메뉴 건너뛰기




Volumn 43, Issue 22, 2004, Pages 7187-7196

Stereospecific alkylation of cis-3-chloroacrylic acid dehalogenase by (R)-oxirane-2-carboxylate: Analysis and mechanistic implications

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; BACTERIA; CHEMICAL BONDS; CRYSTALLOGRAPHY; DEHALOGENATION; HYDROLYSIS; MASS SPECTROMETRY; OXYGEN; SUBSTITUTION REACTIONS;

EID: 2642526986     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049823h     Document Type: Article
Times cited : (18)

References (28)
  • 1
    • 0034972743 scopus 로고    scopus 로고
    • trans-3-Chloroacrylic acid dehalogenase from Pseudomonas pavonaceae 170 shares structural and mechanistic similarities with 4-oxalocrotonate tautomerase
    • Poelarends, G. J., Saunier, R., and Janssen, D. B. (2001) trans-3-Chloroacrylic acid dehalogenase from Pseudomonas pavonaceae 170 shares structural and mechanistic similarities with 4-oxalocrotonate tautomerase, J. Bacteriol. 183, 4269-4277.
    • (2001) J. Bacteriol. , vol.183 , pp. 4269-4277
    • Poelarends, G.J.1    Saunier, R.2    Janssen, D.B.3
  • 2
    • 0041846667 scopus 로고    scopus 로고
    • Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: Consequences of and evidence for a hydration reaction
    • Wang, S. C., Person, M. D., Johnson, W. H., Jr., and Whitman, C. P. (2003) Reactions of trans-3-chloroacrylic acid dehalogenase with acetylene substrates: consequences of and evidence for a hydration reaction, Biochemistry 42, 8762-8773.
    • (2003) Biochemistry , vol.42 , pp. 8762-8773
    • Wang, S.C.1    Person, M.D.2    Johnson Jr., W.H.3    Whitman, C.P.4
  • 3
    • 1642576243 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a cis-3-chloroacrylic acid dehalogenase: Insights into the mechanistic, structural, and evolutionary relationship between isomer-specific 3-chloroacrylic acid dehalogenases
    • Poelarends, G. J., Serrano, H., Person, M. D., Johnson, W. H., Jr., Murzin, A. G., and Whitman, C. P. (2004) Cloning, expression, and characterization of a cis-3-chloroacrylic acid dehalogenase: insights into the mechanistic, structural, and evolutionary relationship between isomer-specific 3-chloroacrylic acid dehalogenases, Biochemistry 43, 759-772.
    • (2004) Biochemistry , vol.43 , pp. 759-772
    • Poelarends, G.J.1    Serrano, H.2    Person, M.D.3    Johnson Jr., W.H.4    Murzin, A.G.5    Whitman, C.P.6
  • 5
    • 1642483053 scopus 로고    scopus 로고
    • The X-ray structure of trans-3-chloroacrylic acid dehalogenase reveals a novel hydration mechanism in the tautomerase superfamily
    • de Jong, R. M., Brugman, W., Poelarends, G. J., Whitman, C. P., and Dijkstra, B. W. (2004) The X-ray structure of trans-3-chloroacrylic acid dehalogenase reveals a novel hydration mechanism in the tautomerase superfamily, J. Biol. Chem. 279, 11546-11552.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11546-11552
    • De Jong, R.M.1    Brugman, W.2    Poelarends, G.J.3    Whitman, C.P.4    Dijkstra, B.W.5
  • 6
    • 1842531456 scopus 로고    scopus 로고
    • The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: A kinetic, NMR, and mutational analysis
    • Azurmendi, H. F., Wang, S. C., Massiah, M. A., Poelarends, G. J., Whitman, C. P., and Mildvan, A. S. (2004) The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis, Biochemistry 43, 4082-4091.
    • (2004) Biochemistry , vol.43 , pp. 4082-4091
    • Azurmendi, H.F.1    Wang, S.C.2    Massiah, M.A.3    Poelarends, G.J.4    Whitman, C.P.5    Mildvan, A.S.6
  • 7
    • 85027424616 scopus 로고    scopus 로고
    • Ethyl glycidate from (S)-serine: Ethyl (R)-(+)-2,3-epoxypropanoate
    • Petit, Y., and Larcheveque, M. (1998) Ethyl glycidate from (S)-serine: ethyl (R)-(+)-2,3-epoxypropanoate, Org. Synth. 75, 37-44.
    • (1998) Org. Synth. , vol.75 , pp. 37-44
    • Petit, Y.1    Larcheveque, M.2
  • 8
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 9
    • 0001479670 scopus 로고
    • A simple ultraviolet spectrophotometric method for the determination of protein
    • Waddell, W. J. (1956) A simple ultraviolet spectrophotometric method for the determination of protein, J. Lab. Clin. Med. 48, 311-314.
    • (1956) J. Lab. Clin. Med. , vol.48 , pp. 311-314
    • Waddell, W.J.1
  • 10
    • 0030064737 scopus 로고    scopus 로고
    • Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: Affinity labeling and heteronuclear NMR studies
    • Stivers, J. T., Abeygunawardana, C., Mildvan, A. S., Hajipour, G., Whitman, C. P., and Chen, L. H. (1996) Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies, Biochemistry 35, 803-813.
    • (1996) Biochemistry , vol.35 , pp. 803-813
    • Stivers, J.T.1    Abeygunawardana, C.2    Mildvan, A.S.3    Hajipour, G.4    Whitman, C.P.5    Chen, L.H.6
  • 11
    • 1642494892 scopus 로고    scopus 로고
    • Reactions of 4-oxalocrotonate tautomerase and YwhB with 3-halopropiolates: Analysis and implications
    • Wang, S. C., Johnson, W. H., Jr., Czerwinski, R. M., and Whitman, C. P. (2004) Reactions of 4-oxalocrotonate tautomerase and YwhB with 3-halopropiolates: analysis and implications, Biochemistry 43, 748-758.
    • (2004) Biochemistry , vol.43 , pp. 748-758
    • Wang, S.C.1    Johnson Jr., W.H.2    Czerwinski, R.M.3    Whitman, C.P.4
  • 12
    • 0015452895 scopus 로고
    • Staphylococcal protease: A proteolytic enzyme specific for glutamoyl bonds
    • Houmard, J., and Drapeau, G. R. (1972) Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds, Proc. Natl. Acad. Sci. U.S.A. 69, 3506-3509.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 3506-3509
    • Houmard, J.1    Drapeau, G.R.2
  • 15
    • 0014119257 scopus 로고
    • Bromopyruvate inactivation of 2-keto-3-deoxy-6-phosphogluconic aldolase. I. Kinetic evidence for active site specificity
    • Meloche, H. P. (1967) Bromopyruvate inactivation of 2-keto-3-deoxy-6-phosphogluconic aldolase. I. Kinetic evidence for active site specificity, Biochemistry 6, 2273-2280.
    • (1967) Biochemistry , vol.6 , pp. 2273-2280
    • Meloche, H.P.1
  • 16
    • 0037986377 scopus 로고    scopus 로고
    • An integrated approach to identifying chemically induced posttranslational modifications using comparative MALDI-MS and targeted HPLC-ESI-MS/MS
    • Person, M. D., Monks, T. J., and Lau, S. S. (2003) An integrated approach to identifying chemically induced posttranslational modifications using comparative MALDI-MS and targeted HPLC-ESI-MS/MS, Chem. Res. Toxicol. 16, 598-608.
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 598-608
    • Person, M.D.1    Monks, T.J.2    Lau, S.S.3
  • 17
    • 0036612878 scopus 로고    scopus 로고
    • The 4-oxalocrotonate tautomerase family of enzymes: How nature makes new enzymes using a β-α-β structural motif
    • Whitman, C. P. (2002) The 4-oxalocrotonate tautomerase family of enzymes: how nature makes new enzymes using a β-α-β structural motif, Arch. Biochem. Biophys. 402, 1-13.
    • (2002) Arch. Biochem. Biophys. , vol.402 , pp. 1-13
    • Whitman, C.P.1
  • 18
    • 1542676972 scopus 로고    scopus 로고
    • Mechanistic characterization of a bacterial malonate semialdehyde decarboxylase: Identification of a new activity in the tautomerase superfamily
    • Poelarends, G. J., Johnson, W. H., Jr., Murzin, A. G., and Whitman, C. P. (2003) Mechanistic characterization of a bacterial malonate semialdehyde decarboxylase: identification of a new activity in the tautomerase superfamily, J. Biol. Chem. 278, 48674-48683.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48674-48683
    • Poelarends, G.J.1    Johnson Jr., W.H.2    Murzin, A.G.3    Whitman, C.P.4
  • 19
    • 0030060180 scopus 로고    scopus 로고
    • Enzymatic ketonization of 2-hydroxymuconate: Specificity and mechanism investigated by the crystal structures of two isomerases
    • Subramanya, H. S., Roper, D. I., Dauter, Z., Dodson, E. J., Davies, G. J., Wilson, K. S., and Wigley, D. B. (1996) Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases, Biochemistry 35, 792-802.
    • (1996) Biochemistry , vol.35 , pp. 792-802
    • Subramanya, H.S.1    Roper, D.I.2    Dauter, Z.3    Dodson, E.J.4    Davies, G.J.5    Wilson, K.S.6    Wigley, D.B.7
  • 20
    • 0033535983 scopus 로고    scopus 로고
    • Crystal structure of macrophage migration inhibitory factor complexed with (E)-2-fluoro-p-hydroxycinnamate at 1.8 Å resolution: Implications for enzymatic catalysis and inhibition
    • Taylor, A. B., Johnson, W. H., Jr., Czerwinski, R. M., Li, H.-S., Hackert, M. L., and Whitman, C. P. (1999) Crystal structure of macrophage migration inhibitory factor complexed with (E)-2-fluoro-p-hydroxycinnamate at 1.8 Å resolution: implications for enzymatic catalysis and inhibition, Biochemistry 38, 7444-7452.
    • (1999) Biochemistry , vol.38 , pp. 7444-7452
    • Taylor, A.B.1    Johnson Jr., W.H.2    Czerwinski, R.M.3    Li, H.-S.4    Hackert, M.L.5    Whitman, C.P.6
  • 21
    • 0037044309 scopus 로고    scopus 로고
    • The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli, confirms the structural basis for oligomer diversity
    • Almrud, J. J., Kern, A. D., Wang, S. C., Czerwinski, R. M., Johnson, W. H., Jr., Murzin, A. G., Hackert, M. L., and Whitman, C. P. (2002) The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli, confirms the structural basis for oligomer diversity, Biochemistry 41, 12010-12024.
    • (2002) Biochemistry , vol.41 , pp. 12010-12024
    • Almrud, J.J.1    Kern, A.D.2    Wang, S.C.3    Czerwinski, R.M.4    Johnson Jr., W.H.5    Murzin, A.G.6    Hackert, M.L.7    Whitman, C.P.8
  • 23
    • 0033835264 scopus 로고    scopus 로고
    • Site-directed mutagenesis of squalene-hopene cyclase: Altered substrate specificity and product distribution
    • Dang, T., and Prestwich, G. D. (2000) Site-directed mutagenesis of squalene-hopene cyclase: altered substrate specificity and product distribution, Chem. Biol. 7, 643-649.
    • (2000) Chem. Biol. , vol.7 , pp. 643-649
    • Dang, T.1    Prestwich, G.D.2
  • 24
    • 0028009918 scopus 로고
    • The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: Mechanistic and crystallographic evidence for stereospecific alkylation by (R)-α-phenylglycidate
    • Landro, J. A., Gerlt, J. A., Kozarich, J. W., Koo, C. W., Shah, V. J., Kenyon, G. L., Neidhart, D. J., Fujita, S., and Petsko, G. A. (1994) The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-α-phenylglycidate, Biochemistry 33, 635-643.
    • (1994) Biochemistry , vol.33 , pp. 635-643
    • Landro, J.A.1    Gerlt, J.A.2    Kozarich, J.W.3    Koo, C.W.4    Shah, V.J.5    Kenyon, G.L.6    Neidhart, D.J.7    Fujita, S.8    Petsko, G.A.9
  • 25
    • 0034194545 scopus 로고    scopus 로고
    • Epoxyalkyl glycosides of D-xylose and xylo-oligosaccharides are active-site markers of xylanases from glycoside hydrolase family 11, not from family 10
    • Ntarima, P., Nerinckx, W., Klarskov, K., Devreese, B., Mahalingeshwara, K. B., Van Beeumen, J., and Claeyssens, M. (2000) Epoxyalkyl glycosides of D-xylose and xylo-oligosaccharides are active-site markers of xylanases from glycoside hydrolase family 11, not from family 10, Biochem. J. 347, 865-873.
    • (2000) Biochem. J. , vol.347 , pp. 865-873
    • Ntarima, P.1    Nerinckx, W.2    Klarskov, K.3    Devreese, B.4    Mahalingeshwara, K.B.5    Van Beeumen, J.6    Claeyssens, M.7
  • 26
    • 0003922512 scopus 로고    scopus 로고
    • Prentice-Hall, Upper Saddle River, NJ
    • Wade, L. G., Jr. (1999) Organic Chemistry, 4th ed., pp 1045-1048, Prentice-Hall, Upper Saddle River, NJ.
    • (1999) Organic Chemistry, 4th Ed. , pp. 1045-1048
    • Wade Jr., L.G.1
  • 27
    • 2642570710 scopus 로고
    • Buffer catalysis in epoxide hydrolyses
    • Whalen, D. L. (1973) Buffer catalysis in epoxide hydrolyses, J. Am. Chem. Soc. 95, 3432-3434.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 3432-3434
    • Whalen, D.L.1
  • 28
    • 0029744988 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors
    • Meara, J. P., and Rich, D. H. (1996) Mechanistic studies on the inactivation of papain by epoxysuccinyl inhibitors. J. Med. Chem 39, 3357-3366.
    • (1996) J. Med. Chem. , vol.39 , pp. 3357-3366
    • Meara, J.P.1    Rich, D.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.