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Volumn 46, Issue 33, 2007, Pages 9596-9604

Phenylpyruvate tautomerase activity of trans-3-chloroacrylic acid dehalogenase: Evidence for an enol intermediate in the dehalogenase reaction?

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMATIC CONVERSION; HYDROLYTIC DEHALOGENASES; PARTIAL REACTIONS; PHENYLPYRUVATE TAUTOMERASE (PPT) ACTIVITY;

EID: 34548090241     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7007189     Document Type: Article
Times cited : (16)

References (49)
  • 1
    • 0011919360 scopus 로고    scopus 로고
    • Microbial dehalogenases
    • Barton, D, and Nakanishi, K, Eds, Elsevier, Amsterdam
    • Copley, S. D. (1999) Microbial dehalogenases, in Comprehensive Natural Products Chemistry (Barton, D., and Nakanishi, K., Eds.) Vol. 5, pp 401-422, Elsevier, Amsterdam.
    • (1999) Comprehensive Natural Products Chemistry , vol.5 , pp. 401-422
    • Copley, S.D.1
  • 3
    • 0026398921 scopus 로고
    • Bacterial degradation of 3-chloroacrylic acid and the characterization of cis- and trans-specific dehalogenases
    • van Hylckama Vlieg, J. E. T., and Janssen, D. B. (1992) Bacterial degradation of 3-chloroacrylic acid and the characterization of cis- and trans-specific dehalogenases, Biodegradation 2, 139-150.
    • (1992) Biodegradation , vol.2 , pp. 139-150
    • van Hylckama Vlieg, J.E.T.1    Janssen, D.B.2
  • 5
    • 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
  • 6
    • 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
  • 7
    • 1842531456 scopus 로고    scopus 로고
    • The roles of activesite 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 activesite 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
  • 8
    • 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
  • 9
    • 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
  • 10
    • 2642526986 scopus 로고    scopus 로고
    • Stereospecific alkylation of cis-chloroacrylic acid dehalogenase by (R)-oxirane-2-carboxylate: Analysis and mechanistic implications
    • Poelarends, G. J., Serrano, H., Johnson, W. H., Jr., and Whitman, C. P. (2004) Stereospecific alkylation of cis-chloroacrylic acid dehalogenase by (R)-oxirane-2-carboxylate: Analysis and mechanistic implications, Biochemistry 43, 7187-7196.
    • (2004) Biochemistry , vol.43 , pp. 7187-7196
    • Poelarends, G.J.1    Serrano, H.2    Johnson Jr., W.H.3    Whitman, C.P.4
  • 11
    • 34047269260 scopus 로고    scopus 로고
    • Crystal structures of native and inactivated cis-3-chloroacrylic acid dehalogenase: Structural basis for substrate specificity and inactivation by (R)-oxirane-2-carboxylate
    • de Jong, R. M., Bazzacco, P., Poelarends, G. J., Johnson, W. H., Jr., Kim, Y.-J., Burks, E. A., Serrano, H., Thunnissen, A.-M. W. H., Whitman, C. P., and Dijkstra, B. W. (2007) Crystal structures of native and inactivated cis-3-chloroacrylic acid dehalogenase: Structural basis for substrate specificity and inactivation by (R)-oxirane-2-carboxylate, J. Biol. Chem. 282, 2440-2449.
    • (2007) J. Biol. Chem , vol.282 , pp. 2440-2449
    • de Jong, R.M.1    Bazzacco, P.2    Poelarends, G.J.3    Johnson Jr., W.H.4    Kim, Y.-J.5    Burks, E.A.6    Serrano, H.7    Thunnissen, A.-M.W.H.8    Whitman, C.P.9    Dijkstra, B.W.10
  • 12
    • 0029950031 scopus 로고    scopus 로고
    • Structural classification of proteins: New superfamilies
    • Murzin, A. G. (1996) Structural classification of proteins: New superfamilies, Curr. Opin. Struct. Biol. 6, 386-394.
    • (1996) Curr. Opin. Struct. Biol , vol.6 , pp. 386-394
    • Murzin, A.G.1
  • 13
    • 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
  • 14
    • 4644358158 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the tautomerase superfamily: Mechanistic and structural studies of the 1,3-dichloropropene catabolic enzymes
    • Poelarends, G. J., and Whitman, C. P. (2004) Evolution of enzymatic activity in the tautomerase superfamily: Mechanistic and structural studies of the 1,3-dichloropropene catabolic enzymes, Bioorg. Chem. 32, 376-392.
    • (2004) Bioorg. Chem , vol.32 , pp. 376-392
    • Poelarends, G.J.1    Whitman, C.P.2
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0032516444 scopus 로고    scopus 로고
    • Characterization of the role of the amino-terminal proline in the enzymatic activity catalyzed by macrophage migration inhibitory factor
    • Stamps, S. L., Fitzgerald, M. C., and Whitman, C. P. (1998) Characterization of the role of the amino-terminal proline in the enzymatic activity catalyzed by macrophage migration inhibitory factor, Biochemistry 37, 10195-10202.
    • (1998) Biochemistry , vol.37 , pp. 10195-10202
    • Stamps, S.L.1    Fitzgerald, M.C.2    Whitman, C.P.3
  • 18
    • 0033535983 scopus 로고    scopus 로고
    • Crystal structure of macrophage migration inhibitory factor complexed with (E)-2fluoro-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)-2fluoro-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
  • 19
    • 0040142161 scopus 로고    scopus 로고
    • A kinetic and stereochemical investigation of the role of lysine-32 in the phenylpyruvate tautomerase activity catalyzed by macrophage migration inhibitory factor
    • Johnson, W. H., Jr., Czerwinski, R. M., Stamps, S. L., and Whitman, C. P. (1999) A kinetic and stereochemical investigation of the role of lysine-32 in the phenylpyruvate tautomerase activity catalyzed by macrophage migration inhibitory factor, Biochemistry 38, 16024-16033.
    • (1999) Biochemistry , vol.38 , pp. 16024-16033
    • Johnson Jr., W.H.1    Czerwinski, R.M.2    Stamps, S.L.3    Whitman, C.P.4
  • 20
    • 0001628218 scopus 로고
    • Stereochemistry of Krebs' cycle hydrations and related reactions
    • Gawron, O., Glaid, A. J., and Fondy, T. P. (1961) Stereochemistry of Krebs' cycle hydrations and related reactions, J. Am. Chem. Soc. 83, 3634-3640.
    • (1961) J. Am. Chem. Soc , vol.83 , pp. 3634-3640
    • Gawron, O.1    Glaid, A.J.2    Fondy, T.P.3
  • 21
    • 0014198255 scopus 로고
    • Stereochemical course of the maleate hydratase reaction
    • Englard, S., Britten, J. S., and Listowsky, I. (1967) Stereochemical course of the maleate hydratase reaction, J. Biol. Chem. 242, 2255-2259.
    • (1967) J. Biol. Chem , vol.242 , pp. 2255-2259
    • Englard, S.1    Britten, J.S.2    Listowsky, I.3
  • 22
    • 0000811657 scopus 로고
    • Enzymic catalysis of the ketoenol tautomerization of phenylpyruvic acids
    • Knox, W. E., and Pitt, B. M. (1957) Enzymic catalysis of the ketoenol tautomerization of phenylpyruvic acids, J. Biol. Chem. 225, 675-688.
    • (1957) J. Biol. Chem , vol.225 , pp. 675-688
    • Knox, W.E.1    Pitt, B.M.2
  • 23
    • 0014690910 scopus 로고
    • Thyroidal phenylpyruvate tautomerase. Isolation and characterization
    • Blasi, F., Fragomele, F., and Covelli, I. (1969) Thyroidal phenylpyruvate tautomerase. Isolation and characterization, J. Biol Chem. 244, 4864-4870.
    • (1969) J. Biol Chem , vol.244 , pp. 4864-4870
    • Blasi, F.1    Fragomele, F.2    Covelli, I.3
  • 24
    • 0033615270 scopus 로고    scopus 로고
    • Enzymatic mechanism of thyroxine biosynthesis: Identification of the lost three-carbon fragment
    • Ma, Y.-A., Sih, C. J., and Harms, A. (1999) Enzymatic mechanism of thyroxine biosynthesis: Identification of the "lost three-carbon fragment", J. Am. Chem. Soc. 121, 8967-8968.
    • (1999) J. Am. Chem. Soc. 121 , pp. 8967-8968
    • Ma, Y.-A.1    Sih, C.J.2    Harms, A.3
  • 25
    • 0017325604 scopus 로고
    • Stereospecificity of phenylpyruvate tautomerase. A convenient method for the preparation of chirally labeled phenylpyruvates
    • Retey, J., Bartl, K., Ripp, E., and Hull, W. E. (1977) Stereospecificity of phenylpyruvate tautomerase. A convenient method for the preparation of chirally labeled phenylpyruvates, Eur. J. Biochem. 72, 251-257.
    • (1977) Eur. J. Biochem , vol.72 , pp. 251-257
    • Retey, J.1    Bartl, K.2    Ripp, E.3    Hull, W.E.4
  • 26
    • 0000949242 scopus 로고
    • Mechanistic and stereochemical study of phenylpyruvate tautomerase
    • Pirrung, M. C., Chen, J., Rowley, E. G., and McPhail, A. T. (1993) Mechanistic and stereochemical study of phenylpyruvate tautomerase, J. Am. Chem. Soc. 115, 7103-7110.
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 7103-7110
    • Pirrung, M.C.1    Chen, J.2    Rowley, E.G.3    McPhail, A.T.4
  • 28
    • 84873780558 scopus 로고
    • In vitro cell migration as a model for delayed hypersensitivity
    • George, M., and Vaughan, J. H. (1962) In vitro cell migration as a model for delayed hypersensitivity, Proc. Soc. Exp. Biol. Med. 111, 514-521.
    • (1962) Proc. Soc. Exp. Biol. Med , vol.111 , pp. 514-521
    • George, M.1    Vaughan, J.H.2
  • 29
    • 0013933261 scopus 로고
    • Mechanism of a reaction in vitro associated with delayed-type hypersensitivity
    • Bloom, B. R., and Bennett, B. (1966) Mechanism of a reaction in vitro associated with delayed-type hypersensitivity, Science 153, 80-82.
    • (1966) Science , vol.153 , pp. 80-82
    • Bloom, B.R.1    Bennett, B.2
  • 30
    • 0013923944 scopus 로고
    • Delayed hypersensitivity in vitro: Its mediation by cell-free substances formed by lymphoid cell-antigen interaction
    • David, J. R. (1966) Delayed hypersensitivity in vitro: Its mediation by cell-free substances formed by lymphoid cell-antigen interaction, Proc. Natl. Acad. Sci. U.S.A. 56, 72-77.
    • (1966) Proc. Natl. Acad. Sci. U.S.A , vol.56 , pp. 72-77
    • David, J.R.1
  • 33
    • 0037067777 scopus 로고    scopus 로고
    • The tautomerase active site of macrophage migration inhibitory factor is a potential target for discovery of novel anti-inflammatory agents
    • Lubetsky, J., Dios, A., Han, J., Aljabari, B., Ruzsicska, B., Mitchell, R., Lolis, E., and Al-Abed, Y. (2002) The tautomerase active site of macrophage migration inhibitory factor is a potential target for discovery of novel anti-inflammatory agents, J. Biol. Chem. 277, 24976-24982.
    • (2002) J. Biol. Chem , vol.277 , pp. 24976-24982
    • Lubetsky, J.1    Dios, A.2    Han, J.3    Aljabari, B.4    Ruzsicska, B.5    Mitchell, R.6    Lolis, E.7    Al-Abed, Y.8
  • 34
    • 0034664028 scopus 로고    scopus 로고
    • Mechanism of the phenylpyruvate tautomerase activity of macrophage migration inhibitory factor: Properties of the P1G, P1A, Y95F, and N97A mutants
    • Stamps, S. L., Taylor, A. B., Wang, S. C., Hackert, M. L., and Whitman, C. P. (2000) Mechanism of the phenylpyruvate tautomerase activity of macrophage migration inhibitory factor: Properties of the P1G, P1A, Y95F, and N97A mutants, Biochemistry 39, 9671-9678.
    • (2000) Biochemistry , vol.39 , pp. 9671-9678
    • Stamps, S.L.1    Taylor, A.B.2    Wang, S.C.3    Hackert, M.L.4    Whitman, C.P.5
  • 36
    • 0029895838 scopus 로고    scopus 로고
    • Crystal structure at 2.6 Å resolution of human macrophage migration inhibitory factor
    • Sun, H.-W., Bernhagen, J., Bucala, R., and Lolis, E. (1996) Crystal structure at 2.6 Å resolution of human macrophage migration inhibitory factor, Proc. Natl. Acad. Sci. U.S.A. 93, 5191-5196.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 5191-5196
    • Sun, H.-W.1    Bernhagen, J.2    Bucala, R.3    Lolis, E.4
  • 37
    • 0033153283 scopus 로고    scopus 로고
    • Pro-1 of macrophage migration inhibitory factor functions as a catalytic base in the phenylpyruvate tautomerase activity
    • Lubetsky, J., Swope, M., Dealwis, C., Blake, P., and Lolis, E. (1999) Pro-1 of macrophage migration inhibitory factor functions as a catalytic base in the phenylpyruvate tautomerase activity, Biochemistry 38, 7346-7354.
    • (1999) Biochemistry , vol.38 , pp. 7346-7354
    • Lubetsky, J.1    Swope, M.2    Dealwis, C.3    Blake, P.4    Lolis, E.5
  • 38
    • 28044449591 scopus 로고    scopus 로고
    • A persistent pesticide residue and the unusual catalytic proficiency of a dehalogenating enzyme
    • Horvat, C. M., and Wolfenden, R. V. (2005) A persistent pesticide residue and the unusual catalytic proficiency of a dehalogenating enzyme, Proc. Natl. Acad. Sci. U.S.A. 102, 16199-16202.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 16199-16202
    • Horvat, C.M.1    Wolfenden, R.V.2
  • 39
    • 33746914768 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the tautomerase superfamily: Mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase
    • Poelarends, G. J., Almrud, J. J., Serrano, H., Darty, J. E., Johnson, W. H., Jr., Hackert, M. L., and Whitman, C. P. (2006) Evolution of enzymatic activity in the tautomerase superfamily: Mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase, Biochemistry 45, 7700-7708.
    • (2006) Biochemistry , vol.45 , pp. 7700-7708
    • Poelarends, G.J.1    Almrud, J.J.2    Serrano, H.3    Darty, J.E.4    Johnson Jr., W.H.5    Hackert, M.L.6    Whitman, C.P.7
  • 40
    • 1542691395 scopus 로고
    • Preparation and properties of enolpyruvate
    • Peliska, J. A., and O'Leary, M. H. (1991) Preparation and properties of enolpyruvate, J. Am. Chem. Soc. 113, 1841-1842.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 1841-1842
    • Peliska, J.A.1    O'Leary, M.H.2
  • 41
    • 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
  • 42
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien, P. J., and Herschlag, D. (1999) Catalytic promiscuity and the evolution of new enzymatic activities, Chem. Biol. 6, R91-R105.
    • (1999) Chem. Biol , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 43
    • 0035873714 scopus 로고    scopus 로고
    • Functional interrelationships in the alkaline phosphatase superfamily: Phosphodiesterase activity of Escherichia coli alkaline phosphatase
    • O'Brien, P. J., and Herschlag, D. (2001) Functional interrelationships in the alkaline phosphatase superfamily: Phosphodiesterase activity of Escherichia coli alkaline phosphatase, Biochemistry 40, 5691-5699.
    • (2001) Biochemistry , vol.40 , pp. 5691-5699
    • O'Brien, P.J.1    Herschlag, D.2
  • 44
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • Copley, S. D. (2003) Enzymes with extra talents: Moonlighting functions and catalytic promiscuity, Curr. Opin. Chem. Biol. 7, 265-272.
    • (2003) Curr. Opin. Chem. Biol , vol.7 , pp. 265-272
    • Copley, S.D.1
  • 45
    • 25444456889 scopus 로고    scopus 로고
    • Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily
    • Roodveldt, C., and Tawfik, D. S. (2005) Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily, Biochemistry 44, 12728-12736.
    • (2005) Biochemistry , vol.44 , pp. 12728-12736
    • Roodveldt, C.1    Tawfik, D.S.2
  • 46
    • 13544277381 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: Enhancing the promiscuous D-arabino-hex-3- ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase
    • Yew, W. S., Akana, J., Wise, E. L., Rayment, I., and Gerlt, J. A. (2005) Evolution of enzymatic activities in the orotidine 5′-monophosphate decarboxylase suprafamily: Enhancing the promiscuous D-arabino-hex-3- ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, Biochemistry 44, 1807-1815.
    • (2005) Biochemistry , vol.44 , pp. 1807-1815
    • Yew, W.S.1    Akana, J.2    Wise, E.L.3    Rayment, I.4    Gerlt, J.A.5
  • 47
    • 0344012191 scopus 로고    scopus 로고
    • The 4-oxalocrotonate tautomerase- and YwhB-catalyzed hydration of 3E-haloacrylates: Implications for 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 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
  • 48
    • 10044221852 scopus 로고    scopus 로고
    • The hydratase activity of malonate semialdehyde decarboxylase: Mechanistic and evolutionary implications
    • Poelarends, G. J., Serrano, H., Johnson, W. H., Jr., Hoffman, D. W., and Whitman, C. P. (2004) The hydratase activity of malonate semialdehyde decarboxylase: Mechanistic and evolutionary implications, J. Am. Chem. Soc. 126, 15658-15659.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 15658-15659
    • Poelarends, G.J.1    Serrano, H.2    Johnson Jr., W.H.3    Hoffman, D.W.4    Whitman, C.P.5
  • 49
    • 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


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