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Volumn 25, Issue 11, 2012, Pages 2443-2450

The mitochondrial amidoxime reducing component (mARC) is involved in detoxification of N-hydroxylated base analogues

Author keywords

[No Author keywords available]

Indexed keywords

CELL DNA; ENZYME; MITOCHONDRIAL AMIDOXIME REDUCING COMPONENT; MOLYBDENUM COMPLEX; NUCLEIC ACID BASE; NUCLEOSIDE; PURINE; PYRIMIDINE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 84869471923     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx300298m     Document Type: Article
Times cited : (55)

References (31)
  • 2
    • 79952752115 scopus 로고    scopus 로고
    • Molybdenum enzymes in higher organisms
    • Hille, R., Nishino, T., and Bittner, F. (2011) Molybdenum enzymes in higher organisms Coord. Chem. Rev. 255, 1179-1205
    • (2011) Coord. Chem. Rev. , vol.255 , pp. 1179-1205
    • Hille, R.1    Nishino, T.2    Bittner, F.3
  • 3
    • 42449117257 scopus 로고    scopus 로고
    • Mammalian aldehyde oxidases: Genetics, evolution and biochemistry
    • Garattini, E., Fratelli, M., and Terao, M. (2008) Mammalian aldehyde oxidases: Genetics, evolution and biochemistry Cell. Mol. Life Sci. 65, 1019-1048
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1019-1048
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 4
    • 0026669725 scopus 로고
    • The pterin molybdenum cofactors
    • Rajagopalan, K. V. and Johnson, J. L. (1992) The pterin molybdenum cofactors J. Biol. Chem. 267, 10199-10202
    • (1992) J. Biol. Chem. , vol.267 , pp. 10199-10202
    • Rajagopalan, K.V.1    Johnson, J.L.2
  • 5
    • 33845952893 scopus 로고    scopus 로고
    • Identification of the missing component in the mitochondrial benzamidoxime prodrug-converting system as a novel molybdenum enzyme
    • Havemeyer, A., Bittner, F., Wollers, S., Mendel, R., Kunze, T., and Clement, B. (2006) Identification of the missing component in the mitochondrial benzamidoxime prodrug-converting system as a novel molybdenum enzyme J. Biol. Chem. 281, 34796-34802
    • (2006) J. Biol. Chem. , vol.281 , pp. 34796-34802
    • Havemeyer, A.1    Bittner, F.2    Wollers, S.3    Mendel, R.4    Kunze, T.5    Clement, B.6
  • 6
    • 0037154431 scopus 로고    scopus 로고
    • MOSC domains: Ancient, predicted sulfur-carrier domains, present in diverse metal-sulfur cluster biosynthesis proteins including Molybdenum cofactor sulfurases
    • Anantharaman, V. and Aravind, L. (2002) MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal-sulfur cluster biosynthesis proteins including Molybdenum cofactor sulfurases FEMS Microbiol. Lett. 207, 55-61
    • (2002) FEMS Microbiol. Lett. , vol.207 , pp. 55-61
    • Anantharaman, V.1    Aravind, L.2
  • 9
    • 78549238237 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum-enzyme family in eukaryotes
    • Wahl, B., Reichmann, D., Niks, D., Krompholz, N., Havemeyer, A., Clement, B., Messerschmidt, T., Rothkegel, M., Biester, H., Hille, R., Mendel, R. R., and Bittner, F. (2010) Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum-enzyme family in eukaryotes J. Biol. Chem. 285, 37847-37859
    • (2010) J. Biol. Chem. , vol.285 , pp. 37847-37859
    • Wahl, B.1    Reichmann, D.2    Niks, D.3    Krompholz, N.4    Havemeyer, A.5    Clement, B.6    Messerschmidt, T.7    Rothkegel, M.8    Biester, H.9    Hille, R.10    Mendel, R.R.11    Bittner, F.12
  • 10
    • 84857462023 scopus 로고    scopus 로고
    • An amidoxime reductase system in adipocyte mitochondria containing cytochrome b5 type B (CYB5B) and molybdenum cofactor sulfurase C-terminal containing 2 (MOSC2) of importance for lipid synthesis
    • Neve, E. P., Nordling, A., Andersson, T. B., Hellman, U., Diczfalusy, U., Johansson, I., and Ingelman-Sundberg, M. (2012) An amidoxime reductase system in adipocyte mitochondria containing cytochrome b5 type B (CYB5B) and molybdenum cofactor sulfurase C-terminal containing 2 (MOSC2) of importance for lipid synthesis J. Biol. Chem. 287, 6307-6317
    • (2012) J. Biol. Chem. , vol.287 , pp. 6307-6317
    • Neve, E.P.1    Nordling, A.2    Andersson, T.B.3    Hellman, U.4    Diczfalusy, U.5    Johansson, I.6    Ingelman-Sundberg, M.7
  • 11
    • 80054882002 scopus 로고    scopus 로고
    • The fourth mammalian molybdenum enzyme mARC: Current state of research
    • Havemeyer, A., Lang, J., and Clement, B. (2011) The fourth mammalian molybdenum enzyme mARC: Current state of research Drug Metab Rev 43, 524-539
    • (2011) Drug Metab Rev , vol.43 , pp. 524-539
    • Havemeyer, A.1    Lang, J.2    Clement, B.3
  • 13
    • 0030807474 scopus 로고    scopus 로고
    • Naming the mutagenic nucleic acid base analogs: The Galatea syndrome
    • Khromov-Borisov, N. N. (1997) Naming the mutagenic nucleic acid base analogs: The Galatea syndrome Mutat. Res. 379, 95-103
    • (1997) Mutat. Res. , vol.379 , pp. 95-103
    • Khromov-Borisov, N.N.1
  • 14
    • 0025176645 scopus 로고
    • Hepatic-Microsomal N-Hydroxylation of Adenine to 6-N-Hydroxylaminopurine
    • Clement, B. and Kunze, T. (1990) Hepatic-Microsomal N-Hydroxylation of Adenine to 6-N-Hydroxylaminopurine Biochem. Pharmacol. 39, 925-933
    • (1990) Biochem. Pharmacol. , vol.39 , pp. 925-933
    • Clement, B.1    Kunze, T.2
  • 15
    • 0032532285 scopus 로고    scopus 로고
    • Oxidation of DNA bases, deoxyribonucleosides and homopolymers by peroxyl radicals
    • Simandan, T., Sun, J., and Dix, T. A. (1998) Oxidation of DNA bases, deoxyribonucleosides and homopolymers by peroxyl radicals Biochem. J. 335 (Part 2) 233-240
    • (1998) Biochem. J. , vol.335 , Issue.PART 2 , pp. 233-240
    • Simandan, T.1    Sun, J.2    Dix, T.A.3
  • 16
    • 0022974708 scopus 로고
    • Biochemical studies on the mutagen, 6-N-hydroxylaminopurine. Synthesis of the deoxynucleoside triphosphate and its incorporation into DNA in vitro
    • Abdul-Masih, M. T. and Bessman, M. J. (1986) Biochemical studies on the mutagen, 6-N-hydroxylaminopurine. Synthesis of the deoxynucleoside triphosphate and its incorporation into DNA in vitro J. Biol. Chem. 261, 2020-2026
    • (1986) J. Biol. Chem. , vol.261 , pp. 2020-2026
    • Abdul-Masih, M.T.1    Bessman, M.J.2
  • 18
    • 84857546209 scopus 로고    scopus 로고
    • Elevated Levels of DNA Strand Breaks Induced by a Base Analog in the Human Cell Line with the P32T ITPA Variant
    • 10.4061/2010/872180
    • Waisertreiger, I. S., Menezes, M. R., Randazzo, J., and Pavlov, Y. I. (2010) Elevated Levels of DNA Strand Breaks Induced by a Base Analog in the Human Cell Line with the P32T ITPA Variant J Nucleic Acids 10.4061/2010/872180
    • (2010) J Nucleic Acids
    • Waisertreiger, I.S.1    Menezes, M.R.2    Randazzo, J.3    Pavlov, Y.I.4
  • 20
    • 0025091897 scopus 로고
    • Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane
    • Hovius, R., Lambrechts, H., Nicolay, K., and de Kruijff, B. (1990) Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane Biochim. Biophys. Acta 1021, 217-226
    • (1990) Biochim. Biophys. Acta , vol.1021 , pp. 217-226
    • Hovius, R.1    Lambrechts, H.2    Nicolay, K.3    De Kruijff, B.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0000171230 scopus 로고
    • A new method for preparing flavin-adenine dinucleotide
    • Whitby, L. G. (1953) A new method for preparing flavin-adenine dinucleotide Biochem. J. 54, 437-442
    • (1953) Biochem. J. , vol.54 , pp. 437-442
    • Whitby, L.G.1
  • 23
    • 0017869007 scopus 로고
    • The measurement of difference spectra: Application to the cytochromes of microsomes
    • Estabrook, R. W. and Werringloer, J. (1978) The measurement of difference spectra: Application to the cytochromes of microsomes Methods Enzymol. 52, 212-220
    • (1978) Methods Enzymol. , vol.52 , pp. 212-220
    • Estabrook, R.W.1    Werringloer, J.2
  • 24
    • 33745490496 scopus 로고    scopus 로고
    • Mutations in neutrophil elastase causing congenital neutropenia lead to cytoplasmic protein accumulation and induction of the unfolded protein response
    • Kollner, I., Sodeik, B., Schreek, S., Heyn, H., von Neuhoff, N., Germeshausen, M., Zeidler, C., Kruger, M., Schlegelberger, B., Welte, K., and Beger, C. (2006) Mutations in neutrophil elastase causing congenital neutropenia lead to cytoplasmic protein accumulation and induction of the unfolded protein response Blood 108, 493-500
    • (2006) Blood , vol.108 , pp. 493-500
    • Kollner, I.1    Sodeik, B.2    Schreek, S.3    Heyn, H.4    Von Neuhoff, N.5    Germeshausen, M.6    Zeidler, C.7    Kruger, M.8    Schlegelberger, B.9    Welte, K.10    Beger, C.11
  • 26
    • 46249108210 scopus 로고    scopus 로고
    • The use of total protein stains as loading controls: An alternative to high-abundance single-protein controls in semi-quantitative immunoblotting
    • Aldridge, G. M., Podrebarac, D. M., Greenough, W. T., and Weiler, I. J. (2008) The use of total protein stains as loading controls: An alternative to high-abundance single-protein controls in semi-quantitative immunoblotting J. Neurosci. Methods 172, 250-254
    • (2008) J. Neurosci. Methods , vol.172 , pp. 250-254
    • Aldridge, G.M.1    Podrebarac, D.M.2    Greenough, W.T.3    Weiler, I.J.4
  • 27
    • 0026756768 scopus 로고
    • The reduction of 6-N-hydroxylaminopurine to adenine by xanthine oxidase
    • Clement, B. and Kunze, T. (1992) The reduction of 6-N-hydroxylaminopurine to adenine by xanthine oxidase Biochem. Pharmacol. 44, 1501-1509
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1501-1509
    • Clement, B.1    Kunze, T.2
  • 28
    • 80053442039 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii Molybdenum Cofactor Enzyme crARC Has a Zn-Dependent Activity and Protein Partners Similar to Those of Its Human Homologue
    • Chamizo-Ampudia, A., Galvan, A., Fernandez, E., and Llamas, A. (2011) The Chlamydomonas reinhardtii Molybdenum Cofactor Enzyme crARC Has a Zn-Dependent Activity and Protein Partners Similar to Those of Its Human Homologue Eukaryotic Cell 10, 1270-1282
    • (2011) Eukaryotic Cell , vol.10 , pp. 1270-1282
    • Chamizo-Ampudia, A.1    Galvan, A.2    Fernandez, E.3    Llamas, A.4
  • 29
    • 34247091997 scopus 로고    scopus 로고
    • Molybdenum cofactor-dependent resistance to N-hydroxylated base analogs in Escherichia coli is independent of MobA function
    • Kozmin, S. G. and Schaaper, R. M. (2007) Molybdenum cofactor-dependent resistance to N-hydroxylated base analogs in Escherichia coli is independent of MobA function Mutat. Res. 619, 9-15
    • (2007) Mutat. Res. , vol.619 , pp. 9-15
    • Kozmin, S.G.1    Schaaper, R.M.2
  • 30
    • 40549106101 scopus 로고    scopus 로고
    • YcbX and yiiM, two novel determinants for resistance of Escherichia coli to N-hydroxylated base analogues
    • Kozmin, S. G., Leroy, P., Pavlov, Y. I., and Schaaper, R. M. (2008) YcbX and yiiM, two novel determinants for resistance of Escherichia coli to N-hydroxylated base analogues Mol. Microbiol. 68, 51-65
    • (2008) Mol. Microbiol. , vol.68 , pp. 51-65
    • Kozmin, S.G.1    Leroy, P.2    Pavlov, Y.I.3    Schaaper, R.M.4
  • 31
    • 77950646264 scopus 로고    scopus 로고
    • Role for CysJ flavin reductase in molybdenum cofactor-dependent resistance of Escherichia coli to 6-N-hydroxylaminopurine
    • Kozmin, S. G., Wang, J., and Schaaper, R. M. (2010) Role for CysJ flavin reductase in molybdenum cofactor-dependent resistance of Escherichia coli to 6-N-hydroxylaminopurine J. Bacteriol. 192, 2026-2033
    • (2010) J. Bacteriol. , vol.192 , pp. 2026-2033
    • Kozmin, S.G.1    Wang, J.2    Schaaper, R.M.3


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