. Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts. Georgakopoulos, A., Marambaud, P., Efthimiopoulos, S., Shioi, J., Cui, W., Li, H.C., Schütte, M., Gordon, R., Holstein, G.R., Martinelli, G., Mehta, P., Friedrich, V.L., Robakis, N.K. Mol. Cell (1999) [Pubmed]
  34. Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway. Esselens, C., Oorschot, V., Baert, V., Raemaekers, T., Spittaels, K., Serneels, L., Zheng, H., Saftig, P., De Strooper, B., Klumperman, J., Annaert, W. J. Cell Biol. (2004) [Pubmed]
  35. Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Grimsby, J., Chen, K., Wang, L.J., Lan, N.C., Shih, J.C. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  36. Fig1, an interleukin 4-induced mouse B cell gene isolated by cDNA representational difference analysis. Chu, C.C., Paul, W.E. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  37. Phenotype of chromosome 14-linked familial Alzheimer's disease in a large kindred. Lampe, T.H., Bird, T.D., Nochlin, D., Nemens, E., Risse, S.C., Sumi, S.M., Koerker, R., Leaird, B., Wier, M., Raskind, M.A. Ann. Neurol. (1994) [Pubmed]
  38. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Gross, E., Sevier, C.S., Vala, A., Kaiser, C.A., Fass, D. Nat. Struct. Biol. (2002) [Pubmed]
  39. Catalytic properties of streptococcal NADH oxidase containing artificial flavins. Ahmed, S.A., Claiborne, A. J. Biol. Chem. (1992) [Pubmed]
  40. Lysine can replace arginine 67 in the mediation of covalent attachment of FAD to histidine 71 of 6-hydroxy-D-nicotine oxidase. Mauch, L., Bichler, V., Brandsch, R. J. Biol. Chem. (1990) [Pubmed]
  41. Thermal inactivation of glucose oxidase. Mechanism and stabilization using additives. Gouda, M.D., Singh, S.A., Rao, A.G., Thakur, M.S., Karanth, N.G. J. Biol. Chem. (2003) [Pubmed]
  42. Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase. Satomura, T., Kawakami, R., Sakuraba, H., Ohshima, T. J. Biol. Chem. (2002) [Pubmed]
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