메뉴 건너뛰기




Volumn 47, Issue 2, 2008, Pages 680-688

Characterization of the substrate mimic bound to engineered prostacyclin synthase in solution using high-resolution NMR spectroscopy and mutagenesis: Implication of the molecular mechanism in biosynthesis of prostacyclin

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; MOLECULAR MECHANICS; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

EID: 38849099652     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701671q     Document Type: Article
Times cited : (8)

References (30)
  • 1
    • 0021022903 scopus 로고
    • Arachidonate metabolism in vascular disorders
    • Majerus, P. W. (1983) Arachidonate metabolism in vascular disorders, J. Clin. Invest. 72, 1521-1525.
    • (1983) J. Clin. Invest , vol.72 , pp. 1521-1525
    • Majerus, P.W.1
  • 2
    • 0021989951 scopus 로고
    • Endothelial cell prostacyclin production induced by activated neutrophils
    • Miller, D. K., Sadowski, S., Soderman, D. D., and Kuehl, F. A., Jr. (1985) Endothelial cell prostacyclin production induced by activated neutrophils, J. Biol. Chem. 260, 1006-1014
    • (1985) J. Biol. Chem , vol.260 , pp. 1006-1014
    • Miller, D.K.1    Sadowski, S.2    Soderman, D.D.3    Kuehl Jr., F.A.4
  • 3
    • 0022559202 scopus 로고
    • Prostaglandin biosynthesis and its compartmentation in vascular smooth muscle and endothelial cells
    • Smith, W. L. (1986) Prostaglandin biosynthesis and its compartmentation in vascular smooth muscle and endothelial cells, Annu. Rev. Physiol. 48, 251-262.
    • (1986) Annu. Rev. Physiol , vol.48 , pp. 251-262
    • Smith, W.L.1
  • 4
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot, D., Loll, P. J., and Garavito, R. M. (1994) The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1, Nature 367, 243-249.
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 9
    • 0027296775 scopus 로고
    • Amino-terminal topology of thromboxane synthase in the endoplasmic reticulum
    • Ruan, K. H., Wang, L. H., Wu, K. K., and Kulmacz, R. J. (1993) Amino-terminal topology of thromboxane synthase in the endoplasmic reticulum, J. Biol. Chem. 268, 19483-19490.
    • (1993) J. Biol. Chem , vol.268 , pp. 19483-19490
    • Ruan, K.H.1    Wang, L.H.2    Wu, K.K.3    Kulmacz, R.J.4
  • 10
    • 0028030885 scopus 로고
    • Characterization of the structure and membrane interaction of NH2-terminal domain of thromboxane A2 synthase
    • Ruan, K. H., Li, P., Kulmacz, R. J., and Wu, K. K. (1994) Characterization of the structure and membrane interaction of NH2-terminal domain of thromboxane A2 synthase, J. Biol. Chem. 269, 20938-20942.
    • (1994) J. Biol. Chem , vol.269 , pp. 20938-20942
    • Ruan, K.H.1    Li, P.2    Kulmacz, R.J.3    Wu, K.K.4
  • 11
    • 0024494718 scopus 로고
    • On the mechanism of prostacyclin and thromboxane A2 biosynthesis
    • Hecker, M., and Ullrich, V. (1989) On the mechanism of prostacyclin and thromboxane A2 biosynthesis, J. Biol. Chem. 264, 141-150.
    • (1989) J. Biol. Chem , vol.264 , pp. 141-150
    • Hecker, M.1    Ullrich, V.2
  • 12
    • 0027995192 scopus 로고
    • Prostacyclin and thromboxane synthase: New aspects of hemethiolate catalysis
    • Ullrich, V., and Brugger, R. (1994) Prostacyclin and thromboxane synthase: new aspects of hemethiolate catalysis, Angew Chem., Int. Ed. Engl. 33, 1911-1919.
    • (1994) Angew Chem., Int. Ed. Engl , vol.33 , pp. 1911-1919
    • Ullrich, V.1    Brugger, R.2
  • 13
    • 33750810887 scopus 로고    scopus 로고
    • Crystal structure of the human prostacyclin synthase
    • Chiang, C. W., Yeh, H. C., Wang, L. H., and Chan, N. L. (2006) Crystal structure of the human prostacyclin synthase, J. Mol. Biol. 364, 266-274.
    • (2006) J. Mol. Biol , vol.364 , pp. 266-274
    • Chiang, C.W.1    Yeh, H.C.2    Wang, L.H.3    Chan, N.L.4
  • 14
    • 28444473094 scopus 로고    scopus 로고
    • Ruan, K. H., Wu, J., and Wang, L. H. (2005) Solution structure of a common substrate mimetic of cyclooxygenase-downstream synthases bound to an engineered thromboxane A2 synthase using a high-resolution NMR technique, Arch. Biochem. Biophys. 444,-165-173.
    • Ruan, K. H., Wu, J., and Wang, L. H. (2005) Solution structure of a common substrate mimetic of cyclooxygenase-downstream synthases bound to an engineered thromboxane A2 synthase using a high-resolution NMR technique, Arch. Biochem. Biophys. 444,-165-173.
  • 15
    • 31044436812 scopus 로고    scopus 로고
    • Characterization of heme environment and mechanism of peroxide bond cleavage in human prostacyclin synthase
    • Yeh, H. C., Hsu, P. Y., Wang, J. S., Tsai, A. L., and Wang, L. H. (2005) Characterization of heme environment and mechanism of peroxide bond cleavage in human prostacyclin synthase, Biochim. Biophys. Acta 1738, 121-132.
    • (2005) Biochim. Biophys. Acta , vol.1738 , pp. 121-132
    • Yeh, H.C.1    Hsu, P.Y.2    Wang, J.S.3    Tsai, A.L.4    Wang, L.H.5
  • 16
    • 0030187103 scopus 로고    scopus 로고
    • Simple, distortion-free homonuclear spectra of peptides and nucleic acids in water using excitation sculpting
    • Callihan, D., West, J., Kumar, S., Schweitzer, B. I., and Logan, T. M. (1996) Simple, distortion-free homonuclear spectra of peptides and nucleic acids in water using excitation sculpting, J. Magn. Reson. B. 112, 82-85.
    • (1996) J. Magn. Reson. B , vol.112 , pp. 82-85
    • Callihan, D.1    West, J.2    Kumar, S.3    Schweitzer, B.I.4    Logan, T.M.5
  • 18
    • 0026045990 scopus 로고
    • A 175-psec molecular dynamics simulation of camphor-bound cytochrome P-450cam
    • Paulsen, M. D., and Ornstein, R. L. (1991) A 175-psec molecular dynamics simulation of camphor-bound cytochrome P-450cam, Proteins 11, 184-204.
    • (1991) Proteins , vol.11 , pp. 184-204
    • Paulsen, M.D.1    Ornstein, R.L.2
  • 19
    • 0026936915 scopus 로고
    • Predicting the product specificity and coupling of cytochrome P450cam
    • Paulsen, M. D., and Ornstein, R. L. (1992) Predicting the product specificity and coupling of cytochrome P450cam, J. Comput.-Aided Mol. Des. 6, 449-460.
    • (1992) J. Comput.-Aided Mol. Des , vol.6 , pp. 449-460
    • Paulsen, M.D.1    Ornstein, R.L.2
  • 20
    • 0031030586 scopus 로고    scopus 로고
    • Prostacyclin synthase active sites. Identification by molecular modeling-guided site-directed mutagenesis
    • Shyue, S. K., Ruan, K. H., Wang, L. H., and Wu, K. K. (1997) Prostacyclin synthase active sites. Identification by molecular modeling-guided site-directed mutagenesis, J. Biol. Chem. 272, 3657-3662.
    • (1997) J. Biol. Chem , vol.272 , pp. 3657-3662
    • Shyue, S.K.1    Ruan, K.H.2    Wang, L.H.3    Wu, K.K.4
  • 21
    • 0008896605 scopus 로고
    • Dynamical NOE in multiple-spin systems undergoing chemical exchange
    • Landy, S. B., and Rao, B. D. N. (1989) Dynamical NOE in multiple-spin systems undergoing chemical exchange, J. Magn. Reson. 81, 371-377.
    • (1989) J. Magn. Reson , vol.81 , pp. 371-377
    • Landy, S.B.1    Rao, B.D.N.2
  • 22
    • 0000071182 scopus 로고
    • Theory and experimental results of transfer-NOE experiments. 1. The influence of the off rate versus cross-relaxation rates
    • Lippens, R. M., Cerf, C., and Hallenga, K. (1992) Theory and experimental results of transfer-NOE experiments. 1. The influence of the off rate versus cross-relaxation rates, J. Magn. Reson. 99, 268-281.
    • (1992) J. Magn. Reson , vol.99 , pp. 268-281
    • Lippens, R.M.1    Cerf, C.2    Hallenga, K.3
  • 23
    • 0038629254 scopus 로고    scopus 로고
    • Identification of the residues in the helix F/G loop important to catalytic function of membrane-bound prostacyclin synthase
    • Deng, H., Wu, J., So, S. P., and Ruan, K. H. (2003) Identification of the residues in the helix F/G loop important to catalytic function of membrane-bound prostacyclin synthase, Biochemistry 42, 5609-5617.
    • (2003) Biochemistry , vol.42 , pp. 5609-5617
    • Deng, H.1    Wu, J.2    So, S.P.3    Ruan, K.H.4
  • 26
    • 33748927167 scopus 로고    scopus 로고
    • STD and TRNOESY NMR studies for the epitope mapping of the phosphorylation motif of the oncogenic protein beta-catenin recognized by a selective monoclonal antibody
    • Megy, S., Bertho, G., Gharbi-Benarous, J., Baleux, F., Benarous, R., and Girault, J. P. (2006) STD and TRNOESY NMR studies for the epitope mapping of the phosphorylation motif of the oncogenic protein beta-catenin recognized by a selective monoclonal antibody, FEBS Lett. 580, 5411-5422.
    • (2006) FEBS Lett , vol.580 , pp. 5411-5422
    • Megy, S.1    Bertho, G.2    Gharbi-Benarous, J.3    Baleux, F.4    Benarous, R.5    Girault, J.P.6
  • 27
    • 0001780788 scopus 로고    scopus 로고
    • Campbell, P. A, and Sykes, B. (1991) Theoretical evaluation of the two-dimensional transferred nuclear Overhauser effect, J. Magn. Reson. 93, 77-92.
    • Campbell, P. A, and Sykes, B. (1991) Theoretical evaluation of the two-dimensional transferred nuclear Overhauser effect, J. Magn. Reson. 93, 77-92.
  • 28
    • 0141987859 scopus 로고    scopus 로고
    • Exchange-transferred NOE spectroscopy and bound ligand structure determination
    • Post, C. B. (2003) Exchange-transferred NOE spectroscopy and bound ligand structure determination, Curr. Opin. Struct. Biol. 13, 581-588.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 581-588
    • Post, C.B.1
  • 29
    • 0037086473 scopus 로고    scopus 로고
    • Substrate access channel topology in membrane-bound prostacyclin synthase
    • Deng, H., Huang, A., So, S. P., Lin, Y. Z., and Ruan. K. H. (2002) Substrate access channel topology in membrane-bound prostacyclin synthase, Biochem. J. 362, 545-551.
    • (2002) Biochem. J , vol.362 , pp. 545-551
    • Deng, H.1    Huang, A.2    So, S.P.3    Lin, Y.Z.4    Ruan, K.H.5
  • 30
    • 0029664951 scopus 로고    scopus 로고
    • Identification of thromboxane A2 synthase active site residues by molecular modeling-guided site-directed mutagenesis
    • Wang, L. H., Matijevic-Aleksic, N., Hsu, P. Y., Ruan, K. H., Wu, K. K., and Kulmacz, R. J. (1996) Identification of thromboxane A2 synthase active site residues by molecular modeling-guided site-directed mutagenesis, J. Biol. Chem. 271, 19970-19975.
    • (1996) J. Biol. Chem , vol.271 , pp. 19970-19975
    • Wang, L.H.1    Matijevic-Aleksic, N.2    Hsu, P.Y.3    Ruan, K.H.4    Wu, K.K.5    Kulmacz, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.