메뉴 건너뛰기




Volumn 185, Issue 1, 2003, Pages 20-27

Cinnamate:coenzyme A ligase from the filamentous bacterium Streptomyces coelicolor A3(2)

Author keywords

[No Author keywords available]

Indexed keywords

CAFFEIC ACID; CINNAMATE COENZYME A LIGASE; CINNAMIC ACID; LIGASE; PARA COUMARIC ACID; UNCLASSIFIED DRUG;

EID: 0037216584     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.1.20-27.2003     Document Type: Article
Times cited : (71)

References (29)
  • 2
    • 0025744288 scopus 로고
    • Structural comparison, modes of expression, and putative cis-acting elements of the two 4-coumarate:CoA ligase genes in potato
    • Becker-André, M., P. Schulze-Lefert, and K. Hahlbrock. 1991. Structural comparison, modes of expression, and putative cis-acting elements of the two 4-coumarate:CoA ligase genes in potato. J. Biol. Chem. 266:8551-8559.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8551-8559
    • Becker-André, M.1    Schulze-Lefert, P.2    Hahlbrock, K.3
  • 3
    • 0014760598 scopus 로고
    • Biosynthesis of cinnamide and detection of phenylalanine ammonia-lyase in Streptomyces verticillatus
    • Bezanson, G. S., D. Desaty, A. V. Emes, and L. C. Vining. 1970. Biosynthesis of cinnamide and detection of phenylalanine ammonia-lyase in Streptomyces verticillatus. Can. J. Microbiol. 16:147-151.
    • (1970) Can. J. Microbiol. , vol.16 , pp. 147-151
    • Bezanson, G.S.1    Desaty, D.2    Emes, A.V.3    Vining, L.C.4
  • 4
    • 0034028789 scopus 로고    scopus 로고
    • Lignins and lignification: Selected issues
    • Boudet, A. M. 2000. Lignins and lignification: Selected issues. Plant Physiol. Biochem. 38:81-96.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 81-96
    • Boudet, A.M.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for activation of phenylalanine in the nonribosomal biosynthesis of gramicidin S
    • Conti, E., T. Stachelhaus, M. A. Marahiel, and P. Brick. 1997. Structural basis for activation of phenylalanine in the nonribosomal biosynthesis of gramicidin S. EMBO J. 14:4174-4183.
    • (1997) EMBO J. , vol.14 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 7
    • 0035012053 scopus 로고    scopus 로고
    • Structure and evolution of 4-coumarate:CoA ligase (4CL) gene family
    • Cukovic, D., J. Ehlting, J. A. VanZiffle, and C. J. Douglas. 2001. Structure and evolution of 4-coumarate:CoA ligase (4CL) gene family. Biol. Chem. 382:645-654.
    • (2001) Biol. Chem. , vol.382 , pp. 645-654
    • Cukovic, D.1    Ehlting, J.2    VanZiffle, J.A.3    Douglas, C.J.4
  • 8
    • 0028829961 scopus 로고
    • Stress-induced phenylpropanoid metabolism
    • Dixon, R. A., and N. L. Paiva. 1995. Stress-induced phenylpropanoid metabolism. Plant Cell 7:1085-1097.
    • (1995) Plant Cell , vol.7 , pp. 1085-1097
    • Dixon, R.A.1    Paiva, N.L.2
  • 9
    • 0030157380 scopus 로고    scopus 로고
    • Phenylpropanoid metabolism and lignin biosynthesis: From weeds to trees
    • Douglas, C. J. 1996. Phenylpropanoid metabolism and lignin biosynthesis: From weeds to trees. Trends Plant Sci. 1:171-178.
    • (1996) Trends Plant Sci. , vol.1 , pp. 171-178
    • Douglas, C.J.1
  • 10
    • 0039552100 scopus 로고    scopus 로고
    • Three 4-coumarate:Coenzyme A ligases in Arabidopsis thaliana represent two evolutionarily divergent classes in angiosperms
    • Ehlting, J., D. Büttner, Q. Wang, C. J. Douglas, I. E. Somssich, and E. Kombrink. 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    Büttner, D.2    Wang, Q.3    Douglas, C.J.4    Somssich, I.E.5    Kombrink, E.6
  • 11
    • 0034788886 scopus 로고    scopus 로고
    • Identification of 4-coumarate:Coenzyme A ligase (4CL) substrate recognition domains
    • Ehlting, J., J. J. K. Shin, and C. J. Douglas. 2001. Identification of 4-coumarate:Coenzyme A ligase (4CL) substrate recognition domains. Plant J. 27:455-465.
    • (2001) Plant J. , vol.27 , pp. 455-465
    • Ehlting, J.1    Shin, J.J.K.2    Douglas, C.J.3
  • 12
    • 0014777998 scopus 로고
    • Partial purification and properties of L-phenylalanine ammonia-lyase from Streptomyces verticillatus
    • Emes, A. V., and L. C. Vining. 1970. Partial purification and properties of L-phenylalanine ammonia-lyase from Streptomyces verticillatus. Can. J. Microbiol. 48:613-622.
    • (1970) Can. J. Microbiol. , vol.48 , pp. 613-622
    • Emes, A.V.1    Vining, L.C.2
  • 13
    • 0028054686 scopus 로고
    • The fadD gene of Escherichia coli K-12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family
    • Fulda, M., E. Heinz, and F. P. Wolter. 1994. The fadD gene of Escherichia coli K-12 is located close to rnd at 39.6 min of the chromosomal map and is a new member of the AMP-binding protein family. Mol. Gen. Genet. 242:241-249.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 241-249
    • Fulda, M.1    Heinz, E.2    Wolter, F.P.3
  • 15
    • 0034634672 scopus 로고    scopus 로고
    • A plant-like biosynthesis of benzoyl-CoA in the marine bacterium "Streptomyces maritimus"
    • Hertweck, C., and B. S. Moore. 2000. A plant-like biosynthesis of benzoyl-CoA in the marine bacterium "Streptomyces maritimus." Tetrahedron 56:9115-9120.
    • (2000) Tetrahedron , vol.56 , pp. 9115-9120
    • Hertweck, C.1    Moore, B.S.2
  • 17
    • 0028245937 scopus 로고
    • A-factor as a microbial hormone that controls cellular differentiation and secondary metabolism in Streptomyces griseus
    • Horinouchi, S., and T. Beppu. 1994. A-factor as a microbial hormone that controls cellular differentiation and secondary metabolism in Streptomyces griseus. Mol. Microbiol. 12:859-864.
    • (1994) Mol. Microbiol. , vol.12 , pp. 859-864
    • Horinouchi, S.1    Beppu, T.2
  • 18
    • 0032574720 scopus 로고    scopus 로고
    • Compartmentalized expression of two structurally and functionally distinct 4-coumarate:CoA ligase genes in aspen (Populus tremuloides)
    • Hu, W. J., A. Kawaoka, C. J. Tsai, J. H. Lung, K. Osakabe, H. Ebinuma, and V. L. Chiang. 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.H.4    Osakabe, K.5    Ebinuma, H.6    Chiang, V.L.7
  • 19
    • 0016630210 scopus 로고
    • Isoenzymes ofp-coumarate:CoA ligase from cell suspension cultures of Glycine max
    • Knobloch, K. H., and K. Hahlbrock. 1975. Isoenzymes ofp-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
  • 20
    • 0017747551 scopus 로고
    • 4-Coumarate:CoA ligase from cell suspension cultures of Petroselinum hortense Hoffm
    • Knobloch, K. H., and K. Hahlbrock. 1977. 4-Coumarate:CoA ligase from cell suspension cultures of Petroselinum hortense Hoffm. Arch. Biochem. Biophys. 184:237-248.
    • (1977) Arch. Biochem. Biophys. , vol.184 , pp. 237-248
    • Knobloch, K.H.1    Hahlbrock, K.2
  • 21
    • 0000796426 scopus 로고
    • Distribution and roles of p-hydroxycinnamate:CoA ligase in lignin biosynthesis
    • Kutsuki, H., M. Shimada, and T. Higuchi. 1981. Distribution and roles of p-hydroxycinnamate:CoA ligase in lignin biosynthesis. Phytochemistry 21:267-271.
    • (1981) Phytochemistry , vol.21 , pp. 267-271
    • Kutsuki, H.1    Shimada, M.2    Higuchi, T.3
  • 22
    • 0034521526 scopus 로고    scopus 로고
    • Cloning, sequencing and analysis of the enterosin biosynthesis gene cluster from the marine isolate "Streptomyces maritimus": Evidence for the derailment of an aromatic polyketide synthase
    • Piel, J., C. Hertweck, P. R. Shipley, D. M. Hunt, M. S. Newman, and B. S. Moore. 2000. Cloning, sequencing and analysis of the enterosin biosynthesis gene cluster from the marine isolate "Streptomyces maritimus": Evidence for the derailment of an aromatic polyketide synthase. Chem. Biol. 7:943-955.
    • (2000) Chem. Biol. , vol.7 , pp. 943-955
    • Piel, J.1    Hertweck, C.2    Shipley, P.R.3    Hunt, D.M.4    Newman, M.S.5    Moore, B.S.6
  • 24
    • 0016736883 scopus 로고
    • Chemical synthesis and properties of hydroxycinnamoyl-coenzyme A derivatives
    • Stöckigt, J., and M. H. Zenk. 1975. Chemical synthesis and properties of hydroxycinnamoyl-coenzyme A derivatives. Z. Naturforsch. 30c:352-358.
    • (1975) Z. Naturforsch. , vol.30 C , pp. 352-358
    • Stöckigt, J.1    Zenk, M.H.2
  • 25
    • 17544396621 scopus 로고    scopus 로고
    • Mutational analysis of 4-coumarate:CoA ligase identifies functionally important amino acids and verifies its close relationship to other adenylate-forming enzymes
    • Stuible, H. P., D. Büttner, J. Ehlting, K. Hahlbrock, and E. Kombrink. 2000. Mutational analysis of 4-coumarate:CoA ligase identifies functionally important amino acids and verifies its close relationship to other adenylate-forming enzymes. FEBS Lett. 467:117-122.
    • (2000) FEBS Lett. , vol.467 , pp. 117-122
    • Stuible, H.P.1    Büttner, D.2    Ehlting, J.3    Hahlbrock, K.4    Kombrink, E.5
  • 26
    • 0035920183 scopus 로고    scopus 로고
    • Identification of the substrate specificity-conferring amino acid residues of 4-coumarate:Coenzyme A ligase allows the rational design of mutant enzymes with new catalytic properties
    • Stuible, H. P., and E. Kombrink. 2001. Identification of the substrate specificity-conferring amino acid residues of 4-coumarate:Coenzyme A ligase allows the rational design of mutant enzymes with new catalytic properties. J. Biol. Chem. 276:26893-26897.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26893-26897
    • Stuible, H.P.1    Kombrink, E.2
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 28
    • 0027639644 scopus 로고
    • Molecular cloning and expression of 4-coumarate:Coenzyme A ligase, an enzyme involved in the resistance of soybean (Glycine max) against pathogen infection
    • Uhlmann, A., and J. Ebel. 1993. Molecular cloning and expression of 4-coumarate:Coenzyme A ligase, an enzyme involved in the resistance of soybean (Glycine max) against pathogen infection. Plant Physiol. 102:1147-1156.
    • (1993) Plant Physiol. , vol.102 , pp. 1147-1156
    • Uhlmann, A.1    Ebel, J.2
  • 29
    • 0032082930 scopus 로고    scopus 로고
    • Phenylpropanoid biosynthesis and its regulation
    • Weisshaar, B., and G. I. Jenkins. 1998. Phenylpropanoid biosynthesis and its regulation. Curr. Opin. Plant Biol. 1:251-257.
    • (1998) Curr. Opin. Plant Biol. , vol.1 , pp. 251-257
    • Weisshaar, B.1    Jenkins, G.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.