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Volumn 51, Issue 22, 2012, Pages 4580-4589

Active site binding and catalytic role of bicarbonate in 1,4-dihydroxy-2-naphthoyl coenzyme a synthases from vitamin K biosynthetic pathways

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ANION BINDING; ASPARTATE RESIDUE; BIOSYNTHETIC PATHWAY; CARBON-CARBON BOND FORMATION REACTIONS; CATALYTIC BASE; CATALYTIC ROLE; CHLORIDE IONS; COENZYME A; COFACTORS; ELECTROSTATIC ATTRACTIONS; ENOLATES; ENZYMATIC ACTIVITIES; ENZYME ACTIVE SITES; HYDROPHOBIC INTERACTIONS; ORTHOLOGUES; SIDE-CHAINS; STRUCTURAL BASIS; SYNECHOCYSTIS SP; SYNTHASES; VITAMIN K; VITAMIN K1;

EID: 84861910725     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300486j     Document Type: Article
Times cited : (11)

References (65)
  • 1
    • 0035219809 scopus 로고    scopus 로고
    • Biosynthesis of menaquinone (Vitamin K2) and ubiquinone (Coenzyme Q): A perspective on enzymatic mechanisms
    • Meganathan, R. (2001) Biosynthesis of menaquinone (Vitamin K2) and ubiquinone (Coenzyme Q): A perspective on enzymatic mechanisms. Vitam. Horm. 61, 173-218.
    • (2001) Vitam. Horm. , vol.61 , pp. 173-218
    • Meganathan, R.1
  • 2
    • 43549091597 scopus 로고    scopus 로고
    • Evidence of a chimeric genome in the cyannobacterial ancestor of plastids
    • Gross, J., Meurer, J., and Bhattacharya, D. (2008) Evidence of a chimeric genome in the cyannobacterial ancestor of plastids. BMC Evol. Biol. 8, 117.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 117
    • Gross, J.1    Meurer, J.2    Bhattacharya, D.3
  • 3
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • DOI 10.1038/nature02200
    • Shem, A. B., Frolow, F., and Nelson, N. (2003) Crystal structure of plant photosystem I. Nature 426, 630-635. (Pubitemid 38009364)
    • (2003) Nature , vol.426 , Issue.6967 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 4
    • 34648813427 scopus 로고    scopus 로고
    • Menaquinone biosynthesis in Escherichia coli: Identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity
    • DOI 10.1021/bi700810x
    • Jiang, M., Cao, Y., Guo, Z.-F., Chen, M., Chen, X., and Guo, Z. (2007) Menaquinone biosynthesis in Escherichia coli: Identification of 2-succinyl-5-enolpyruvyl-6-hydroxyl-3- cyclohexene-1-carboxylate (SEPHCHC) as a novel intermediate and re-evaluation of MenD activity. Biochemistry 46, 10979-10989. (Pubitemid 47463049)
    • (2007) Biochemistry , vol.46 , Issue.38 , pp. 10979-10989
    • Jiang, M.1    Cao, Y.2    Guo, Z.-F.3    Chen, M.4    Chen, X.5    Guo, Z.6
  • 5
    • 36348960245 scopus 로고    scopus 로고
    • Determination of the stereochemistry of 2-succinyl-5- Enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic acid, a key intermediate in menaquinone biosynthesis
    • Jiang, M., Chen, M., Cao, Y., Yang, Y., Sze, K. H., Chen, X., and Guo, Z. (2007) Determination of the stereochemistry of 2-succinyl-5- enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic acid, a key intermediate in menaquinone biosynthesis. Org. Lett. 9, 4765-4767.
    • (2007) Org. Lett. , vol.9 , pp. 4765-4767
    • Jiang, M.1    Chen, M.2    Cao, Y.3    Yang, Y.4    Sze, K.H.5    Chen, X.6    Guo, Z.7
  • 6
    • 40849094350 scopus 로고    scopus 로고
    • Identification and characterization of (1R,6R)-2-succinyl-6-hydroxy-2,4- cyclohexadiene-1-carboxylate synthase in the menaquinone biosynthesis of Escherichia coli
    • DOI 10.1021/bi7023755
    • Jiang, M., Chen, X., Guo, Z.-F., Cao, Y., Chen, M., and Guo, Z. (2008) Identification and characterization of (1R,6R)-2-succinyl-6- hydroxy-2,4-cyclohexadiene-1-carboxylate synthase in the menaquinone biosynthesis of Escherichia coli. Biochemistry 47, 3426-3434. (Pubitemid 351399231)
    • (2008) Biochemistry , vol.47 , Issue.11 , pp. 3426-3434
    • Jiang, M.1    Chen, X.2    Guo, Z.-F.3    Cao, Y.4    Chen, M.5    Guo, Z.6
  • 7
    • 23944489821 scopus 로고    scopus 로고
    • The vitamin K-dependent carboxylase
    • Berkner, K. L. (2005) The vitamin K-dependent carboxylase. Annu. Rev. Nutr. 25, 127-149.
    • (2005) Annu. Rev. Nutr. , vol.25 , pp. 127-149
    • Berkner, K.L.1
  • 8
    • 34548118698 scopus 로고    scopus 로고
    • Discovery of 1,4-didydroxy-2-naphthoate prenyltransferase inhibitors: New drug leads for multidrug-resistant gram-positive pathogens
    • DOI 10.1021/jm070638m
    • Kurosu, M., Narayanasamy, P., Biswas, K., Dhiman, R., and Crick, D. C. (2007) Discovery of 1,4-dihydroxy-2-naphthoate prenyltransferase inhibitors: New drug leads for multidrug-resistant Gram-positive pathogens. J. Med. Chem. 50, 3973-3975. (Pubitemid 47301729)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.17 , pp. 3973-3975
    • Kurosu, M.1    Narayanasamy, P.2    Biswas, K.3    Dhiman, R.4    Crick, D.C.5
  • 9
    • 55249100482 scopus 로고    scopus 로고
    • Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis
    • Lu, X., Zhang, H., Tonge, P. J., and Tan., D. S. (2008) Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis. Bioorg. Med. Chem. Lett. 18, 5963-5966.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5963-5966
    • Lu, X.1    Zhang, H.2    Tonge, P.J.3    Tan, D.S.4
  • 10
    • 77949796314 scopus 로고    scopus 로고
    • Succinylphosphonate esters are competitive inhibitors of MenD that show active-site discrimination between homologous á- ketoglutaratedecarboxylating enzymes
    • Fang, M., Toogood, R. D., Macova, A., Ho, K., Franzblau, S. G., McNeil, M. R., Sanders, D. A. R., and Palmer, D. R. J. (2010) Succinylphosphonate esters are competitive inhibitors of MenD that show active-site discrimination between homologous á-ketoglutaratedecarboxylating enzymes. Biochemistry 49, 2672-2679.
    • (2010) Biochemistry , vol.49 , pp. 2672-2679
    • Fang, M.1    Toogood, R.D.2    Macova, A.3    Ho, K.4    Franzblau, S.G.5    McNeil, M.R.6    Sanders, D.A.R.7    Palmer, D.R.J.8
  • 11
    • 77957886578 scopus 로고    scopus 로고
    • Synthesis and SAR studies of 1,4-benzoxazine MenB inhibitors: Novel antibacterial agents against Mycobacterium tuberculosis
    • Li, X., Liu, N., Zhang, H., Knudson, S. E., Slayden, R. A., and Tonge, P. J. (2010) Synthesis and SAR studies of 1,4-benzoxazine MenB inhibitors: Novel antibacterial agents against Mycobacterium tuberculosis. Bioorg. Med. Chem. Lett. 20, 6306-6309.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 6306-6309
    • Li, X.1    Liu, N.2    Zhang, H.3    Knudson, S.E.4    Slayden, R.A.5    Tonge, P.J.6
  • 12
    • 80955150848 scopus 로고    scopus 로고
    • CoA adducts of 4-oxo-4-phenylbut-2-enoates: Inhibitors of MenB from the M. tuberculosis menaquinone biosynthesis pathway
    • Li, X., Liu, N., Zhang, H., Knudson, S. E., Li, H. J., Lai, C. T., Simmerling, C., Slayden, R. A., and Tonge, P. J. (2011) CoA adducts of 4-oxo-4-phenylbut-2-enoates: Inhibitors of MenB from the M. tuberculosis menaquinone biosynthesis pathway. ACS Med. Chem. Lett. 2, 818-823.
    • (2011) ACS Med. Chem. Lett. , vol.2 , pp. 818-823
    • Li, X.1    Liu, N.2    Zhang, H.3    Knudson, S.E.4    Li, H.J.5    Lai, C.T.6    Simmerling, C.7    Slayden, R.A.8    Tonge, P.J.9
  • 13
    • 84155174673 scopus 로고    scopus 로고
    • Stable analogues of OSB-AMP: Potent inhibitors of MenE, the o-succinylbenzoate-CoA synthetase from bacterial menaquinone biosynthesis
    • Lu, X., Zhou, R., Sharma, I., Li, X., Kumar, G., Swaminathan, S., Tonge, P. J., and Tan, D. S. (2012) Stable analogues of OSB-AMP: Potent inhibitors of MenE, the o-succinylbenzoate-CoA synthetase from bacterial menaquinone biosynthesis. ChemBioChem 13, 129-136.
    • (2012) ChemBioChem , vol.13 , pp. 129-136
    • Lu, X.1    Zhou, R.2    Sharma, I.3    Li, X.4    Kumar, G.5    Swaminathan, S.6    Tonge, P.J.7    Tan, D.S.8
  • 14
    • 0026611037 scopus 로고
    • Menaquinone (Vitamin K2) biosynthesis: Nucleotide sequence and expression of the menB gene from Escherichia coli
    • Sharma, V., Suvarna, K., Meganathan, R., and Hudspeth, M. E. S. (1992) Menaquinone (Vitamin K2) biosynthesis: Nucleotide sequence and expression of the menB gene from Escherichia coli. J. Bacteriol. 174, 5057-5062.
    • (1992) J. Bacteriol. , vol.174 , pp. 5057-5062
    • Sharma, V.1    Suvarna, K.2    Meganathan, R.3    Hudspeth, M.E.S.4
  • 19
    • 33745183354 scopus 로고    scopus 로고
    • A plant locus essential for phylloquinone (Vitamin K1) biosynthesis originated from a fusion of four eubacterial genes
    • Gross, J., Cho, W. K., Lezhneva, L., Falk, J., Krupinska, K., Shinozaki, K., Seki, M., Herrmann, R. G., and Meurer, J. (2006) A plant locus essential for phylloquinone (Vitamin K1) biosynthesis originated from a fusion of four eubacterial genes. J. Biol. Chem. 281, 17189-17196.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17189-17196
    • Gross, J.1    Cho, W.K.2    Lezhneva, L.3    Falk, J.4    Krupinska, K.5    Shinozaki, K.6    Seki, M.7    Herrmann, R.G.8    Meurer, J.9
  • 20
    • 77956905385 scopus 로고    scopus 로고
    • A bicarbonate cofactor modulates 1,4-dihydroxy-2-naphthoyl coenzyme A synthase in menaquinone biosynthesis of Escherichia coli
    • Jiang, M., Chen, M., Guo, Z. F., and Guo, Z. (2010) A bicarbonate cofactor modulates 1,4-dihydroxy-2-naphthoyl coenzyme A synthase in menaquinone biosynthesis of Escherichia coli. J. Biol. Chem. 285, 30159-30169.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30159-30169
    • Jiang, M.1    Chen, M.2    Guo, Z.F.3    Guo, Z.4
  • 21
    • 84856331676 scopus 로고    scopus 로고
    • Characterization of 1,4-dihydroxy- 2-naphthoyl-coenzyme A synthase (MenB) in phylloquinone biosynthesis of Synechocystis sp. PCC 6803
    • Song, H., and Guo, Z. (2012) Characterization of 1,4-dihydroxy- 2-naphthoyl-coenzyme A synthase (MenB) in phylloquinone biosynthesis of Synechocystis sp. PCC 6803. Sci. China, Ser. B: Chem. 55, 98-105.
    • (2012) Sci. China, Ser. B: Chem. , vol.55 , pp. 98-105
    • Song, H.1    Guo, Z.2
  • 22
    • 0028601410 scopus 로고
    • Enoyl-coenzyme A hydratase-catalyzed exchange of the α- Protons of coenzyme A thiol esters: A model for an enolized intermediate in the enzyme-catalyzed elimination
    • D'Ordine, R. L., Bahnson, B. J., Tonge, P. J., and Anderson, V. E. (1994) Enoyl-coenzyme A hydratase-catalyzed exchange of the α- protons of coenzyme A thiol esters: A model for an enolized intermediate in the enzyme-catalyzed elimination. Biochemistry 33, 14733-14742.
    • (1994) Biochemistry , vol.33 , pp. 14733-14742
    • D'Ordine, R.L.1    Bahnson, B.J.2    Tonge, P.J.3    Anderson, V.E.4
  • 23
    • 0028890344 scopus 로고
    • Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue
    • Newen, G. M., Janssen, U., and Stoffel, W. (1995) Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue. Eur. J. Biochem. 228, 68-73.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 68-73
    • Newen, G.M.1    Janssen, U.2    Stoffel, W.3
  • 24
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: A spiral fold defines the CoA-binding pocket
    • Engel, C. K., Mathieu, M., Zeelen, J. P., Hiltunen, J. K., and Wierenga, R. K. (1996) Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 Å resolution: A spiral fold defines the CoA-binding pocket. EMBO J. 19, 5135-5145. (Pubitemid 26336195)
    • (1996) EMBO Journal , vol.15 , Issue.19 , pp. 5135-5145
    • Engel, C.K.1    Mathieu, M.2    Zeelen, J.Ph.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 25
    • 0032488815 scopus 로고    scopus 로고
    • The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule
    • DOI 10.1006/jmbi.1997.1491
    • Engel, C. K., Kiema, T. R., Hiltunen, J. K., and Wierenga, R. K. (1998) The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule. J. Mol. Biol. 275, 847-859. (Pubitemid 28077700)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.5 , pp. 847-859
    • Engel, C.K.1    Kiema, T.R.2    Kalervo, H.J.3    Wierenga, R.K.4
  • 26
    • 0032528950 scopus 로고    scopus 로고
    • The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate sidechains for catalysis
    • Modis, Y., Filppula, S. A., Novikov, D. K., Norledge, B., Hiltunen, J. K., and Wierenga, R. K. (1998) The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate side chains for catalysis. Structure 6, 957-970. (Pubitemid 28397918)
    • (1998) Structure , vol.6 , Issue.8 , pp. 957-970
    • Modis, Y.1    Filppula, S.A.2    Novikov, D.K.3    Norledge, B.4    Kalervo, H.J.5    Wierenga, R.K.6
  • 27
    • 0033537658 scopus 로고    scopus 로고
    • Mutagenic and enzymological studies of the hydratase and isomerase activities of 2- Enoyl-CoA hydratase-1
    • Kiema, T. R., Engel, C. K., Schmitz, W., Filppula, S. A., Wierenga, R. K., and Hiltunen., J. K. (1999) Mutagenic and enzymological studies of the hydratase and isomerase activities of 2- enoyl-CoA hydratase-1. Biochemistry 38, 2991-2999.
    • (1999) Biochemistry , vol.38 , pp. 2991-2999
    • Kiema, T.R.1    Engel, C.K.2    Schmitz, W.3    Filppula, S.A.4    Wierenga, R.K.5    Hiltunen, J.K.6
  • 30
    • 80155126202 scopus 로고    scopus 로고
    • Mechanism of the intramolecular Claisen condensation reaction catalyzed by MenB, a crotonase superfamily member
    • Li, H. L., Li, X., Liu, N., Zhang, H., Truglio, J. J., Mishra, S., Kisker, C. F., Garcia-Diaz, M., and Tonge, P. J. (2011) Mechanism of the intramolecular Claisen condensation reaction catalyzed by MenB, a crotonase superfamily member. Biochemistry 50, 9532-9544.
    • (2011) Biochemistry , vol.50 , pp. 9532-9544
    • Li, H.L.1    Li, X.2    Liu, N.3    Zhang, H.4    Truglio, J.J.5    Mishra, S.6    Kisker, C.F.7    Garcia-Diaz, M.8    Tonge, P.J.9
  • 31
    • 0025184639 scopus 로고
    • 2) biosynthesis
    • DOI 10.1111/j.1432-1033.1990.tb19246.x
    • Igbavboa, U., and Leistner, E. (1990) Sequence of function in the crotonase superfamily: The stereochemistry course of the reaction catalyzed by naphthoate synthase, an enzyme involved in menaquinone (vitamin K2) biosynthesis. Eur. J. Biochem. 192, 441-449. (Pubitemid 20283513)
    • (1990) European Journal of Biochemistry , vol.192 , Issue.2 , pp. 441-449
    • Igbavboa, U.1    Leistner, E.2
  • 35
    • 33846569091 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase
    • DOI 10.1021/ja065064+
    • Jiang, M., and Guo, Z. (2007) Effects of macromolecular crowding on the intrinsic catalytic efficiency and structure of enterobactin-specific isochorismate synthase. J. Am. Chem. Soc. 129, 730-731. (Pubitemid 46183901)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.4 , pp. 730-731
    • Jiang, M.1    Guo, Z.2
  • 36
    • 67651208493 scopus 로고    scopus 로고
    • Catalytic mechanism of SHCHC synthase in the menaquinone biosynthesis of Escherichia coli: Identification and mutational analysis of the active site residues
    • Jiang, M., Chen, X., Wu, X. H., Chen, M., Wu, Y., and Guo, Z. (2009) Catalytic mechanism of SHCHC synthase in the menaquinone biosynthesis of Escherichia coli: Identification and mutational analysis of the active site residues. Biochemistry 48, 6921-6931.
    • (2009) Biochemistry , vol.48 , pp. 6921-6931
    • Jiang, M.1    Chen, X.2    Wu, X.H.3    Chen, M.4    Wu, Y.5    Guo, Z.6
  • 37
    • 0031253625 scopus 로고    scopus 로고
    • Efficient in vivo synthesis and rapid purification of chorismic acid using an engineered Escherichia coil strain
    • DOI 10.1006/bioo.1997.1073
    • Grisostomi, G., Kast, P., Pulido, R., Huynh, J., and Hilvert, D. (1997) Efficient in vivo synthesis and rapid purification of chorismic acid using an engineered Escherichia coli strain. Bioorg. Chem. 25, 297-305. (Pubitemid 28218792)
    • (1997) Bioorganic Chemistry , vol.25 , Issue.5-6 , pp. 297-305
    • Grisostomi, C.1    Kast, P.2    Pulido, R.3    Huynh, J.4    Hilvert, D.5
  • 38
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for Protein Crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 45
    • 70349597601 scopus 로고    scopus 로고
    • Electronic Ligand Builder and Optimization Workbench (eLBOW): A tool for ligand coordinate and restraint generation
    • Moriarty, N. W., Grosse-Kunstleve, R. W., and Adams, P. D. (2009) electronic Ligand Builder and Optimization Workbench (eLBOW): A tool for ligand coordinate and restraint generation. Acta Crystallogr. D65, 1074-1080.
    • (2009) Acta Crystallogr. , vol.D65 , pp. 1074-1080
    • Moriarty, N.W.1    Grosse-Kunstleve, R.W.2    Adams, P.D.3
  • 47
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 50
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • DOI 10.1093/nar/gkh381
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) PDB2PQR: An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-W667. (Pubitemid 38997419)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 52
    • 32944466172 scopus 로고    scopus 로고
    • Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms
    • DOI 10.1107/S0907444905017531
    • Johnston, J. M., Arcus, V. L., and Baker, E. N. (2005) Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms. Acta Crystallogr. D61, 1199-1206. (Pubitemid 43961291)
    • (2005) Acta Crystallographica Section D: Biological Crystallography , vol.61 , Issue.9 , pp. 1199-1206
    • Johnston, J.M.1    Arcus, V.L.2    Baker, E.N.3
  • 53
    • 0027382865 scopus 로고
    • Site-directed mutagenesis of putative active-site amino acid residues of 3,2-trans-enoyl-CoA isomerase, conserved within the low-homology isomerase/hydratase enzyme family
    • DOI 10.1021/bi00093a018
    • Muller-Newen, G., and Stoffel, W. (1993) Site-directed mutagenesis of putative active-site amino acid residues of 3,2- transenoyl-CoA isomerase, conserved within the low-homology isomerase/hydratase enzyme family. Biochemistry 32, 11405-11412. (Pubitemid 23332053)
    • (1993) Biochemistry , vol.32 , Issue.42 , pp. 11405-11412
    • Muller-Newen, G.1    Stoffel, W.2
  • 55
    • 0032528950 scopus 로고    scopus 로고
    • The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate sidechains for catalysis
    • Modis, Y., Filppula, S. A., Novikov, D. K., Norledge, B., Hiltunen, J. K., and Wierenga, R. K. (1998) The crystal structure of dienoyl-CoA isomerase at 1.5 Å resolution reveals the importance of aspartate and glutamate sidechains for catalysis. Structure 6, 957-970. (Pubitemid 28397918)
    • (1998) Structure , vol.6 , Issue.8 , pp. 957-970
    • Modis, Y.1    Filppula, S.A.2    Novikov, D.K.3    Norledge, B.4    Kalervo, H.J.5    Wierenga, R.K.6
  • 56
    • 50949084595 scopus 로고    scopus 로고
    • A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) with acetyl-CoA and vanillin gives insights into substrate specificity and mechanism
    • Bennett, J. P., Bertin, L., Moulton, B., Fairlamb, I. J. S., Brzozowski, A. M., Walton, N. J., and Grogan, G. (2008) A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (HCHL) with acetyl-CoA and vanillin gives insights into substrate specificity and mechanism. Biochem. J. 414, 281-289.
    • (2008) Biochem. J. , vol.414 , pp. 281-289
    • Bennett, J.P.1    Bertin, L.2    Moulton, B.3    Fairlamb, I.J.S.4    Brzozowski, A.M.5    Walton, N.J.6    Grogan, G.7
  • 57
    • 0016730832 scopus 로고
    • Substrate stereochemistry of the acetyl-CoA acetyltransferase reaction
    • Willadsen, P., and Eggerer, H. (1975) Substrate stereochemistry of the acetyl-CoA acetyltransferase reaction. Eur. J. Biochem. 54, 253-258.
    • (1975) Eur. J. Biochem. , vol.54 , pp. 253-258
    • Willadsen, P.1    Eggerer, H.2
  • 58
  • 59
    • 0034643811 scopus 로고    scopus 로고
    • Orientation of coenzyme a substrates, nicotinamide and active site functional groups in (di)enoyl-coenzyme A reductases
    • DOI 10.1021/bi0000566
    • Fillgrove, K. L., and Anderson, V. E. (2000) Orientation of coenzyme A substrates, nicotinamide and active site functional groups in (Di)enoylcoenzyme A reductases. Biochemistry 39, 7001-7011. (Pubitemid 30390394)
    • (2000) Biochemistry , vol.39 , Issue.23 , pp. 7001-7011
    • Fillgrove, K.L.1    Anderson, V.E.2
  • 60
    • 34249084726 scopus 로고    scopus 로고
    • Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis
    • DOI 10.1038/nature05702, PII NATURE05702
    • Widboom, P., Fielding, E. N., Liu, Y., and Bruner, S. D. (2007) Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis. Nature 447, 342-345. (Pubitemid 46788825)
    • (2007) Nature , vol.447 , Issue.7142 , pp. 342-345
    • Widboom, P.F.1    Fielding, E.N.2    Liu, Y.3    Bruner, S.D.4
  • 61
    • 37049015634 scopus 로고    scopus 로고
    • Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC
    • DOI 10.1021/bi701148b
    • Fielding, E. N., Widboom, P. F., and Bruner, S. D. (2007) Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC. Biochemistry 46, 13994-14000. (Pubitemid 350250296)
    • (2007) Biochemistry , vol.46 , Issue.49 , pp. 13994-14000
    • Fielding, E.N.1    Widboom, P.F.2    Bruner, S.D.3
  • 62
    • 2942565719 scopus 로고    scopus 로고
    • Evolution of function in the crotonase superfamily: The stereochemical course of the reaction catalyzed by 2-ketocyclohexanecarboxyl-CoA hydrolase
    • DOI 10.1021/ja0482381
    • Eberhard, E. D., and Gerlt, J. A. (2004) Evolution of function in the crotonase superfamily: The stereochemical course of the reaction catalyzed by 2-ketocyclohexanecarboxyl-CoA hydrolase. J. Am. Chem. Soc. 126, 7188-7189. (Pubitemid 38747764)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.23 , pp. 7188-7189
    • Eberhard, E.D.1    Gerlt, J.A.2
  • 63
    • 79959777970 scopus 로고    scopus 로고
    • Stabilization of the second oxyanion intermediate by 1,4-dihydroxy-2- naphthoyl coenzyme A synthase of the menaquinone pathway: Spectroscopic evidence of the involvement of a conserved aspartic acid
    • Chen, M., Jiang, M., Sun, Y., Guo, Z. F., and Guo, Z. (2011) Stabilization of the second oxyanion intermediate by 1,4-dihydroxy-2- naphthoyl coenzyme A synthase of the menaquinone pathway: Spectroscopic evidence of the involvement of a conserved aspartic acid. Biochemistry 50, 5893-5904.
    • (2011) Biochemistry , vol.50 , pp. 5893-5904
    • Chen, M.1    Jiang, M.2    Sun, Y.3    Guo, Z.F.4    Guo, Z.5
  • 64
    • 0033587656 scopus 로고    scopus 로고
    • Role of glutamate 144 and glutamate 164 in the catalytic mechanism of enoyl-CoA hydratase
    • Hofstein, H. A., Feng, Y., Anderson, V. E., and Tonge, P. J. (1999) Role of glutamate 144 and glutamate 164 in the catalytic mechanism of enoyl-CoA hydratase. Biochemistry 38, 9508-9516.
    • (1999) Biochemistry , vol.38 , pp. 9508-9516
    • Hofstein, H.A.1    Feng, Y.2    Anderson, V.E.3    Tonge, P.J.4
  • 65
    • 0037176907 scopus 로고    scopus 로고
    • Structural mechanism of enoyl-CoA hydratase: Three atoms from a single water are added in either an E1cb stepwise or concerted fashion
    • DOI 10.1021/bi015844p
    • Bahnson, B. J., Anderson, V. E., and Petsko., G. A. (2002) Structural mechanism of enoyl-CoA hydratase: Three atoms from a single water are added in either an E1cb stepwise or concerted fashion. Biochemistry 41, 2621-2629. (Pubitemid 34168931)
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2621-2629
    • Bahnson, B.J.1    Anderson, V.E.2    Petsko, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.