메뉴 건너뛰기




Volumn 280, Issue 15, 2013, Pages 3685-3696

The ORF slr0091 of Synechocystis sp. PCC6803 encodes a high-light induced aldehyde dehydrogenase converting apocarotenals and alkanals

Author keywords

aldehyde dehydrogenase; alkanals; apocarotenoids; carotenoid cleavage; cyanobacteria

Indexed keywords

ALDEHYDE; ALDEHYDE DEHYDROGENASE; ALKANAL; APOCAROTENAL; RETINAL; UNCLASSIFIED DRUG;

EID: 84880329211     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12361     Document Type: Article
Times cited : (32)

References (48)
  • 3
    • 3042551383 scopus 로고    scopus 로고
    • Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism
    • Vasiliou V, Pappa A, &, Estey T, (2004) Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism. Drug Metab Rev 36, 279-299.
    • (2004) Drug Metab Rev , vol.36 , pp. 279-299
    • Vasiliou, V.1    Pappa, A.2    Estey, T.3
  • 4
    • 77957145640 scopus 로고    scopus 로고
    • Molecular characterization, expression analysis, and role of ALDH3B1 in the cellular protection against oxidative stress
    • Marchitti SA, Brocker C, Orlicky DJ, &, Vasiliou V, (2010) Molecular characterization, expression analysis, and role of ALDH3B1 in the cellular protection against oxidative stress. Free Radic Biol Med 49, 1432-1443.
    • (2010) Free Radic Biol Med , vol.49 , pp. 1432-1443
    • Marchitti, S.A.1    Brocker, C.2    Orlicky, D.J.3    Vasiliou, V.4
  • 5
    • 0041762551 scopus 로고    scopus 로고
    • Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance
    • Sunkar R, Bartels D, &, Kirch H-H, (2003) Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance. Plant J 35, 452-464.
    • (2003) Plant J , vol.35 , pp. 452-464
    • Sunkar, R.1    Bartels, D.2    Kirch, H.-H.3
  • 6
    • 33646575943 scopus 로고    scopus 로고
    • Over-expression of different aldehyde dehydrogenase genes in Arabidopsis thaliana confers tolerance to abiotic stress and protects plants against lipid peroxidation and oxidative stress
    • Kotchoni SO, Kuhns C, Ditzer A, Kirch H-H, &, Bartels D, (2006) Over-expression of different aldehyde dehydrogenase genes in Arabidopsis thaliana confers tolerance to abiotic stress and protects plants against lipid peroxidation and oxidative stress. Plant, Cell Environ 29, 1033-1048.
    • (2006) Plant, Cell Environ , vol.29 , pp. 1033-1048
    • Kotchoni, S.O.1    Kuhns, C.2    Ditzer, A.3    Kirch, H.-H.4    Bartels, D.5
  • 7
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H, Schaur RJ, &, Zollner H, (1991) Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 11, 81-128.
    • (1991) Free Radic Biol Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 8
    • 0346724680 scopus 로고    scopus 로고
    • Human aldehyde dehydrogenase 3A1 (ALDH3A1): Biochemical characterization and immunohistochemical localization in the cornea
    • Pappa A, Estey T, Manzer R, Brown D, &, Vasiliou V, (2003) Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea. Biochem J 376, 615-623.
    • (2003) Biochem J , vol.376 , pp. 615-623
    • Pappa, A.1    Estey, T.2    Manzer, R.3    Brown, D.4    Vasiliou, V.5
  • 9
    • 49249123034 scopus 로고    scopus 로고
    • The ylo-1 gene encodes an aldehyde dehydrogenase responsible for the last reaction in the Neurospora carotenoid pathway
    • Estrada AF, Youssar L, Scherzinger D, Al-Babili S, &, Avalos J, (2008) The ylo-1 gene encodes an aldehyde dehydrogenase responsible for the last reaction in the Neurospora carotenoid pathway. Mol Microbiol 69, 1207-1220.
    • (2008) Mol Microbiol , vol.69 , pp. 1207-1220
    • Estrada, A.F.1    Youssar, L.2    Scherzinger, D.3    Al-Babili, S.4    Avalos, J.5
  • 10
    • 84860390110 scopus 로고    scopus 로고
    • The gene carD encodes the aldehyde dehydrogenase responsible for neurosporaxanthin biosynthesis in Fusarium fujikuroi
    • Díaz-Sánchez V, Estrada AF, Trautmann D, Al-Babili S, &, Avalos J, (2011) The gene carD encodes the aldehyde dehydrogenase responsible for neurosporaxanthin biosynthesis in Fusarium fujikuroi. FEBS J 278, 3164-3176.
    • (2011) FEBS J , vol.278 , pp. 3164-3176
    • Díaz-Sánchez, V.1    Estrada, A.F.2    Trautmann, D.3    Al-Babili, S.4    Avalos, J.5
  • 11
    • 16344383492 scopus 로고    scopus 로고
    • Oxidative tailoring of carotenoids: A prospect towards novel functions in plants
    • Bouvier F, Isner J-C, Dogbo O, &, Camara B, (2005) Oxidative tailoring of carotenoids: a prospect towards novel functions in plants. Trends Plant Sci 10, 187-194.
    • (2005) Trends Plant Sci , vol.10 , pp. 187-194
    • Bouvier, F.1    Isner, J.-C.2    Dogbo, O.3    Camara, B.4
  • 12
    • 33745946053 scopus 로고    scopus 로고
    • Vitamin synthesis in plants: Tocopherols and carotenoids
    • DellaPenna D, &, Pogson BJ, (2006) Vitamin synthesis in plants: tocopherols and carotenoids. Annu Rev Plant Biol 57, 711-738.
    • (2006) Annu Rev Plant Biol , vol.57 , pp. 711-738
    • Dellapenna, D.1    Pogson, B.J.2
  • 13
    • 79953065470 scopus 로고    scopus 로고
    • Carotenoids and their cleavage products: Biosynthesis and functions
    • Walter MH, &, Strack D, (2011) Carotenoids and their cleavage products: biosynthesis and functions. Nat Prod Rep 28, 663-692.
    • (2011) Nat Prod Rep , vol.28 , pp. 663-692
    • Walter, M.H.1    Strack, D.2
  • 14
    • 0033397253 scopus 로고    scopus 로고
    • Co-oxidation of β-carotene catalyzed by soybean and recombinant pea lipoxygenases
    • Wu Z, Robinson DS, Hughes RK, Casey R, Hardy D, &, West SI, (1999) Co-oxidation of β-carotene catalyzed by soybean and recombinant pea lipoxygenases. J Agric Food Chem 47, 4899-4906.
    • (1999) J Agric Food Chem , vol.47 , pp. 4899-4906
    • Wu, Z.1    Robinson, D.S.2    Hughes, R.K.3    Casey, R.4    Hardy, D.5    West, S.I.6
  • 16
    • 0034697178 scopus 로고    scopus 로고
    • Filling the gap in vitamin A research. Molecular identification of an enzyme cleaving β-carotene to retinal
    • Von Lintig J, &, Vogt K, (2000) Filling the gap in vitamin A research. Molecular identification of an enzyme cleaving β-carotene to retinal. J Biol Chem 275, 11915-11920.
    • (2000) J Biol Chem , vol.275 , pp. 11915-11920
    • Von Lintig, J.1    Vogt, K.2
  • 17
    • 34247874569 scopus 로고    scopus 로고
    • Retinal biosynthesis in fungi: Characterization of the carotenoid oxygenase CarX from Fusarium fujikuroi
    • Prado-Cabrero A, Scherzinger D, Avalos J, &, Al-Babili S, (2007a) Retinal biosynthesis in fungi: characterization of the carotenoid oxygenase CarX from Fusarium fujikuroi. Eukaryot Cell 6, 650-657.
    • (2007) Eukaryot Cell , vol.6 , pp. 650-657
    • Prado-Cabrero, A.1    Scherzinger, D.2    Avalos, J.3    Al-Babili, S.4
  • 18
    • 0037933420 scopus 로고    scopus 로고
    • Biosynthesis of the food and cosmetic plant pigment bixin (annatto)
    • Bouvier F, Dogbo O, &, Camara B, (2003) Biosynthesis of the food and cosmetic plant pigment bixin (annatto). Science 300, 2089-2091.
    • (2003) Science , vol.300 , pp. 2089-2091
    • Bouvier, F.1    Dogbo, O.2    Camara, B.3
  • 19
    • 35648978119 scopus 로고    scopus 로고
    • Carotenoids and carotenogenesis in cyanobacteria: Unique ketocarotenoids and carotenoid glycosides
    • Takaichi S, &, Mochimaru M, (2007) Carotenoids and carotenogenesis in cyanobacteria: unique ketocarotenoids and carotenoid glycosides. Cell Mol Life Sci 64, 2607-2619.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2607-2619
    • Takaichi, S.1    Mochimaru, M.2
  • 20
    • 33646233188 scopus 로고    scopus 로고
    • Effect of pretreatment of salt, copper and temperature on ultraviolet-B-induced antioxidants in diazotrophic cyanobacterium Anabaena doliolum
    • Srivastava AK, Bhargava P, Mishra Y, Shukla B, &, Rai LC, (2006) Effect of pretreatment of salt, copper and temperature on ultraviolet-B-induced antioxidants in diazotrophic cyanobacterium Anabaena doliolum. J Basic Microbiol 46, 135-144.
    • (2006) J Basic Microbiol , vol.46 , pp. 135-144
    • Srivastava, A.K.1    Bhargava, P.2    Mishra, Y.3    Shukla, B.4    Rai, L.C.5
  • 22
    • 77957914336 scopus 로고    scopus 로고
    • Roles of xanthophyll carotenoids in protection against photoinhibition and oxidative stress in the cyanobacterium Synechococcus sp. strain PCC 7002
    • Zhu Y, Graham JE, Ludwig M, Xiong W, Alvey RM, Shen G, &, Bryant DA, (2010) Roles of xanthophyll carotenoids in protection against photoinhibition and oxidative stress in the cyanobacterium Synechococcus sp. strain PCC 7002. Arch Biochem Biophys 504, 86-99.
    • (2010) Arch Biochem Biophys , vol.504 , pp. 86-99
    • Zhu, Y.1    Graham, J.E.2    Ludwig, M.3    Xiong, W.4    Alvey, R.M.5    Shen, G.6    Bryant, D.A.7
  • 24
    • 33846018938 scopus 로고    scopus 로고
    • Identification of carotenoid cleavage dioxygenases from Nostoc sp. PCC 7120 with different cleavage activities
    • Marasco EK, Vay K, &, Schmidt-Dannert C, (2006) Identification of carotenoid cleavage dioxygenases from Nostoc sp. PCC 7120 with different cleavage activities. J Biol Chem 281, 31583-31593.
    • (2006) J Biol Chem , vol.281 , pp. 31583-31593
    • Marasco, E.K.1    Vay, K.2    Schmidt-Dannert, C.3
  • 25
    • 45149134225 scopus 로고    scopus 로고
    • In vitro characterization of a carotenoid cleavage dioxygenase from Nostoc sp. PCC 7120 reveals a novel cleavage pattern, cytosolic localization and induction by highlight
    • Scherzinger D, &, Al-Babili S, (2008) In vitro characterization of a carotenoid cleavage dioxygenase from Nostoc sp. PCC 7120 reveals a novel cleavage pattern, cytosolic localization and induction by highlight. Mol Microbiol 69, 231-244.
    • (2008) Mol Microbiol , vol.69 , pp. 231-244
    • Scherzinger, D.1    Al-Babili, S.2
  • 26
    • 70349243466 scopus 로고    scopus 로고
    • In vitro characterization of Synechocystis CYP120A1 revealed the first nonanimal retinoic acid hydroxylase
    • Alder A, Bigler P, Werck-Reichhart D, &, Al-Babili S, (2009) In vitro characterization of Synechocystis CYP120A1 revealed the first nonanimal retinoic acid hydroxylase. FEBS J 276, 5416-5431.
    • (2009) FEBS J , vol.276 , pp. 5416-5431
    • Alder, A.1    Bigler, P.2    Werck-Reichhart, D.3    Al-Babili, S.4
  • 27
    • 14544289081 scopus 로고    scopus 로고
    • Retinal biosynthesis in Eubacteria: In vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803
    • Ruch S, Beyer P, Ernst H, &, Al-Babili S, (2005) Retinal biosynthesis in Eubacteria: in vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803. Mol Microbiol 55, 1015-1024.
    • (2005) Mol Microbiol , vol.55 , pp. 1015-1024
    • Ruch, S.1    Beyer, P.2    Ernst, H.3    Al-Babili, S.4
  • 28
    • 33748757737 scopus 로고    scopus 로고
    • Retinal is formed from apo-carotenoids in Nostoc sp. PCC7120: In vitro characterization of an apo-carotenoid oxygenase
    • Scherzinger D, Ruch S, Kloer DP, Wilde A, &, Al-Babili S, (2006) Retinal is formed from apo-carotenoids in Nostoc sp. PCC7120: in vitro characterization of an apo-carotenoid oxygenase. Biochem J 398, 361-369.
    • (2006) Biochem J , vol.398 , pp. 361-369
    • Scherzinger, D.1    Ruch, S.2    Kloer, D.P.3    Wilde, A.4    Al-Babili, S.5
  • 29
    • 14744294199 scopus 로고    scopus 로고
    • A retinoic acid binding cytochrome P450: CYP120A1 from Synechocystis sp. PCC 6803
    • Ke N, Baudry J, Makris TM, Schuler M, &, Sligar SG, (2005) A retinoic acid binding cytochrome P450: CYP120A1 from Synechocystis sp. PCC 6803. Arch Biochem Biophys 436, 110-120.
    • (2005) Arch Biochem Biophys , vol.436 , pp. 110-120
    • Ke, N.1    Baudry, J.2    Makris, T.M.3    Schuler, M.4    Sligar, S.G.5
  • 30
    • 45749136727 scopus 로고    scopus 로고
    • Crystal structures of substrate-free and retinoic acid-bound cyanobacterial cytochrome P450 CYP120A1
    • Kühnel K, Ke N, Cryle MJ, Sligar SG, Schuler MA, &, Schlichting I, (2008) Crystal structures of substrate-free and retinoic acid-bound cyanobacterial cytochrome P450 CYP120A1. Biochemistry 47, 6552-6559.
    • (2008) Biochemistry , vol.47 , pp. 6552-6559
    • Kühnel, K.1    Ke, N.2    Cryle, M.J.3    Sligar, S.G.4    Schuler, M.A.5    Schlichting, I.6
  • 31
    • 34247384284 scopus 로고    scopus 로고
    • Identification and biochemical characterization of a novel carotenoid oxygenase: Elucidation of the cleavage step in the Fusarium carotenoid pathway
    • Prado-Cabrero A, Estrada AF, Al-Babili S, &, Avalos J, (2007b) Identification and biochemical characterization of a novel carotenoid oxygenase: elucidation of the cleavage step in the Fusarium carotenoid pathway. Mol Microbiol 64, 448-460.
    • (2007) Mol Microbiol , vol.64 , pp. 448-460
    • Prado-Cabrero, A.1    Estrada, A.F.2    Al-Babili, S.3    Avalos, J.4
  • 32
    • 80053247681 scopus 로고    scopus 로고
    • Cleavage oxygenases for the biosynthesis of trisporoids and other apocarotenoids in Phycomyces
    • Medina HR, Cerdá-Olmedo E, &, Al-Babili S, (2011) Cleavage oxygenases for the biosynthesis of trisporoids and other apocarotenoids in Phycomyces. Mol Microbiol 82, 199-208.
    • (2011) Mol Microbiol , vol.82 , pp. 199-208
    • Medina, H.R.1    Cerdá-Olmedo, E.2    Al-Babili, S.3
  • 36
    • 84895731380 scopus 로고    scopus 로고
    • Aldehyde dehydrogenases in Arabidopsis thaliana: Biochemical requirements, metabolic pathways, and functional analysis
    • Stiti N, Missihoun TD, Kotchoni SO, Kirch H-H, &, Bartels D, (2011) Aldehyde dehydrogenases in Arabidopsis thaliana: biochemical requirements, metabolic pathways, and functional analysis. Front Plant Sci 2, 1-11.
    • (2011) Front Plant Sci , vol.2 , pp. 1-11
    • Stiti, N.1    Missihoun, T.D.2    Kotchoni, S.O.3    Kirch, H.-H.4    Bartels, D.5
  • 37
    • 17744381836 scopus 로고    scopus 로고
    • Detailed expression analysis of selected genes of the aldehyde dehydrogenase (ALDH) gene superfamily in Arabidopsis thaliana
    • Kirch H-H, Schlingensiepen S, Kotchoni S, Sunkar R, &, Bartels D, (2005) Detailed expression analysis of selected genes of the aldehyde dehydrogenase (ALDH) gene superfamily in Arabidopsis thaliana. Plant Mol Biol 57, 315-332.
    • (2005) Plant Mol Biol , vol.57 , pp. 315-332
    • Kirch, H.-H.1    Schlingensiepen, S.2    Kotchoni, S.3    Sunkar, R.4    Bartels, D.5
  • 38
    • 84871888089 scopus 로고    scopus 로고
    • Catalytic properties and reaction mechanism of the CrtO carotenoid ketolase from the cyanobacterium Synechocystis sp. PCC 6803
    • Breitenbach J, Gerjets T, &, Sandmann G, (2013) Catalytic properties and reaction mechanism of the CrtO carotenoid ketolase from the cyanobacterium Synechocystis sp. PCC 6803. Arch Biochem Biophys 529, 86-91.
    • (2013) Arch Biochem Biophys , vol.529 , pp. 86-91
    • Breitenbach, J.1    Gerjets, T.2    Sandmann, G.3
  • 39
    • 27244446652 scopus 로고    scopus 로고
    • Tocopherols protect Synechocystis sp. strain PCC 6803 from lipid peroxidation
    • Maeda H, Sakuragi Y, Bryant DA, &, DellaPenna D, (2005) Tocopherols protect Synechocystis sp. strain PCC 6803 from lipid peroxidation. Plant Physiol 138, 1422-1435.
    • (2005) Plant Physiol , vol.138 , pp. 1422-1435
    • Maeda, H.1    Sakuragi, Y.2    Bryant, D.A.3    Dellapenna, D.4
  • 40
    • 39749124949 scopus 로고    scopus 로고
    • α-tocopherol is essential for acquired chill-light tolerance in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Yang Y, Yin C, Li W, &, Xu X, (2008) α-tocopherol is essential for acquired chill-light tolerance in the cyanobacterium Synechocystis sp. strain PCC 6803. J Bacteriol 190, 1554-1560.
    • (2008) J Bacteriol , vol.190 , pp. 1554-1560
    • Yang, Y.1    Yin, C.2    Li, W.3    Xu, X.4
  • 41
    • 13544267729 scopus 로고    scopus 로고
    • Functional in situ evaluation of photosynthesis-protecting carotenoids in mutants of the cyanobacterium Synechocystis PCC6803
    • Schäfer L, Vioque A, &, Sandmann G, (2005) Functional in situ evaluation of photosynthesis-protecting carotenoids in mutants of the cyanobacterium Synechocystis PCC6803. J Photochem Photobiol, B 78, 195-201.
    • (2005) J Photochem Photobiol, B , vol.78 , pp. 195-201
    • Schäfer, L.1    Vioque, A.2    Sandmann, G.3
  • 42
    • 84870851200 scopus 로고    scopus 로고
    • Microevolution in cyanobacteria: Re-sequencing a motile substrain of Synechocystis sp PCC 6803
    • Trautmann D, Voss B, Wilde A, Al-Babili S, &, Hess WR, (2012) Microevolution in cyanobacteria: re-sequencing a motile substrain of Synechocystis sp PCC 6803. DNA Res 19, 1-14.
    • (2012) DNA Res , vol.19 , pp. 1-14
    • Trautmann, D.1    Voss, B.2    Wilde, A.3    Al-Babili, S.4    Hess, W.R.5
  • 43
    • 0018409915 scopus 로고
    • Generic assignments, strain histories and properties of pure cultures of cyanobacteria
    • Rippka R, Deruelles J, Waterbury JB, Herdman M, &, Stanier RY, (1979) Generic assignments, strain histories and properties of pure cultures of cyanobacteria. Microbiology 111, 1-61.
    • (1979) Microbiology , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3    Herdman, M.4    Stanier, R.Y.5
  • 44
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman SB, &, Wunsch CD, (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 48, 443-453.
    • (1970) J Mol Biol , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 45
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: Multiple sequence alignment with high accuracy and high throughput
    • Edgar RC, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32, 1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 46
    • 0036857358 scopus 로고    scopus 로고
    • QuickTree: Building huge neighbour-joining trees of protein sequences
    • Howe K, Bateman A, &, Durbin R, (2002) QuickTree: building huge neighbour-joining trees of protein sequences. Bioinformatics 18, 1546-1547.
    • (2002) Bioinformatics , vol.18 , pp. 1546-1547
    • Howe, K.1    Bateman, A.2    Durbin, R.3
  • 48
    • 0038392841 scopus 로고    scopus 로고
    • Enzymatic characterization of recombinant mouse retinal dehydrogenase type 1
    • Gagnon I, Duester G, &, Bhat PV, (2003) Enzymatic characterization of recombinant mouse retinal dehydrogenase type 1. Biochem Pharmacol 65, 1685-1690.
    • (2003) Biochem Pharmacol , vol.65 , pp. 1685-1690
    • Gagnon, I.1    Duester, G.2    Bhat, P.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.