메뉴 건너뛰기




Volumn 585, Issue 6, 2011, Pages 893-898

Aminoacyl-coenzyme A synthesis catalyzed by a CoA ligase from Penicillium chrysogenum

Author keywords

Phenylalanine; Aminoacyl coenzyme A; Coenzyme A ligase; Penicillium chrysogenum

Indexed keywords

AMINOACYL COENZYME A; COENZYME A; LONG CHAIN FATTY ACID COENZYME A LIGASE; PHENYLALANINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 79952574775     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.02.018     Document Type: Article
Times cited : (7)

References (29)
  • 1
    • 0029416813 scopus 로고
    • Beta-oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress
    • Kunau, W.H., Dommes, V. and Schulz, H. (1995) Beta-oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress. Prog. Lipid. Res. 34, 267-342.
    • (1995) Prog. Lipid. Res. , vol.34 , pp. 267-342
    • Kunau, W.H.1    Dommes, V.2    Schulz, H.3
  • 2
    • 0036798592 scopus 로고    scopus 로고
    • Trends in lignin modification: A comprehensive analysis of the effects of genetic manipulations/mutations on lignification and vascular integrity
    • DOI 10.1016/S0031-9422(02)00211-X, PII S003194220200211X
    • Anterola, A.M. and Lewis, N.G. (2002) Trends in lignin modification: a comprehensive analysis of the effects of genetic manipulations/mutations on lignification and vascular integrity. Phytochemistry 61, 221-294. (Pubitemid 35189560)
    • (2002) Phytochemistry , vol.61 , Issue.3 , pp. 221-294
    • Anterola, A.M.1    Lewis, N.G.2
  • 4
    • 0034232476 scopus 로고    scopus 로고
    • Xenobiotic-CoA ligases: Kinetic and molecular characterization
    • Knights, K.M. and Drogemuller, C.J. (2000) Xenobiotic-CoA ligases: kinetic and molecular characterization. Curr. Drug Metab. 1, 49-66.
    • (2000) Curr. Drug Metab. , vol.1 , pp. 49-66
    • Knights, K.M.1    Drogemuller, C.J.2
  • 5
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S
    • DOI 10.1093/emboj/16.14.4174
    • Conti, E., Stachelhaus, T., Marahiel, M.A. and Brick, P. (1997) Structural basis for the activation of phenylalanine in the non-ribosomal biosynthesis of gramicidin S. EMBO J. 16, 4174-4183. (Pubitemid 27298170)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 6
    • 0032515953 scopus 로고    scopus 로고
    • Aminoacylation of coenzyme A and pantetheine by aminoacyl-tRNA synthetases: Possible link between noncoded and coded peptide synthesis
    • Jakubowski, H. (1998) Aminoacylation of coenzyme A and pantetheine by aminoacyl-tRNA synthetases: possible link between noncoded and coded peptide synthesis. Biochemistry 37, 5147-5153.
    • (1998) Biochemistry , vol.37 , pp. 5147-5153
    • Jakubowski, H.1
  • 7
    • 33847112437 scopus 로고    scopus 로고
    • Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains
    • DOI 10.1016/j.febslet.2007.01.066, PII S0014579307001135
    • Linne, U., Schäfer, A., Stubbs, M.T. and Marahiel, M.A. (2007) Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains. FEBS Lett. 581, 905-910. (Pubitemid 46282721)
    • (2007) FEBS Letters , vol.581 , Issue.5 , pp. 905-910
    • Linne, U.1    Schafer, A.2    Stubbs, M.T.3    Marahiel, M.A.4
  • 8
    • 0037195848 scopus 로고    scopus 로고
    • A novel epimerization system in fungal secondary metabolism involved in the conversion of isopenicillin N into penicillin N in Acremonium chrysogenum
    • Ullan, R.V., Casqueiro, J., Banuelos, O., Fernandez, F.J., Gutierrez, S. and Martin, J.F. (2002) A novel epimerization system in fungal secondary metabolism involved in the conversion of isopenicillin N into penicillin N in Acremonium chrysogenum. J. Biol. Chem. 277, 46216-46225.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46216-46225
    • Ullan, R.V.1    Casqueiro, J.2    Banuelos, O.3    Fernandez, F.J.4    Gutierrez, S.5    Martin, J.F.6
  • 10
    • 0026768020 scopus 로고
    • Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum: Involvement of this enzyme in the biosynthesis of penicillins
    • Martinez-Blanco, H., Reglero, A., Fernandez-Valverde, M., Ferrero, M.A., Moreno, M.A., Penalva, M.A. and Luengo, J.M. (1992) Isolation and characterization of the acetyl-CoA synthetase from Penicillium chrysogenum: involvement of this enzyme in the biosynthesis of penicillins. J. Biol. Chem. 267, 5474-5481.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5474-5481
    • Martinez-Blanco, H.1    Reglero, A.2    Fernandez-Valverde, M.3    Ferrero, M.A.4    Moreno, M.A.5    Penalva, M.A.6    Luengo, J.M.7
  • 11
    • 12844252572 scopus 로고    scopus 로고
    • Overproduction of a single protein, Pc-Pex11p, results in 2-fold enhanced penicillin production by Penicillium chrysogenum
    • Kiel, J.A.K.W., van der Klei, I.J., van den Berg, M.A., Bovenberg, R.A.L. and Veenhuis, M. (2005) Overproduction of a single protein, Pc-Pex11p, results in 2-fold enhanced penicillin production by Penicillium chrysogenum. Fungal Genet. Biol. 42, 154-164.
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 154-164
    • Kiel, J.A.K.W.1    Van Der Klei, I.J.2    Van Den Berg, M.A.3    Bovenberg, R.A.L.4    Veenhuis, M.5
  • 12
    • 34547122265 scopus 로고    scopus 로고
    • Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolor
    • Heuts, D.P.H.M., van Hellemond, E.W., Janssen, D.B. and Fraaije, M.W. (2007) Discovery, characterization, and kinetic analysis of an alditol oxidase from Streptomyces coelicolor. J. Biol. Chem. 282, 20283-20291.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20283-20291
    • Heuts, D.P.H.M.1    Van Hellemond, E.W.2    Janssen, D.B.3    Fraaije, M.W.4
  • 14
    • 18144366554 scopus 로고    scopus 로고
    • LC/MS/MS method for quantitative determination of long-chain fatty acyl-CoAs
    • Magnes, C., Sinner, F.M., Regittnig, W. and Pieber, T.R. (2005) LC/MS/MS method for quantitative determination of long-chain fatty acyl-CoAs. Anal. Chem. 77, 2889-2894.
    • (2005) Anal. Chem. , vol.77 , pp. 2889-2894
    • Magnes, C.1    Sinner, F.M.2    Regittnig, W.3    Pieber, T.R.4
  • 15
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold, K., Bordoli, L. and Schwede, T. (2006) The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201. (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 16
    • 77954293798 scopus 로고    scopus 로고
    • CPHmodels-3.0 - Remote homology modeling using structure guided sequence profiles
    • Nielsen, M., Lundegaard, C., Lund, O. and Petersen, T.N. (2010) CPHmodels-3.0 - remote homology modeling using structure guided sequence profiles. Nucleic Acids Res. 38, W576-581.
    • (2010) Nucleic Acids Res. , vol.38
    • Nielsen, M.1    Lundegaard, C.2    Lund, O.3    Petersen, T.N.4
  • 17
    • 74249090260 scopus 로고    scopus 로고
    • Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: Four approaches that performed well in CASP8
    • Krieger, E., Joo, K., Lee, J., Lee, J., Raman, S., Thompson, J., Tyka, M., Baker, D. and Karplus, K. (2009) Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8. Proteins 77, 114-122.
    • (2009) Proteins , vol.77 , pp. 114-122
    • Krieger, E.1    Joo, K.2    Lee, J.3    Lee, J.4    Raman, S.5    Thompson, J.6    Tyka, M.7    Baker, D.8    Karplus, K.9
  • 20
    • 0031784872 scopus 로고    scopus 로고
    • Structural basis for the inhibition of firefly luciferase by a general anesthetic
    • Franks, N.P., Jenkins, A., Conti, E., Lieb, W.R. and Brick, P. (1998) Structural basis for the inhibition of firefly luciferase by a general anesthetic. Biophys. J. 75, 2205-2211. (Pubitemid 28492103)
    • (1998) Biophysical Journal , vol.75 , Issue.5 , pp. 2205-2211
    • Franks, N.P.1    Jenkins, A.2    Conti, E.3    Lieb, W.R.4    Brick, P.5
  • 21
    • 78049459077 scopus 로고    scopus 로고
    • Crystal structures of a Populus tomentosa 4-coumarate:CoA ligase shed light on its enzymatic mechanisms
    • Hu, Y., Gai, Y., Yin, L., Wang, X., Feng, C., Feng, L., Li, D., Jiang, X.N. and Wang, D.C. (2010) Crystal structures of a Populus tomentosa 4-coumarate:CoA ligase shed light on its enzymatic mechanisms. Plant Cell 22, 3093-3104.
    • (2010) Plant Cell , vol.22 , pp. 3093-3104
    • Hu, Y.1    Gai, Y.2    Yin, L.3    Wang, X.4    Feng, C.5    Feng, L.6    Li, D.7    Jiang, X.N.8    Wang, D.C.9
  • 22
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function
    • Morris, G.M., Goodsell, D.S., Haliday, R.S., Huey, R., Hart, W.E., Belew, R.K. and Olson, A.J. (1998) Automated docking using a Lamarckian genetic algorithm and empirical binding free energy function. J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Haliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 23
    • 0034634466 scopus 로고    scopus 로고
    • Amino acid selectivity in the aminoacylation of coenzyme A and RNA minihelices by aminoacyl-tRNA synthetases
    • Jakubowski, H. (2000) Amino acid selectivity in the aminoacylation of coenzyme A and RNA minihelices by aminoacyl-tRNA synthetases. J. Biol. Chem. 275, 34845-34848.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34845-34848
    • Jakubowski, H.1
  • 24
    • 0035861070 scopus 로고    scopus 로고
    • Substrate recognition and selection by the initiation module PheATE of gramicidin S synthetase
    • Luo, L., Burkart, M.D., Stachelhaus, T. and Walsh, C.T. (2001) Substrate recognition and selection by the initiation module PheATE of gramicidin S synthetase. J. Am. Chem. Soc. 123, 11208-11218.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11208-11218
    • Luo, L.1    Burkart, M.D.2    Stachelhaus, T.3    Walsh, C.T.4
  • 25
    • 10644277147 scopus 로고    scopus 로고
    • Post-transfer editing in vitro and in vivo by the β subunit of phenylalanyl-tRNA synthetase
    • DOI 10.1038/sj.emboj.7600474
    • Roy, H., Ling, J., Irnov, M. and Ibba, M. (2004) Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase. EMBO J. 23, 4639-4648. (Pubitemid 39657863)
    • (2004) EMBO Journal , vol.23 , Issue.23 , pp. 4639-4648
    • Roy, H.1    Ling, J.2    Irnov, M.3    Ibba, M.4
  • 26
    • 33644677385 scopus 로고    scopus 로고
    • Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase
    • Roy, H., Ling, J., Alfonzo, J. and Ibba, M. (2005) Loss of editing activity during the evolution of mitochondrial phenylalanyl-tRNA synthetase. J. Biol. Chem. 280, 38186-38192.
    • (2005) J. Biol. Chem. , vol.280 , pp. 38186-38192
    • Roy, H.1    Ling, J.2    Alfonzo, J.3    Ibba, M.4
  • 27
    • 0036789932 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of the C-13 phenylpropanoid side chain-CoA acyltransferase that functions in Taxol biosynthesis
    • Walker, K., Fujisaki, S., Long, R. and Croteau, R. (2002) Molecular cloning and heterologous expression of the C-13 phenylpropanoid side chain-CoA acyltransferase that functions in Taxol biosynthesis. Proc. Natl. Acad. Sci. USA 99, 12715-12720.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12715-12720
    • Walker, K.1    Fujisaki, S.2    Long, R.3    Croteau, R.4
  • 28
    • 13444263419 scopus 로고    scopus 로고
    • Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum
    • DOI 10.1111/j.1742-4658.2004.04518.x
    • Herrmann, G., Selmer, T., Jessen, H.J., Gokarn, R.R., Selifonova, O., Gort, S.J. and Buckel, W. (2005) Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum. FEBS J. 272, 813-821. (Pubitemid 40208883)
    • (2005) FEBS Journal , vol.272 , Issue.3 , pp. 813-821
    • Herrmann, G.1    Seimer, T.2    Jessen, H.J.3    Gokarn, R.R.4    Selifonova, O.5    Gort, S.J.6    Buckel, W.7
  • 29
    • 0033574774 scopus 로고    scopus 로고
    • Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis
    • DOI 10.1126/science.284.5413.486
    • Belshaw, P.J., Walsh, C.T. and Stachelhaus, T. (1999) Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. Science 284, 486-489. (Pubitemid 29289621)
    • (1999) Science , vol.284 , Issue.5413 , pp. 486-489
    • Belshaw, P.J.1    Walsh, C.T.2    Stachelhaus, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.