메뉴 건너뛰기




Volumn 43, Issue 3, 2004, Pages 748-758

Reactions of 4-Oxalocrotonate Tautomerase and YwhB with 3-Halopropiolates: Analysis and Implications

Author keywords

[No Author keywords available]

Indexed keywords

ADDITION REACTIONS; ALDEHYDES; CATALYSIS; CHEMICAL MODIFICATION; ENZYME INHIBITION; ENZYMES; ISOMERIZATION; ORGANIC ACIDS; UNSATURATED COMPOUNDS;

EID: 1642494892     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035495u     Document Type: Article
Times cited : (12)

References (37)
  • 1
    • 0021124798 scopus 로고
    • Transposon mutagenesis analysis of meta-cleavage pathway operon genes of the TOL plasmid of Pseudomonas putida mt-2
    • Harayama, S., Lehrbach, P. R., and Timmis, K. N. (1984) Transposon mutagenesis analysis of meta-cleavage pathway operon genes of the TOL plasmid of Pseudomonas putida mt-2, J. Bacteriol. 160, 251-255.
    • (1984) J. Bacteriol. , vol.160 , pp. 251-255
    • Harayama, S.1    Lehrbach, P.R.2    Timmis, K.N.3
  • 2
    • 0001600177 scopus 로고
    • Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol
    • Whitman, C. P., Aird, B. A., Gillespie, W. R., and Stolowich, N. J. (1991) Chemical and enzymatic ketonization of 2-hydroxymuconate, a conjugated enol, J. Am. Chem. Soc. 113, 3154-3162.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 3154-3162
    • Whitman, C.P.1    Aird, B.A.2    Gillespie, W.R.3    Stolowich, N.J.4
  • 4
    • 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
  • 5
    • 0028810542 scopus 로고
    • Total chemical synthesis and catalytic properties of the enzyme enantiomers L- and D-4-oxalocrotonate tautomerase
    • Fitzgerald, M. C., Chernushevich, I., Standing, K. G., Kent, S. B. H., and Whitman, C. P. (1995) Total chemical synthesis and catalytic properties of the enzyme enantiomers L- and D-4-oxalocrotonate tautomerase. J. Am. Chem. Soc. 117, 11075-11080.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11075-11080
    • Fitzgerald, M.C.1    Chernushevich, I.2    Standing, K.G.3    Kent, S.B.H.4    Whitman, C.P.5
  • 6
    • 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
  • 8
    • 0030723733 scopus 로고    scopus 로고
    • Kinetic and structural effects of mutations of the catalytic amino-terminal proline in 4-oxalocrotonate tautomerase
    • Czerwinski, R. M., Johnson, W. H., Jr., Whitman, C. P., Harris, T. K., Abeygunawardana, C., and Mildvan, A. S. (1997) Kinetic and structural effects of mutations of the catalytic amino-terminal proline in 4-oxalocrotonate tautomerase, Biochemistry 36, 14551-14560.
    • (1997) Biochemistry , vol.36 , pp. 14551-14560
    • Czerwinski, R.M.1    Johnson Jr., W.H.2    Whitman, C.P.3    Harris, T.K.4    Abeygunawardana, C.5    Mildvan, A.S.6
  • 9
    • 0032553015 scopus 로고    scopus 로고
    • Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2-oxo-3-pentynoate at 2.4 Å resolution: Analysis and implications for the mechanism of inactivation and catalysis
    • Taylor, A. B., Czerwinski, R. M., Johnson, W. H., Jr., Whitman, C. P., and Hackert, M. L. (1998) Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2-oxo-3-pentynoate at 2.4 Å resolution: analysis and implications for the mechanism of inactivation and catalysis, Biochemistry 37, 14692-14700.
    • (1998) Biochemistry , vol.37 , pp. 14692-14700
    • Taylor, A.B.1    Czerwinski, R.M.2    Johnson Jr., W.H.3    Whitman, C.P.4    Hackert, M.L.5
  • 13
    • 0032191798 scopus 로고    scopus 로고
    • The contribution of the substrate's carboxylate group to the mechanism of 4-oxalocrotonate tautomerase
    • Lian, H., Czerwinski, R. M., Stanley, T. M., Johnson, W. H., Jr., Watson, R. J., and Whitman, C. P (1998) The contribution of the substrate's carboxylate group to the mechanism of 4-oxalocrotonate tautomerase, Bioorg. Chem. 26, 141-156.
    • (1998) Bioorg. Chem. , vol.26 , pp. 141-156
    • Lian, H.1    Czerwinski, R.M.2    Stanley, T.M.3    Johnson Jr., W.H.4    Watson, R.J.5    Whitman, C.P.6
  • 14
    • 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
  • 16
    • 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
  • 17
    • 0345671227 scopus 로고    scopus 로고
    • New role for the amino-terminal proline in the tautomerase superfamily: trans-3-chloroacrylic acid dehalogenase
    • Azurmendi, H. F., Wang, S. C., Massiah, M. A., Whitman, C. P., and Mildvan, A. S. (2003) New role for the amino-terminal proline in the tautomerase superfamily: trans-3-chloroacrylic acid dehalogenase, Biochemistry 42, 8619.
    • (2003) Biochemistry , vol.42 , pp. 8619
    • Azurmendi, H.F.1    Wang, S.C.2    Massiah, M.A.3    Whitman, C.P.4    Mildvan, A.S.5
  • 18
    • 0344012191 scopus 로고    scopus 로고
    • The 4-oxalocrotonate tautomerase-and YwhB-catalyzed hydration of 3E-haloacrylates: Implications for the evolution of new enzymatic activities
    • Wang, S. C., Johnson, W. H., Jr., and Whitman, C. P. (2003) The 4-oxalocrotonate tautomerase-and YwhB-catalyzed hydration of 3E-haloacrylates: Implications for the evolution of new enzymatic activities, J. Am. Chem. Soc. 125, 14282-14283.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14282-14283
    • Wang, S.C.1    Johnson Jr., W.H.2    Whitman, C.P.3
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0001537739 scopus 로고
    • Replacement of positive hydrogen by halogen. I
    • Strauss, F., Kollek, L., Heyn, W., and Kuhnel, R. (1930) Replacement of positive hydrogen by halogen. I, Chem. Ber. 63B, 1868-1885.
    • (1930) Chem. Ber. , vol.63 B , pp. 1868-1885
    • Strauss, F.1    Kollek, L.2    Heyn, W.3    Kuhnel, R.4
  • 22
    • 0042600592 scopus 로고
    • Additions to propiolic and halogen substituted propiolic acids
    • Andersson, K. (1972) Additions to propiolic and halogen substituted propiolic acids, Chem. Scripta 2, 117-120.
    • (1972) Chem. Scripta , vol.2 , pp. 117-120
    • Andersson, K.1
  • 23
    • 0032511427 scopus 로고    scopus 로고
    • Stereochemical and isotopic labeling studies of 2-oxo-hept-4-ene-1,7-dioate hydratase: Evidence for an enzyme-catalyzed ketonization step in the hydration reaction
    • Burks, E. A., Johnson, W. H., Jr., and Whitman, C. P. (1998) Stereochemical and isotopic labeling studies of 2-oxo-hept-4-ene-1,7-dioate hydratase: evidence for an enzyme-catalyzed ketonization step in the hydration reaction, J. Am. Chem. Soc. 120, 7665-7675.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7665-7675
    • Burks, E.A.1    Johnson Jr., W.H.2    Whitman, C.P.3
  • 25
    • 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
  • 26
    • 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
  • 27
    • 0033535983 scopus 로고    scopus 로고
    • Crystal structure of macrophage migration inhibitory factor complexed with (E)-2-fluoro-p-hydroxycinnamate at 1.8 A 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 A 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
  • 30
    • 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
  • 31
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R. A. (1976) Enzyme recruitment in evolution of new function, Annu. Rev. Microbiol. 30, 409-425.
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 32
    • 0028342845 scopus 로고
    • The evolution of functionally novel proteins after gene duplication
    • Hughes, A. L. (1994) The evolution of functionally novel proteins after gene duplication, Proc. R. Soc. London B 256, 119-124.
    • (1994) Proc. R. Soc. London B , vol.256 , pp. 119-124
    • Hughes, A.L.1
  • 33
    • 0030667789 scopus 로고    scopus 로고
    • Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities
    • Babbitt, P. C., and Gerlt, J. A. (1997) Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities, J. Biol. Chem. 272, 30591-30594.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30591-30594
    • Babbitt, P.C.1    Gerlt, J.A.2
  • 34
    • 0011919360 scopus 로고    scopus 로고
    • (Barton, D., and Nakanishi, Eds.), Elsevier Science Ltd., Oxford, U.K.
    • Copley, S. D. (1999) in Comprehensive Natural Products Chemistry (Barton, D., and Nakanishi, Eds.) Vol. 5, pp 401-422, Elsevier Science Ltd., Oxford, U.K.
    • (1999) Comprehensive Natural Products Chemistry , vol.5 , pp. 401-422
    • Copley, S.D.1
  • 35
    • 0035873714 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien, P. J., and Herschlag, D. (2001) Catalytic promiscuity and the evolution of new enzymatic activities, Biochemistry 40, 5691-5699.
    • (2001) Biochemistry , vol.40 , pp. 5691-5699
    • O'Brien, P.J.1    Herschlag, D.2
  • 36
    • 0033528659 scopus 로고    scopus 로고
    • Unexpected divergence of enzyme function and sequence: N-acylamino acid racemase is o-succinylbenzoate synthase
    • Palmer, D. R. J., Garrett, J. B., Sharma, V., Meganathan, R., Babbitt, P. C., and Gerlt, J. A. (1999) Unexpected divergence of enzyme function and sequence: N-acylamino acid racemase is o-succinylbenzoate synthase, Biochemistry 38, 4252-4258.
    • (1999) Biochemistry , vol.38 , pp. 4252-4258
    • Palmer, D.R.J.1    Garrett, J.B.2    Sharma, V.3    Meganathan, R.4    Babbitt, P.C.5    Gerlt, J.A.6
  • 37
    • 0003922512 scopus 로고    scopus 로고
    • Prentice-Hall, Inc., Upper Saddle River, NJ
    • Wade, L. G., Jr. (1999) Organic Chemistry, 4th ed., pp 1045-1048, Prentice-Hall, Inc., Upper Saddle River, NJ.
    • (1999) Organic Chemistry, 4th Ed. , pp. 1045-1048
    • Wade Jr., L.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.