메뉴 건너뛰기




Volumn 72, Issue 3, 2008, Pages 851-855

Kinetic studies of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase reaction using 3-desmethyl allylic substrate analogs

Author keywords

Cis prenyl chain elongating enzyme; Isoprenoid biosynthesis; Prenyltransferase; Substrate specificity; Undecaprenyl diphosphate synthase

Indexed keywords

CIS-PRENYL CHAIN ELONGATING ENZYME; ISOPRENOID BIOSYNTHESIS; PRENYLTRANSFERASE; SUBSTRATE SPECIFICITY; UNDECAPRENYL DIPHOSPHATE SYNTHASE;

EID: 41549083437     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70723     Document Type: Article
Times cited : (6)

References (30)
  • 1
    • 11544324496 scopus 로고    scopus 로고
    • Enzymatic aspects of isoprenoid chain elongation
    • Ogura, K., and Koyama, T., Enzymatic aspects of isoprenoid chain elongation. Chem. Rev., 98, 1263-1276 (1998).
    • (1998) Chem. Rev , vol.98 , pp. 1263-1276
    • Ogura, K.1    Koyama, T.2
  • 2
    • 0030846307 scopus 로고    scopus 로고
    • Creating isoprenoid diversity
    • Sacchettini, J. C., and Poulter, C. D., Creating isoprenoid diversity. Science, 277, 1788-1789 (1997).
    • (1997) Science , vol.277 , pp. 1788-1789
    • Sacchettini, J.C.1    Poulter, C.D.2
  • 3
    • 0032584588 scopus 로고    scopus 로고
    • Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase: No sequence similarity between E- and Z-prenyl diphosphate synthases
    • Shimizu, N., Koyama, T., and Ogura, K., Molecular cloning, expression, and purification of undecaprenyl diphosphate synthase: no sequence similarity between E- and Z-prenyl diphosphate synthases. J. Biol. Chem., 273, 19476-19481 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 19476-19481
    • Shimizu, N.1    Koyama, T.2    Ogura, K.3
  • 4
    • 0035836712 scopus 로고    scopus 로고
    • Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase
    • Fujihashi, M., Zhang, Y.-W., Higuchi, Y., Li, X.-Y., Koyama, T., and Miki, K., Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl. Acad. Sci. USA, 98, 4337-4342 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4337-4342
    • Fujihashi, M.1    Zhang, Y.-W.2    Higuchi, Y.3    Li, X.-Y.4    Koyama, T.5    Miki, K.6
  • 5
    • 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., Wang, A. H., and Liang, P. H., 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).
    • (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.6    Wang, A.H.7    Liang, P.H.8
  • 6
    • 0026800846 scopus 로고
    • Effects of site-directed mutagenesis of the highly conserved aspartate residues in domain II of farnesyl diphosphate synthase activity
    • Marrero, P. F., Poulter, C. D., and Edwards, P. A., Effects of site-directed mutagenesis of the highly conserved aspartate residues in domain II of farnesyl diphosphate synthase activity. J. Biol. Chem., 267, 21873-21878 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 21873-21878
    • Marrero, P.F.1    Poulter, C.D.2    Edwards, P.A.3
  • 7
    • 0027768770 scopus 로고
    • Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthase activity
    • Joly, A., and Edwards, P. A., Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthase activity. J. Biol. Chem., 268, 26983-26989 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 26983-26989
    • Joly, A.1    Edwards, P.A.2
  • 8
    • 0028288134 scopus 로고
    • Yeast farnesyl-diphosphate synthase: Site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II
    • Song, L., and Poulter, C. D., Yeast farnesyl-diphosphate synthase: site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II. Proc. Natl. Acad. Sci. USA, 91, 3044-3048 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3044-3048
    • Song, L.1    Poulter, C.D.2
  • 9
    • 0029782306 scopus 로고    scopus 로고
    • Identification of significant residues in the substrate binding site of Bacillus stearothermophilus farnesyl diphosphate synthase
    • Koyama, T., Tajima, M., Sano, H., Doi, T., Koike-Takeshita, A., Obata, S., Nishino, T., and Ogura, K., Identification of significant residues in the substrate binding site of Bacillus stearothermophilus farnesyl diphosphate synthase. Biochemistry, 35, 9533-9538 (1996).
    • (1996) Biochemistry , vol.35 , pp. 9533-9538
    • Koyama, T.1    Tajima, M.2    Sano, H.3    Doi, T.4    Koike-Takeshita, A.5    Obata, S.6    Nishino, T.7    Ogura, K.8
  • 10
    • 0028718319 scopus 로고
    • Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: Crystallization and site-directed mutagenesis
    • Koyama, T., Obata, S., Osabe, M., Saito, K., Takeshita, A., Nishino, T., and Ogura, K., Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: crystallization and site-directed mutagenesis. Acta Biochim. Pol., 41, 281-292 (1994).
    • (1994) Acta Biochim. Pol , vol.41 , pp. 281-292
    • Koyama, T.1    Obata, S.2    Osabe, M.3    Saito, K.4    Takeshita, A.5    Nishino, T.6    Ogura, K.7
  • 11
    • 0027942696 scopus 로고
    • Structural and functional roles of the cysteine residues of Bacillus stearothermophilus farnesyl diphosphate synthase
    • Koyama, T., Obata, S., Saito, K., Takeshita-Koike, A., and Ogura, K., Structural and functional roles of the cysteine residues of Bacillus stearothermophilus farnesyl diphosphate synthase. Biochemistry, 33, 12644-12648 (1994).
    • (1994) Biochemistry , vol.33 , pp. 12644-12648
    • Koyama, T.1    Obata, S.2    Saito, K.3    Takeshita-Koike, A.4    Ogura, K.5
  • 12
    • 0027961825 scopus 로고
    • Site-directed mutagenesis of farnesyl diphosphate synthase: Effect of substitution on the three carboxyl-terminal amino acids
    • Koyama, T., Saito, K., Ogura, K., Obata, S., and Takeshita, A., Site-directed mutagenesis of farnesyl diphosphate synthase: effect of substitution on the three carboxyl-terminal amino acids. Can. J. Chem., 72, 75-79 (1994).
    • (1994) Can. J. Chem , vol.72 , pp. 75-79
    • Koyama, T.1    Saito, K.2    Ogura, K.3    Obata, S.4    Takeshita, A.5
  • 13
    • 0029804201 scopus 로고    scopus 로고
    • A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product
    • Ohnuma, S., Narita, K., Nakazawa, T., Ishida, C., Takeuchi, Y., Ohto, C., and Nishino, T., A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product. J. Biol. Chem., 271, 30748-30754 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 30748-30754
    • Ohnuma, S.1    Narita, K.2    Nakazawa, T.3    Ishida, C.4    Takeuchi, Y.5    Ohto, C.6    Nishino, T.7
  • 14
    • 0028145239 scopus 로고
    • Crystal structure of recombinant farnesyl diphosphate synthase at 2.6Å resolution
    • Tarshis, L. C., Yan, M., Poulter, C. D., and Sacchettini, J. C., Crystal structure of recombinant farnesyl diphosphate synthase at 2.6Å resolution. Biochemistry, 33, 10871-10879 (1994).
    • (1994) Biochemistry , vol.33 , pp. 10871-10879
    • Tarshis, L.C.1    Yan, M.2    Poulter, C.D.3    Sacchettini, J.C.4
  • 16
    • 0031495890 scopus 로고    scopus 로고
    • An artificial substrate for the thermostable farnesyl diphosphate synthase from Bacillus stearothermophilus
    • Nagaki, M., Koyama, T., Nishino, T., Shimizu, K., Maki, Y., and Ogura, K., An artificial substrate for the thermostable farnesyl diphosphate synthase from Bacillus stearothermophilus. Chem. Lett., 26, 497-498 (1997).
    • (1997) Chem. Lett , vol.26 , pp. 497-498
    • Nagaki, M.1    Koyama, T.2    Nishino, T.3    Shimizu, K.4    Maki, Y.5    Ogura, K.6
  • 17
    • 0035921017 scopus 로고    scopus 로고
    • Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases
    • Nagaki, M., Kimura, K., Kimura, H., Maki, Y., Goto, E., Nishino, T., and Koyama, T., Artificial substrates of medium-chain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases. Bioorg. Med. Chem. Lett., 11, 2157-2159 (2001).
    • (2001) Bioorg. Med. Chem. Lett , vol.11 , pp. 2157-2159
    • Nagaki, M.1    Kimura, K.2    Kimura, H.3    Maki, Y.4    Goto, E.5    Nishino, T.6    Koyama, T.7
  • 18
    • 0344806943 scopus 로고    scopus 로고
    • Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase
    • Fujikura, K., Zhang, Y.-W., Fujihashi, M., Miki, K., and Koyama, T., Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase. Biochemistry, 42, 4035-4041 (2003).
    • (2003) Biochemistry , vol.42 , pp. 4035-4041
    • Fujikura, K.1    Zhang, Y.-W.2    Fujihashi, M.3    Miki, K.4    Koyama, T.5
  • 19
    • 0034528539 scopus 로고    scopus 로고
    • Significance of Asn-77 and Trp-78 in the catalytic function of undecaprenyl diphosphate synthase of Micrococcus luteus B-P 26
    • Fujikura, K., Zhang, Y.-W., Yoshizaki, H., Nishino, T., and Koyama, T., Significance of Asn-77 and Trp-78 in the catalytic function of undecaprenyl diphosphate synthase of Micrococcus luteus B-P 26. J. Biochem., 128, 917-922 (2000).
    • (2000) J. Biochem , vol.128 , pp. 917-922
    • Fujikura, K.1    Zhang, Y.-W.2    Yoshizaki, H.3    Nishino, T.4    Koyama, T.5
  • 22
    • 0000262852 scopus 로고    scopus 로고
    • Highly selective synthesis of Z-unsaturated esters by using new Horner-Emmons reagents, ethyl (diarylphosphono) acetates
    • Ando, K., Highly selective synthesis of Z-unsaturated esters by using new Horner-Emmons reagents, ethyl (diarylphosphono) acetates. J. Org. Chem., 62, 1934-1939 (1997).
    • (1997) J. Org. Chem , vol.62 , pp. 1934-1939
    • Ando, K.1
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0032972775 scopus 로고    scopus 로고
    • Structural motif of phosphate-binding site common to various protein superfamilies: All-against-all structural comparison of protein-mononucleotide complexes
    • Kinoshita, K., Sadanami, K., Kidera, A., and Go, N., Structural motif of phosphate-binding site common to various protein superfamilies: all-against-all structural comparison of protein-mononucleotide complexes. Protein Eng., 12, 11-14 (1999).
    • (1999) Protein Eng , vol.12 , pp. 11-14
    • Kinoshita, K.1    Sadanami, K.2    Kidera, A.3    Go, N.4
  • 25
    • 33748564953 scopus 로고    scopus 로고
    • Structure and function of cis-prenyl chain elongating enzyme
    • Takahashi, S., and Koyama, T., Structure and function of cis-prenyl chain elongating enzyme. Chem. Rec., 6, 194-205 (2006).
    • (2006) Chem. Rec , vol.6 , pp. 194-205
    • Takahashi, S.1    Koyama, T.2
  • 26
    • 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., Wang, A. H., and Liang, P. H., Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies. Protein Sci., 13, 971-978 (2004).
    • (2004) Protein Sci , vol.13 , pp. 971-978
    • Chang, S.Y.1    Ko, T.P.2    Chen, A.P.3    Wang, A.H.4    Liang, P.H.5
  • 27
    • 20144382151 scopus 로고    scopus 로고
    • Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate
    • Guo, R. T., Ko, T. P., Chen, A. P., Kuo, C. J., Wang, A. H., and Liang, P. H., Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate. J. Biol. Chem., 280, 20762-20774 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 20762-20774
    • Guo, R.T.1    Ko, T.P.2    Chen, A.P.3    Kuo, C.J.4    Wang, A.H.5    Liang, P.H.6
  • 28
    • 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., 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).
    • (2003) J. Biol. Chem , vol.278 , pp. 29298-29307
    • Chang, S.Y.1    Ko, T.P.2    Liang, P.H.3    Wang, A.H.4
  • 29
    • 14244265227 scopus 로고    scopus 로고
    • Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase
    • Chen, A. P., Chang, S. Y., Lin, Y. C., Sun, Y. S., Chen, C. T., Wang, A. H., and Liang, P. H., Substrate and product specificities of cis-type undecaprenyl pyrophosphate synthase. Biochem. J., 386, 169-176 (2005).
    • (2005) Biochem. J , vol.386 , pp. 169-176
    • Chen, A.P.1    Chang, S.Y.2    Lin, Y.C.3    Sun, Y.S.4    Chen, C.T.5    Wang, A.H.6    Liang, P.H.7
  • 30
    • 33644934032 scopus 로고    scopus 로고
    • Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases
    • Kharel, Y., Takahashi, S., Yamashita, S., and Koyama, T., Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases. FEBS J., 273, 647-657 (2006).
    • (2006) FEBS J , vol.273 , pp. 647-657
    • Kharel, Y.1    Takahashi, S.2    Yamashita, S.3    Koyama, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.