-
1
-
-
11544324496
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
15
-
-
0030480263
-
Regulation of product chain length by isoprenyl diphosphate synthases
-
Tarshis, L. C., Proteau, P. J., Kellogg, B. A., Sacchettini, J. C., and Poulter, C. D., Regulation of product chain length by isoprenyl diphosphate synthases. Proc. Natl. Acad. Sci. USA, 93, 15018-15023 (1996).
-
(1996)
Proc. Natl. Acad. Sci. USA
, vol.93
, pp. 15018-15023
-
-
Tarshis, L.C.1
Proteau, P.J.2
Kellogg, B.A.3
Sacchettini, J.C.4
Poulter, C.D.5
-
16
-
-
0031495890
-
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
-
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
-
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
-
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
-
20
-
-
33845374468
-
Phosphorylation of isoprenoid alcohols
-
Davisson, V. J., Woodside, A. B., Neal, T. R., Stremler, K. E., Muehlbacher, M., and Poulter, C. D., Phosphorylation of isoprenoid alcohols. J. Org. Chem., 51, 4768-4779 (1986).
-
(1986)
J. Org. Chem
, vol.51
, pp. 4768-4779
-
-
Davisson, V.J.1
Woodside, A.B.2
Neal, T.R.3
Stremler, K.E.4
Muehlbacher, M.5
Poulter, C.D.6
-
21
-
-
0004136246
-
-
2nd ed, Cold Spring Harbor Laboratory, Cold Spring Harbor
-
Sambrook, J., Fritsch, E. F., and Maniatis, T., "Molecular Cloning, a Laboratory Manual" 2nd ed., Cold Spring Harbor Laboratory, Cold Spring Harbor (1989).
-
(1989)
Molecular Cloning, a Laboratory Manual
-
-
Sambrook, J.1
Fritsch, E.F.2
Maniatis, T.3
-
22
-
-
0000262852
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
|