메뉴 건너뛰기




Volumn 386, Issue 1, 2005, Pages 169-176

Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase

Author keywords

Computer modelling; Prenyltransferase; Product specificity; Site directed mutagenesis; Substrate specificity; Undecaprenyl pyrophosphate synthase

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; CONDENSATION REACTIONS; CRYSTAL STRUCTURE; DISSOCIATION; ESCHERICHIA COLI; HYDROCARBONS; HYDROPHOBICITY; LIPIDS; RATE CONSTANTS; SUBSTRATES;

EID: 14244265227     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040785     Document Type: Article
Times cited : (23)

References (25)
  • 1
    • 0036375597 scopus 로고    scopus 로고
    • Structure, mechanism and function of prenyltransferases
    • Liang, P. H., Ko, T. P. and Wang, A. H.-J. (2002) Structure, mechanism and function of prenyltransferases. Eur. J. Biochem. 269, 3339-3354
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3339-3354
    • Liang, P.H.1    Ko, T.P.2    Wang, A.H.-J.3
  • 3
    • 0000680126 scopus 로고
    • Prenyl transferases and isomerase
    • (Porter, J. W. and Spurgeon, S. L., eds.), Chapter 4, John Wiley & Sons, New York
    • Poulter, C. D. and Rilling, H. C. (1982) Prenyl transferases and isomerase. In Biosynthesis of Isoprenoid Compounds, vol. 1 (Porter, J. W. and Spurgeon, S. L., eds.), Chapter 4, pp. 161-224, John Wiley & Sons, New York
    • (1982) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 161-224
    • Poulter, C.D.1    Rilling, H.C.2
  • 4
    • 11544324496 scopus 로고    scopus 로고
    • Enzymatic aspects of isoprenoid chain elongation
    • Ogura, K. and Koyama, T. (1998) Enzymatic aspects of isoprenoid chain elongation. Chem. Rev. 98, 1263-1276
    • (1998) Chem. Rev. , vol.98 , pp. 1263-1276
    • Ogura, K.1    Koyama, T.2
  • 5
    • 0028269724 scopus 로고
    • Isoprenyl diphosphate synthases: Protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure
    • Chen, A., Kroon, P. A. and Poulter, C. D. (1994) Isoprenyl diphosphate synthases: protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure. Protein Sci. 3, 600-607
    • (1994) Protein Sci. , vol.3 , pp. 600-607
    • Chen, A.1    Kroon, P.A.2    Poulter, C.D.3
  • 7
    • 1042301374 scopus 로고    scopus 로고
    • Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination
    • Guo, R. T., Kuo, C. J., Chou, C. C., Ko, T. P., Shr, H. L., Liang, P. H. and Wang, A. H.-J. (2004) Crystal structure of octaprenyl pyrophosphate synthase from hyperthermophilic Thermotoga maritima and mechanism of product chain length determination. J. Biol. Chem. 279, 4903-4912
    • (2004) J. Biol. Chem. , vol.279 , pp. 4903-4912
    • Guo, R.T.1    Kuo, C.J.2    Chou, C.C.3    Ko, T.P.4    Shr, H.L.5    Liang, P.H.6    Wang, A.H.-J.7
  • 8
    • 0036510754 scopus 로고    scopus 로고
    • Probing the conformational change of Escherichia coli undecaprenyl pyrophosphate synthase during catalysis using an inhibitor and tryptophan mutants
    • Chen, Y. H., Chen, A. P.-C., Chen, C.-T., Wang, A. H.-J. and Liang, P. H. (2002) Probing the conformational change of Escherichia coli undecaprenyl pyrophosphate synthase during catalysis using an inhibitor and tryptophan mutants. J. Biol. Chem. 277, 7369-7376
    • (2002) J. Biol. Chem. , vol.277 , pp. 7369-7376
    • Chen, Y.H.1    Chen, A.P.-C.2    Chen, C.-T.3    Wang, A.H.-J.4    Liang, P.H.5
  • 9
    • 0041705990 scopus 로고    scopus 로고
    • Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and Triton
    • Chang, S. Y., Ko, T. P., Liang, P. H. and Wang, A. H.-J. (2003) Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and Triton. J. Biol. Chem. 278, 29298-29307
    • (2003) J. Biol. Chem. , vol.278 , pp. 29298-29307
    • Chang, S.Y.1    Ko, T.P.2    Liang, P.H.3    Wang, A.H.-J.4
  • 10
    • 1842611457 scopus 로고    scopus 로고
    • Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies
    • Chang, S. Y., Ko, T. P., Chen, A. P.-C., Wang, A. H.-J. and Liang, P. H. (2004) Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies. Protein Sci. 13, 971-978
    • (2004) Protein Sci. , vol.13 , pp. 971-978
    • Chang, S.Y.1    Ko, T.P.2    Chen, A.P.-C.3    Wang, A.H.-J.4    Liang, P.H.5
  • 11
    • 1842455937 scopus 로고    scopus 로고
    • Bacterial polysaccharides
    • Chapter 21, Cold Spring Harbor Laboratory Press, Plainview, NY
    • Varki, A., Cummings, R., Esko, J., Freeze, H., Hart, G. and Marth, J. (1999) Bacterial polysaccharides. In Essentials of Glycobiology, Chapter 21, pp. 322-325, Cold Spring Harbor Laboratory Press, Plainview, NY
    • (1999) Essentials of Glycobiology , pp. 322-325
    • Varki, A.1    Cummings, R.2    Esko, J.3    Freeze, H.4    Hart, G.5    Marth, J.6
  • 12
    • 0035861579 scopus 로고    scopus 로고
    • Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis
    • Ko, T. P., Chen, Y. K., Robinson, H., Tsai, P. C., Gao, Y.-G., Chen, A. P.-C., Wang, A. H.-J. and Liang, P. H. (2001) Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. J. Biol. Chem. 276, 47474-47482
    • (2001) J. Biol. Chem. , vol.276 , pp. 47474-47482
    • Ko, T.P.1    Chen, Y.K.2    Robinson, H.3    Tsai, P.C.4    Gao, Y.-G.5    Chen, A.P.-C.6    Wang, A.H.-J.7    Liang, P.H.8
  • 13
    • 0345313624 scopus 로고    scopus 로고
    • Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: Cloning, expression, and characterization of the essential uppS gene
    • Apfel, C. M., Takacs, B., Fountoulakis, M. Stieger, M. and Keck, W. (1999) Use of genomics to identify bacterial undecaprenyl pyrophosphate synthetase: cloning, expression, and characterization of the essential uppS gene. J. Bacteriol. 181, 483-492
    • (1999) J. Bacteriol. , vol.181 , pp. 483-492
    • Apfel, C.M.1    Takacs, B.2    Fountoulakis, M.3    Stieger, M.4    Keck, W.5
  • 14
    • 0347298751 scopus 로고    scopus 로고
    • Synthesis and application of a fluorescent substrate analogue to study ligand interactions for undecaprenyl pyrophosphate synthase
    • Chen, A. P.-C., Chen, Y. H., Liu, H. P., Li, Y. C., Chen, C.-T. and Liang, P. H. (2002) Synthesis and application of a fluorescent substrate analogue to study ligand interactions for undecaprenyl pyrophosphate synthase. J. Am. Chem. Soc. 124, 15217-15224
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 15217-15224
    • Chen, A.P.-C.1    Chen, Y.H.2    Liu, H.P.3    Li, Y.C.4    Chen, C.-T.5    Liang, P.H.6
  • 15
    • 0034609518 scopus 로고    scopus 로고
    • Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction
    • Pan, J. J., Chiou, S. T. and Liang, P. H. (2000) Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction. Biochemistry 39, 10936-10942
    • (2000) Biochemistry , vol.39 , pp. 10936-10942
    • Pan, J.J.1    Chiou, S.T.2    Liang, P.H.3
  • 16
    • 0001131495 scopus 로고
    • Enzyme kinetics: Behavior and analysis of rapid equilibrium and steady-state enzyme systems
    • John Wiley and Sons, New York
    • Segel, I. H. (1993) Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-state Enzyme Systems. In Wiley Classics Library edn, pp. 100-108, John Wiley and Sons, New York
    • (1993) Wiley Classics Library Edn. , pp. 100-108
    • Segel, I.H.1
  • 17
    • 0034649372 scopus 로고    scopus 로고
    • Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis
    • Pan, J. J., Yang, L. W. and Liang, P. H. (2000) Effect of site-directed mutagenesis of the conserved aspartate and glutamate on E. coli undecaprenyl pyrophosphate synthase catalysis. Biochemistry 39, 13856-13861
    • (2000) Biochemistry , vol.39 , pp. 13856-13861
    • Pan, J.J.1    Yang, L.W.2    Liang, P.H.3
  • 18
    • 0033585443 scopus 로고    scopus 로고
    • Engineered isoprenoid pathway enhances astaxanthin production in Escherichia coli
    • Wang, C. W., Oh, M. K.and Liao, J. C. (1999) Engineered isoprenoid pathway enhances astaxanthin production in Escherichia coli. Biotechnol. Bioeng. 62, 235-241
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 235-241
    • Wang, C.W.1    Oh, M.K.2    Liao, J.C.3
  • 19
    • 0034838359 scopus 로고    scopus 로고
    • Engineering Escherichia coli for the synthesis of taxadiene, a key intermediate in the biosynthesis of taxol
    • Huang, Q., Roessner, C. A., Croteau, R. and Scott, A. I. (2001) Engineering Escherichia coli for the synthesis of taxadiene, a key intermediate in the biosynthesis of taxol. Bioorg. Med. Chem. 9, 2237-2242
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2237-2242
    • Huang, Q.1    Roessner, C.A.2    Croteau, R.3    Scott, A.I.4
  • 20
    • 1642457237 scopus 로고    scopus 로고
    • Coordinate expression of multiple bacterial carotenoid genes in canola leading to altered carotenoid production
    • Ravanello, M. P., Ke, D., Alvarez, J., Huang, B. and Shewmaker, C. K. (2003) Coordinate expression of multiple bacterial carotenoid genes in canola leading to altered carotenoid production. Metab. Eng. 5, 255-263
    • (2003) Metab. Eng. , vol.5 , pp. 255-263
    • Ravanello, M.P.1    Ke, D.2    Alvarez, J.3    Huang, B.4    Shewmaker, C.K.5
  • 21
    • 0026638165 scopus 로고
    • The crtE gene in Erwinia herbicola encodes geranylgeranyl diphosphate synthase
    • Math, S. K., Hearst, J. E. and Poulter, C. D. (1992) The crtE gene in Erwinia herbicola encodes geranylgeranyl diphosphate synthase. Proc. Natl. Acad. Sci. U.S.A. 89, 6761-6764
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6761-6764
    • Math, S.K.1    Hearst, J.E.2    Poulter, C.D.3
  • 22
    • 0348111215 scopus 로고    scopus 로고
    • Identification of the active conformation and the importance of length of the flexible loop 72-83 in regulating the conformational change of undecaprenyl pyrophosphate synthase
    • Chang, S. Y., Chen, Y. K., Wang, A. H.-J. and Liang, P. H. (2003) Identification of the active conformation and the importance of length of the flexible loop 72-83 in regulating the conformational change of undecaprenyl pyrophosphate synthase. Biochemistry 42, 14452-14459
    • (2003) Biochemistry , vol.42 , pp. 14452-14459
    • Chang, S.Y.1    Chen, Y.K.2    Wang, A.H.-J.3    Liang, P.H.4
  • 23
    • 0035832806 scopus 로고    scopus 로고
    • Similarities and differences in rubber biochemistry among plant species
    • Cornish, K. (2001) Similarities and differences in rubber biochemistry among plant species, Phytochemistry 57, 1123-1134
    • (2001) Phytochemistry , vol.57 , pp. 1123-1134
    • Cornish, K.1
  • 24
    • 0033202922 scopus 로고    scopus 로고
    • Molecular analysis of prenyl chain elongating enzymes
    • Koyama, T. (1999) Molecular analysis of prenyl chain elongating enzymes. Biosci. Biotechnol. Biochem. 63, 1671-1676
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1671-1676
    • Koyama, T.1
  • 25
    • 0345256451 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of cDNA encoding cis-prenyltransferases from Hevea brasiliensis. A key factor participating in natural rubber biosynthesis
    • Asawatreratanakul, K., Zhang, Y. W., Wititsuwannakul, D., Wititsuwannakul, R., Takahashi, S., Rattanapittayaporn, A. and Koyama, T. (2003) Molecular cloning, expression and characterization of cDNA encoding cis-prenyltransferases from Hevea brasiliensis. A key factor participating in natural rubber biosynthesis. Eur. J. Biochem. 270, 4671-4680
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4671-4680
    • Asawatreratanakul, K.1    Zhang, Y.W.2    Wititsuwannakul, D.3    Wititsuwannakul, R.4    Takahashi, S.5    Rattanapittayaporn, A.6    Koyama, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.