메뉴 건너뛰기




Volumn 38, Issue 3, 2008, Pages 354-366

Functional characterization of a Drosophila melanogaster succinic semialdehyde dehydrogenase and a non-specific aldehyde dehydrogenase

Author keywords

Aldehyde dehydrogenase; Drosophila melanogaster; GABA catabolism; Site directed mutagenesis; Succinic semialdehyde dehydrogenase

Indexed keywords

4 AMINOBUTYRIC ACID; ALDEHYDE DEHYDROGENASE; HYBRID PROTEIN; SUCCINATE SEMIALDEHYDE DEHYDROGENASE;

EID: 38949113655     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2007.12.004     Document Type: Article
Times cited : (19)

References (46)
  • 2
    • 0025138339 scopus 로고
    • Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenase
    • Abriola D.P., MacKerell Jr. A.D., and Pietruszko R. Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenase. Biochem. J. 266 (1990) 179-187
    • (1990) Biochem. J. , vol.266 , pp. 179-187
    • Abriola, D.P.1    MacKerell Jr., A.D.2    Pietruszko, R.3
  • 3
    • 0025667055 scopus 로고
    • Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD)
    • Bartsch K., von Johnn-Martevil A., and Schulz A. Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD). J. Bacteriol. 172 (1990) 7035-7042
    • (1990) J. Bacteriol. , vol.172 , pp. 7035-7042
    • Bartsch, K.1    von Johnn-Martevil, A.2    Schulz, A.3
  • 5
    • 0018800405 scopus 로고
    • Succinic semialdehyde dehydrogenase. Reactivity of lysyl residues
    • Blaner W.S., and Churchich J. Succinic semialdehyde dehydrogenase. Reactivity of lysyl residues. J. Biol. Chem. 254 (1979) 1794-1798
    • (1979) J. Biol. Chem. , vol.254 , pp. 1794-1798
    • Blaner, W.S.1    Churchich, J.2
  • 6
    • 0025640958 scopus 로고
    • Chemical modification of aldehyde dehydrogenase by a vinyl ketone analogue of an insect pheromone
    • Blatter E.E., Tasayco M.L., Prestwich G., and Pietruszko R. Chemical modification of aldehyde dehydrogenase by a vinyl ketone analogue of an insect pheromone. Biochem. J. 272 (1990) 351-358
    • (1990) Biochem. J. , vol.272 , pp. 351-358
    • Blatter, E.E.1    Tasayco, M.L.2    Prestwich, G.3    Pietruszko, R.4
  • 7
    • 0037636431 scopus 로고    scopus 로고
    • Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants
    • Bouche N., Fait A., Bouchez D., Moller S.G., and Fromm H. Mitochondrial succinic-semialdehyde dehydrogenase of the gamma-aminobutyrate shunt is required to restrict levels of reactive oxygen intermediates in plants. Proc. Nat. Acad. Sci. USA 100 (2003) 6843-6848
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100 , pp. 6843-6848
    • Bouche, N.1    Fait, A.2    Bouchez, D.3    Moller, S.G.4    Fromm, H.5
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 25144509878 scopus 로고    scopus 로고
    • Insect GABA receptors: splicing, editing, and targeting by antiparasitics and insecticides
    • Buckingham S.D., Biggin P.C., Sattelle B.M., Brown L.A., and Sattelle D.B. Insect GABA receptors: splicing, editing, and targeting by antiparasitics and insecticides. Mol. Pharmacol. 68 (2005) 942-951
    • (2005) Mol. Pharmacol. , vol.68 , pp. 942-951
    • Buckingham, S.D.1    Biggin, P.C.2    Sattelle, B.M.3    Brown, L.A.4    Sattelle, D.B.5
  • 10
    • 0033213346 scopus 로고    scopus 로고
    • Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides
    • Busch K.B., and Fromm H. Plant succinic semialdehyde dehydrogenase. Cloning, purification, localization in mitochondria, and regulation by adenine nucleotides. Plant Physiol. 121 (1999) 589-597
    • (1999) Plant Physiol. , vol.121 , pp. 589-597
    • Busch, K.B.1    Fromm, H.2
  • 11
    • 0026725305 scopus 로고
    • Succinic semialdehyde dehydrogenase from mammalian brain: subunit analysis using polyclonal antiserum
    • Chambliss K.L., and Gibson K.M. Succinic semialdehyde dehydrogenase from mammalian brain: subunit analysis using polyclonal antiserum. Int. J. Biochem. 24 (1992) 1493-1499
    • (1992) Int. J. Biochem. , vol.24 , pp. 1493-1499
    • Chambliss, K.L.1    Gibson, K.M.2
  • 12
    • 0028895777 scopus 로고
    • Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression
    • Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A., Jakobs C., and Gibson K.M. Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression. J. Biol. Chem. 270 (1995) 461-467
    • (1995) J. Biol. Chem. , vol.270 , pp. 461-467
    • Chambliss, K.L.1    Caudle, D.L.2    Hinson, D.D.3    Moomaw, C.R.4    Slaughter, C.A.5    Jakobs, C.6    Gibson, K.M.7
  • 13
    • 0031350114 scopus 로고    scopus 로고
    • Neuromuscular glutamatergic and GABAergic channels
    • Dudel J., Adelsberger H., and Heckmann M. Neuromuscular glutamatergic and GABAergic channels. Invert. Neurosci. 3 (1997) 89-92
    • (1997) Invert. Neurosci. , vol.3 , pp. 89-92
    • Dudel, J.1    Adelsberger, H.2    Heckmann, M.3
  • 14
    • 0028961395 scopus 로고
    • Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis
    • Farres J., Wang T.T., Cunningham S.J., and Weiner H. Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochemistry 34 (1995) 2592-2598
    • (1995) Biochemistry , vol.34 , pp. 2592-2598
    • Farres, J.1    Wang, T.T.2    Cunningham, S.J.3    Weiner, H.4
  • 15
    • 33646744136 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase is essential for both adult and larval ethanol resistance in Drosophila melanogaster
    • Fry J.D., and Saweikis M. Aldehyde dehydrogenase is essential for both adult and larval ethanol resistance in Drosophila melanogaster. Genet. Res. 87 (2006) 87-92
    • (2006) Genet. Res. , vol.87 , pp. 87-92
    • Fry, J.D.1    Saweikis, M.2
  • 17
    • 0014046990 scopus 로고
    • The metabolism of gamma-aminobutyric acid (GABA) in the lobster nervous system. I. GABA-glutamate transaminase
    • Hall Z.W., and Kravitz E.A. The metabolism of gamma-aminobutyric acid (GABA) in the lobster nervous system. I. GABA-glutamate transaminase. J. Neurochem. 14 (1967) 45-54
    • (1967) J. Neurochem. , vol.14 , pp. 45-54
    • Hall, Z.W.1    Kravitz, E.A.2
  • 18
    • 0014035548 scopus 로고
    • The metabolism of gamma-aminobutyric acid (GABA) in the lobster nervous system. II. Succinic semialdehyde dehydrogenase
    • Hall Z.W., and Kravitz E.A. The metabolism of gamma-aminobutyric acid (GABA) in the lobster nervous system. II. Succinic semialdehyde dehydrogenase. J. Neurochem. 14 (1967) 55-61
    • (1967) J. Neurochem. , vol.14 , pp. 55-61
    • Hall, Z.W.1    Kravitz, E.A.2
  • 19
    • 0019877610 scopus 로고
    • Selective chemical modification of human liver aldehyde dehydrogenases E1 and E2 by iodoacetamide
    • Hempel J.D., and Pietruszko R. Selective chemical modification of human liver aldehyde dehydrogenases E1 and E2 by iodoacetamide. J. Biol. Chem. 256 (1981) 10889-10896
    • (1981) J. Biol. Chem. , vol.256 , pp. 10889-10896
    • Hempel, J.D.1    Pietruszko, R.2
  • 20
    • 0022341743 scopus 로고
    • Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations
    • Hempel J., Kaiser R., and Jornvall H. Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur. J. Biochem. 153 (1985) 13-28
    • (1985) Eur. J. Biochem. , vol.153 , pp. 13-28
    • Hempel, J.1    Kaiser, R.2    Jornvall, H.3
  • 23
    • 0033282769 scopus 로고    scopus 로고
    • Three-dimensional structure of mitochondrial aldehyde dehydrogenase. Mechanistic implications
    • Hurley T.D., Steinmetz C.G., and Weiner H. Three-dimensional structure of mitochondrial aldehyde dehydrogenase. Mechanistic implications. Adv. Exp. Med. Biol. 463 (1999) 15-25
    • (1999) Adv. Exp. Med. Biol. , vol.463 , pp. 15-25
    • Hurley, T.D.1    Steinmetz, C.G.2    Weiner, H.3
  • 24
    • 0002401415 scopus 로고
    • Aldehyde oxidation. II. Evidence for closely juxtaposed sulfhydryl groups on dehydrogenases
    • Jakoby W.B. Aldehyde oxidation. II. Evidence for closely juxtaposed sulfhydryl groups on dehydrogenases. J. Biol. Chem. 232 (1958) 89-97
    • (1958) J. Biol. Chem. , vol.232 , pp. 89-97
    • Jakoby, W.B.1
  • 25
    • 0010501027 scopus 로고
    • Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase
    • Jakoby W.B., and Scott E.M. Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase. J. Biol. Chem. 234 (1959) 937-940
    • (1959) J. Biol. Chem. , vol.234 , pp. 937-940
    • Jakoby, W.B.1    Scott, E.M.2
  • 26
    • 0023957385 scopus 로고
    • Purification and partial characterization of 4-aminobutyrate: 2-oxoglutarate aminotransferase from sheep brain and locust ganglia
    • Jeffery D., Rutherford D.M., Weitzman P.D., and Lunt G.G. Purification and partial characterization of 4-aminobutyrate: 2-oxoglutarate aminotransferase from sheep brain and locust ganglia. Biochem. J. 249 (1988) 795-799
    • (1988) Biochem. J. , vol.249 , pp. 795-799
    • Jeffery, D.1    Rutherford, D.M.2    Weitzman, P.D.3    Lunt, G.G.4
  • 27
    • 26044443055 scopus 로고    scopus 로고
    • High-level expression and characterization of the recombinant enzyme, and tissue distribution of human succinic semialdehyde dehydrogenase
    • Kang J.H., Park Y.B., Huh T.L., Lee W.H., Choi M.S., and Kwon O.S. High-level expression and characterization of the recombinant enzyme, and tissue distribution of human succinic semialdehyde dehydrogenase. Protein Expr. Purif. 44 (2005) 16-22
    • (2005) Protein Expr. Purif. , vol.44 , pp. 16-22
    • Kang, J.H.1    Park, Y.B.2    Huh, T.L.3    Lee, W.H.4    Choi, M.S.5    Kwon, O.S.6
  • 28
    • 0025803664 scopus 로고
    • Identification of a catalytically essential nucleophilic residue in sheep liver cytoplasmic aldehyde dehydrogenase
    • Kitson T.M., Hill J.P., and Midwinter G.G. Identification of a catalytically essential nucleophilic residue in sheep liver cytoplasmic aldehyde dehydrogenase. Biochem. J. 275 (1991) 207-210
    • (1991) Biochem. J. , vol.275 , pp. 207-210
    • Kitson, T.M.1    Hill, J.P.2    Midwinter, G.G.3
  • 29
    • 0013800863 scopus 로고
    • A comparison of the enzymes and substrates of gamma-aminobutyric acid metabolism in lobster excitatory and inhibitory axons
    • Kravitz E.A., Molinoff P.B., and Hall Z.W. A comparison of the enzymes and substrates of gamma-aminobutyric acid metabolism in lobster excitatory and inhibitory axons. Proc. Nat. Acad. Sci. USA 54 (1965) 778-782
    • (1965) Proc. Nat. Acad. Sci. USA , vol.54 , pp. 778-782
    • Kravitz, E.A.1    Molinoff, P.B.2    Hall, Z.W.3
  • 31
    • 0025259295 scopus 로고
    • Evidence for reactivity of serine-74 with trans-4-(N,N-dimethylamino)cinnamaldehyde during oxidation by the cytoplasmic aldehyde dehydrogenase from sheep liver
    • Loomes K.M., Midwinter G.G., Blackwell L.F., and Buckley P.D. Evidence for reactivity of serine-74 with trans-4-(N,N-dimethylamino)cinnamaldehyde during oxidation by the cytoplasmic aldehyde dehydrogenase from sheep liver. Biochemistry 29 (1990) 2070-2075
    • (1990) Biochemistry , vol.29 , pp. 2070-2075
    • Loomes, K.M.1    Midwinter, G.G.2    Blackwell, L.F.3    Buckley, P.D.4
  • 32
    • 0344604517 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a succinate semialdehyde dehydrogenase involved in the catabolism of 4-hydroxybutyric acid in Ralstonia eutropha
    • Lutke-Eversloh T., and Steinbuchel A. Biochemical and molecular characterization of a succinate semialdehyde dehydrogenase involved in the catabolism of 4-hydroxybutyric acid in Ralstonia eutropha. FEMS Microbiol. Lett. 181 (1999) 63-71
    • (1999) FEMS Microbiol. Lett. , vol.181 , pp. 63-71
    • Lutke-Eversloh, T.1    Steinbuchel, A.2
  • 33
    • 0025369088 scopus 로고
    • In vivo cloning and characterization of the gabCTDP gene cluster of Escherichia coli K-12
    • Metzer E., and Halpern Y.S. In vivo cloning and characterization of the gabCTDP gene cluster of Escherichia coli K-12. J. Bacteriol. 172 (1990) 3250-3256
    • (1990) J. Bacteriol. , vol.172 , pp. 3250-3256
    • Metzer, E.1    Halpern, Y.S.2
  • 34
    • 0027429443 scopus 로고
    • Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene
    • Niegemann E., Schulz A., and Bartsch K. Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene. Arch. Microbiol. 160 (1993) 454-460
    • (1993) Arch. Microbiol. , vol.160 , pp. 454-460
    • Niegemann, E.1    Schulz, A.2    Bartsch, K.3
  • 35
    • 0021911431 scopus 로고
    • Response of the cockroach brain gamma-aminobutyric acid system to isonicotinic acid hydrazide and mercaptopropionic acid
    • Pandey A., and Singh R. Response of the cockroach brain gamma-aminobutyric acid system to isonicotinic acid hydrazide and mercaptopropionic acid. Biochem. Int. 10 (1985) 213-220
    • (1985) Biochem. Int. , vol.10 , pp. 213-220
    • Pandey, A.1    Singh, R.2
  • 36
  • 37
    • 0024578526 scopus 로고
    • Purification and properties of two succinic semialdehyde dehydrogenases from Klebsiella pneumoniae
    • Sanchez M., Fernández J., Martin M., Gibello A., and Garrido-Pertierra A. Purification and properties of two succinic semialdehyde dehydrogenases from Klebsiella pneumoniae. Biochim. Biophys. Acta 990 (1989) 225-231
    • (1989) Biochim. Biophys. Acta , vol.990 , pp. 225-231
    • Sanchez, M.1    Fernández, J.2    Martin, M.3    Gibello, A.4    Garrido-Pertierra, A.5
  • 38
    • 0027439723 scopus 로고
    • 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), and gamma-vinyl-gamma-aminobutyric acid (gamma-vinyl GABA) alter neurotransmitter concentrations in the nervous tissue of the goldfish (Carassius auratus) but not the cockroach (Periplaneta americana)
    • Sloley B.D., and McKenna K.F. 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), and gamma-vinyl-gamma-aminobutyric acid (gamma-vinyl GABA) alter neurotransmitter concentrations in the nervous tissue of the goldfish (Carassius auratus) but not the cockroach (Periplaneta americana). Neurochem. Int. 22 (1993) 197-203
    • (1993) Neurochem. Int. , vol.22 , pp. 197-203
    • Sloley, B.D.1    McKenna, K.F.2
  • 39
    • 17744419979 scopus 로고    scopus 로고
    • Aldehyde dehydrogenase gene superfamily: the 2002 update
    • Sophos N.A., and Vasiliou V. Aldehyde dehydrogenase gene superfamily: the 2002 update. Chem. Biol. Interact. 143-144 (2003) 5-22
    • (2003) Chem. Biol. Interact. , vol.143-144 , pp. 5-22
    • Sophos, N.A.1    Vasiliou, V.2
  • 40
    • 21344434773 scopus 로고    scopus 로고
    • An alcohol acyl transferase from apple (cv. Royal Gala), MpAAT1, produces esters involved in apple fruit flavor
    • Souleyre E.J., Greenwood D.R., Friel E.N., Karunairetnam S., and Newcomb R.D. An alcohol acyl transferase from apple (cv. Royal Gala), MpAAT1, produces esters involved in apple fruit flavor. FEBS J. 272 (2005) 3132-3144
    • (2005) FEBS J. , vol.272 , pp. 3132-3144
    • Souleyre, E.J.1    Greenwood, D.R.2    Friel, E.N.3    Karunairetnam, S.4    Newcomb, R.D.5
  • 41
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion
    • Steinmetz C.G., Xie P., Weiner H., and Hurley T.D. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 5 (1997) 701-711
    • (1997) Structure , vol.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.2    Weiner, H.3    Hurley, T.D.4
  • 42
    • 0023851702 scopus 로고
    • Identification of the cysteine residue in the active site of horse liver mitochondrial aldehyde dehydrogenase
    • Tu G.C., and Weiner H. Identification of the cysteine residue in the active site of horse liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 263 (1988) 1212-1217
    • (1988) J. Biol. Chem. , vol.263 , pp. 1212-1217
    • Tu, G.C.1    Weiner, H.2
  • 43
    • 3042551383 scopus 로고    scopus 로고
    • Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism
    • Vasiliou V., Pappa A., and Estey T. Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism. Drug Metab. Rev. 36 (2004) 279-299
    • (2004) Drug Metab. Rev. , vol.36 , pp. 279-299
    • Vasiliou, V.1    Pappa, A.2    Estey, T.3
  • 44
    • 0028922730 scopus 로고
    • Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis
    • Wang X., and Weiner H. Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis. Biochemistry 34 (1995) 237-243
    • (1995) Biochemistry , vol.34 , pp. 237-243
    • Wang, X.1    Weiner, H.2
  • 46
    • 0027186362 scopus 로고
    • Role of the highly conserved histidine residues in rat liver mitochondrial aldehyde dehydrogenase as studied by site-directed mutagenesis
    • Zheng C.F., and Weiner H. Role of the highly conserved histidine residues in rat liver mitochondrial aldehyde dehydrogenase as studied by site-directed mutagenesis. Arch. Biochem. Biophys. 305 (1993) 460-466
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 460-466
    • Zheng, C.F.1    Weiner, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.