메뉴 건너뛰기




Volumn 117, Issue 4, 2004, Pages 303-310

4-Coumarate: Coenzyme a ligase in black locust (Robinia pseudoacacia) catalyses the conversion of sinapate to sinapoyl-CoA

Author keywords

4 Coumarate:coenzyme A ligase (4CL); Lignin biosynthesis; Robinia pseudoacacia L.; Sinapate; Syringyl lignin

Indexed keywords

4 COUMARATE COA LIGASE; 4-COUMARATE-COA LIGASE; ACYL COENZYME A; COUMARIC ACID; ISOENZYME; LIGNIN; LONG CHAIN FATTY ACID COENZYME A LIGASE; SINAPIC ACID; SINAPOYL COENZYME A; SINAPOYL-COENZYME A;

EID: 5444257490     PISSN: 09189440     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10265-004-0159-1     Document Type: Article
Times cited : (19)

References (29)
  • 1
    • 0031990783 scopus 로고    scopus 로고
    • 4-Coumarate: Coenzyme A ligase in hybrid poplar. Properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes
    • Allina SM, Pri-Hadash A, Theilmann DA, Ellis BE, Douglas CJ (1998) 4-Coumarate: coenzyme A ligase in hybrid poplar. Properties of native enzymes, cDNA cloning, and analysis of recombinant enzymes. Plant Physiol 116:743-754
    • (1998) Plant Physiol , vol.116 , pp. 743-754
    • Allina, S.M.1    Pri-Hadash, A.2    Theilmann, D.A.3    Ellis, B.E.4    Douglas, C.J.5
  • 2
    • 0033064130 scopus 로고    scopus 로고
    • Evidence for a novel biosynthetic pathway that regulates the ratio of syringyl to guaiacyl residues in lignin in the differentiating xylem of Magnolia kobus DC
    • Chen F, Yasuda S, Fukushima K (1999) Evidence for a novel biosynthetic pathway that regulates the ratio of syringyl to guaiacyl residues in lignin in the differentiating xylem of Magnolia kobus DC. Planta 207:597-603
    • (1999) Planta , vol.207 , pp. 597-603
    • Chen, F.1    Yasuda, S.2    Fukushima, K.3
  • 3
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate: Coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • Ehlting J, Buttner D, Wang Q, Douglas CJ, Somssich IE, Kombrink E (1999) Three 4-coumarate: coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms. Plant J 19:9-20
    • (1999) Plant J , vol.19 , pp. 9-20
    • Ehlting, J.1    Buttner, D.2    Wang, Q.3    Douglas, C.J.4    Somssich, I.E.5    Kombrink, E.6
  • 4
    • 0001051111 scopus 로고
    • Isoenzymes of hydroxycin-namate:CoA ligase from poplar stems, properties, and tissue distribution
    • Grand C, Boudet A, Boudet AM (1983) Isoenzymes of hydroxycin-namate:CoA ligase from poplar stems, properties, and tissue distribution. Planta 159:225-229
    • (1983) Planta , vol.159 , pp. 225-229
    • Grand, C.1    Boudet, A.2    Boudet, A.M.3
  • 5
    • 0142134965 scopus 로고    scopus 로고
    • Treatment of poplar callus with ferulic and sinapic acids I: Incorporation and enhancement of lignin biosynthesis
    • Hamada K, Ysutsumi Y, Yamauchi K, Fukushima K, Nishida T (2003a) Treatment of poplar callus with ferulic and sinapic acids I: Incorporation and enhancement of lignin biosynthesis. J Wood Sci 49:333-338
    • (2003) J Wood Sci , vol.49 , pp. 333-338
    • Hamada, K.1    Ysutsumi, Y.2    Yamauchi, K.3    Fukushima, K.4    Nishida, T.5
  • 6
    • 0142103234 scopus 로고    scopus 로고
    • Treatment of poplar callus with ferulic and sinapic acids. II: Lignin biosynthesis and its related enzyme
    • Hamada K, Ysutsumi Y, Nishida T (2003b) Treatment of poplar callus with ferulic and sinapic acids. II: Lignin biosynthesis and its related enzyme. J Wood Sci 49:366-370
    • (2003) J Wood Sci , vol.49 , pp. 366-370
    • Hamada, K.1    Ysutsumi, Y.2    Nishida, T.3
  • 7
    • 85047681876 scopus 로고    scopus 로고
    • Differential substrate inhibition couples kinetically distinct 4-coumarate: Conezyme A ligases with spatially distinct metabolic roles in quaking aspen
    • Harding SA, Leshkeich J, Chiang VL, Tsai CJ (2002) Differential substrate inhibition couples kinetically distinct 4-coumarate: conezyme A ligases with spatially distinct metabolic roles in quaking aspen. Plant Physiol 128:428-438
    • (2002) Plant Physiol , vol.128 , pp. 428-438
    • Harding, S.A.1    Leshkeich, J.2    Chiang, V.L.3    Tsai, C.J.4
  • 8
    • 0032574720 scopus 로고    scopus 로고
    • Compartmentalized expression of two structurally and functionally distinct 4-coumarate: CoA ligase genes in aspen (Populus tremuloides)
    • Hu WJ, Kawaoka A, Tsai CJ, Lung J, Osakabe K, Ebinuma H, Chiang VL (1998) Compartmentalized expression of two structurally and functionally distinct 4-coumarate: CoA ligase genes in aspen (Populus tremuloides). Proc Natl Acad Sci USA 95:5407-5412
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5407-5412
    • Hu, W.J.1    Kawaoka, A.2    Tsai, C.J.3    Lung, J.4    Osakabe, K.5    Ebinuma, H.6    Chiang, V.L.7
  • 9
    • 0033621061 scopus 로고    scopus 로고
    • New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent monooxygenase
    • Humphreys JM, Hemm MR, Chapple C (1999) New routes for lignin biosynthesis defined by biochemical characterization of recombinant ferulate 5-hydroxylase, a multifunctional cytochrome P450-dependent monooxygenase. Proc Natl Acad Sci USA 96:10045-10050
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10045-10050
    • Humphreys, J.M.1    Hemm, M.R.2    Chapple, C.3
  • 10
    • 0016630210 scopus 로고
    • Isoenzymes of p-coumarate: CoA ligase from cell suspension cultures of Glycine max
    • Knobloch KH, Hahlbrock K (1975) Isoenzymes of p-coumarate: CoA ligase from cell suspension cultures of Glycine max. Eur J Biochem 52:311-320
    • (1975) Eur J Biochem , vol.52 , pp. 311-320
    • Knobloch, K.H.1    Hahlbrock, K.2
  • 11
    • 0017747551 scopus 로고
    • 4-Coumarate: CoA ligase from cell suspension cultures of Petroselinum hortense Hoffm. Partial purification, substrate specificity, and further properties
    • Knobloch KH, Hahlbrock K (1977) 4-Coumarate: CoA ligase from cell suspension cultures of Petroselinum hortense Hoffm. Partial purification, substrate specificity, and further properties. Arch Biochem Biophys 184:237-248
    • (1977) Arch Biochem Biophys , vol.184 , pp. 237-248
    • Knobloch, K.H.1    Hahlbrock, K.2
  • 12
    • 0000796426 scopus 로고
    • Distribution and roles of p-hydroxycinnamate: CoA ligase in lignin biosynthesis
    • Kutsuki H, Shimada M, Higuchi T (1982) Distribution and roles of p-hydroxycinnamate: CoA ligase in lignin biosynthesis. Phytochem 21:267-271
    • (1982) Phytochem , vol.21 , pp. 267-271
    • Kutsuki, H.1    Shimada, M.2    Higuchi, T.3
  • 13
    • 0022076238 scopus 로고
    • Thioacidolysis of lignin: Comparison with acidolysis
    • Lapierre C, Monties B, Roland C (1985) Thioacidolysis of lignin: comparison with acidolysis. J Wood Chem Technol 5:277-292
    • (1985) J Wood Chem Technol , vol.5 , pp. 277-292
    • Lapierre, C.1    Monties, B.2    Roland, C.3
  • 14
    • 0030250380 scopus 로고    scopus 로고
    • Two divergent members of a tobacco 4-coumarate: Coenzyme A ligase (4CL) gene family. cDNA structure, gene inheritance and expression, and properties of recombinant proteins
    • Lee D, Douglas CJ (1996) Two divergent members of a tobacco 4-coumarate: coenzyme A ligase (4CL) gene family. cDNA structure, gene inheritance and expression, and properties of recombinant proteins. Plant Physiol 112:193-205
    • (1996) Plant Physiol , vol.112 , pp. 193-205
    • Lee, D.1    Douglas, C.J.2
  • 15
    • 0029346985 scopus 로고
    • The Arabidopsis thaliana 4-coumarate: CoA ligase (4CL) gene: Stress and developmentally regulated expression and nucleotide sequence of its cDNA
    • Lee D, Ellard M, Wanner LA, Davis KR, Douglas CJ (1995) The Arabidopsis thaliana 4-coumarate: CoA ligase (4CL) gene: stress and developmentally regulated expression and nucleotide sequence of its cDNA. Plant Mol Biol 28:871-884
    • (1995) Plant Mol Biol , vol.28 , pp. 871-884
    • Lee, D.1    Ellard, M.2    Wanner, L.A.3    Davis, K.R.4    Douglas, C.J.5
  • 16
    • 0031277875 scopus 로고    scopus 로고
    • Antisense suppression of 4-coumarate: Coenzyme A ligase activity in Arabidopsis leads to altered lignin subunit composition
    • Lee D, Meyer K, Chapple C, Douglas CJ (1997) Antisense suppression of 4-coumarate: coenzyme A ligase activity in Arabidopsis leads to altered lignin subunit composition. Plant Cell 9:1985-1998
    • (1997) Plant Cell , vol.9 , pp. 1985-1998
    • Lee, D.1    Meyer, K.2    Chapple, C.3    Douglas, C.J.4
  • 17
    • 0034054073 scopus 로고    scopus 로고
    • 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms
    • Li L, Popko JL, Umezawa T, Chiang VL (2000) 5-Hydroxyconiferyl aldehyde modulates enzymatic methylation for syringyl monolignol formation, a new view of monolignol biosynthesis in angiosperms. J Biol Chem 275:6537-6545
    • (2000) J Biol Chem , vol.275 , pp. 6537-6545
    • Li, L.1    Popko, J.L.2    Umezawa, T.3    Chiang, V.L.4
  • 18
    • 0036179613 scopus 로고    scopus 로고
    • Divergent members of a soybean (Glycine max L.) 4-coumarate: Coenzyme A ligase gene family. Primary structures, catalytic properties, and differential expression
    • Lindermayr C, Mollers B, Fliegmann J, Uhlmann A, Lottspeich F, Meimberg H, Ebel J (2002) Divergent members of a soybean (Glycine max L.) 4-coumarate: coenzyme A ligase gene family. Primary structures, catalytic properties, and differential expression. Eur J Biochem 269:1304-1315
    • (2002) Eur J Biochem , vol.269 , pp. 1304-1315
    • Lindermayr, C.1    Mollers, B.2    Fliegmann, J.3    Uhlmann, A.4    Lottspeich, F.5    Meimberg, H.6    Ebel, J.7
  • 19
    • 0024094402 scopus 로고    scopus 로고
    • Primary structures and catalytic properties of isoenzymes encoded by the two 4-coumarate-CoA ligase genes in parsley
    • Lozoya E, Hoffmann H, Douglas C, Schulz W, Scheel D, Hahlbrock K (1998) Primary structures and catalytic properties of isoenzymes encoded by the two 4-coumarate-CoA ligase genes in parsley. Eur J Biochem 176(3):661-667
    • (1998) Eur J Biochem , vol.176 , Issue.3 , pp. 661-667
    • Lozoya, E.1    Hoffmann, H.2    Douglas, C.3    Schulz, W.4    Scheel, D.5    Hahlbrock, K.6
  • 21
    • 0034015731 scopus 로고    scopus 로고
    • Conversion of guaiacyl to syringyl moieties on the cinnamyl alcohol pathway during the biosynthesis of lignin in angiosperms
    • Matsui N, Chen F, Yasuda S, Fukushima K (2000) Conversion of guaiacyl to syringyl moieties on the cinnamyl alcohol pathway during the biosynthesis of lignin in angiosperms. Planta 210:831-835
    • (2000) Planta , vol.210 , pp. 831-835
    • Matsui, N.1    Chen, F.2    Yasuda, S.3    Fukushima, K.4
  • 22
    • 0012961014 scopus 로고
    • Preparation of caffeic and dihydrocaffeic acids by methods suitable for introduction of C14 into the β-position1
    • Neish AC (1959) Preparation of caffeic and dihydrocaffeic acids by methods suitable for introduction of C14 into the β-position1. Can J Biochem Physiol 37:1431-1438
    • (1959) Can J Biochem Physiol , vol.37 , pp. 1431-1438
    • Neish, A.C.1
  • 25
    • 0016736883 scopus 로고
    • Chemical syntheses and properties of hydroxycinnamoyl-coenzyme A derivatives
    • Stockigt J, Zenk MH (1975) Chemical syntheses and properties of hydroxycinnamoyl-coenzyme A derivatives. Z Naturforsch 30c:352-358
    • (1975) Z Naturforsch , vol.30 C , pp. 352-358
    • Stockigt, J.1    Zenk, M.H.2
  • 26
    • 0029294602 scopus 로고
    • 4-Coumarate-coenzyme-a ligase from loblolly-pine xylem - Isolation, characterization, and complementary-DNA cloning
    • Voo KS, Whetten RW, Omalley DM, Sederoff RR (1995) 4-Coumarate-coenzyme-a ligase from loblolly-pine xylem - Isolation, characterization, and complementary-DNA cloning. Plant Physiol 108(1):85-97
    • (1995) Plant Physiol , vol.108 , Issue.1 , pp. 85-97
    • Voo, K.S.1    Whetten, R.W.2    Omalley, D.M.3    Sederoff, R.R.4
  • 27
    • 0037157054 scopus 로고    scopus 로고
    • Evidence for the biosynthetic pathway from sinapic acid to syringyl lignin using labeled sinapic acid with stable isotope at both methoxy groups in Robinia pseudoacacia and Nerium indicum
    • Yamauchi K, Yasuda S, Fukushima K (2002) Evidence for the biosynthetic pathway from sinapic acid to syringyl lignin using labeled sinapic acid with stable isotope at both methoxy groups in Robinia pseudoacacia and Nerium indicum. J Agric Food Chem 50:3222-3227
    • (2002) J Agric Food Chem , vol.50 , pp. 3222-3227
    • Yamauchi, K.1    Yasuda, S.2    Fukushima, K.3
  • 28
    • 0037837461 scopus 로고    scopus 로고
    • Multiform biosynthetic pathway of syringyl lignin in angiosperms
    • Yamauchi K, Yasuda S, Hamada K, Tsutsumi Y, Fukushima K (2003) Multiform biosynthetic pathway of syringyl lignin in angiosperms. Planta 216(3):496-501
    • (2003) Planta , vol.216 , Issue.3 , pp. 496-501
    • Yamauchi, K.1    Yasuda, S.2    Hamada, K.3    Tsutsumi, Y.4    Fukushima, K.5
  • 29
    • 0031040101 scopus 로고    scopus 로고
    • Molecular cloning of 4-coumarate: Coenzyme A ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood
    • Zhang XH, Chiang VL (1997) Molecular cloning of 4-coumarate: coenzyme A ligase in loblolly pine and the roles of this enzyme in the biosynthesis of lignin in compression wood. Plant Physiol 113:65-74
    • (1997) Plant Physiol , vol.113 , pp. 65-74
    • Zhang, X.H.1    Chiang, V.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.