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Volumn 43, Issue 1, 2004, Pages 224-229

Evolution of Enzymatic Activity in the Enolase Superfamily: Functional Studies of the Promiscuous o-Succinylbenzoate Synthase from Amycolatopsis

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSTS; DEHYDRATION; NEGATIVE IONS; PROTONS; SUBSTRATES;

EID: 0346096856     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035815+     Document Type: Article
Times cited : (63)

References (20)
  • 2
    • 0034923923 scopus 로고    scopus 로고
    • Divergent Evolution of Enzymatic Function: Mechanistically Diverse Superfamilies and Functionally Distinct Suprafamilies
    • Gerlt, J. A., and Babbitt, P. C. (2001) Divergent Evolution of Enzymatic Function: Mechanistically Diverse Superfamilies and Functionally Distinct Suprafamilies, Annu. Rev. Biochem. 70, 209-46.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 3
    • 0035951059 scopus 로고    scopus 로고
    • Evolution of Enzymatic Activities in the Enolase Superfamily: Functional Assignment of Unknown Proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu Epimerases
    • Schmidt, D. M., Hubbard, B. K., and Gerlt, J. A. (2001) Evolution of Enzymatic Activities in the Enolase Superfamily: Functional Assignment of Unknown Proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu Epimerases, Biochemistry 40, 15707-15.
    • (2001) Biochemistry , vol.40 , pp. 15707-15715
    • Schmidt, D.M.1    Hubbard, B.K.2    Gerlt, J.A.3
  • 4
    • 0000036588 scopus 로고    scopus 로고
    • (Neidhart, F. C., Curtiss, R., Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M., and Umbarger, H. E., Eds.), ASM Press, Washington, DC
    • Meganathan, R. (1996) in Escherichia coli and Salmonella (Neidhart, F. C., Curtiss, R., Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., Reznikoff, W. S., Riley, M., Schaechter, M., and Umbarger, H. E., Eds.) pp 642-56, ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella , pp. 642-656
    • Meganathan, R.1
  • 6
    • 0033528659 scopus 로고    scopus 로고
    • Unexpected divergence of enzyme function and sequence: N-acylamino acid racemase is o-succinylbenzoate synthase
    • Palmer, D. R., 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, 4252-8.
    • (1999) Biochemistry , vol.38 , pp. 4252-4258
    • Palmer, D.R.1    Garrett, J.B.2    Sharma, V.3    Meganathan, R.4    Babbitt, P.C.5    Gerlt, J.A.6
  • 7
    • 0034812536 scopus 로고    scopus 로고
    • The Lesser Burden Borne by o-Succinylbenzoate Synthase: An Easy Reaction Involving a Carboxylate Carbon Acid
    • Taylor, E. A., Palmer, D. R., and Gerlt, J. A. (2001) The Lesser Burden Borne by o-Succinylbenzoate Synthase: An Easy Reaction Involving a Carboxylate Carbon Acid, J. Am. Chem. Soc. 123, 5824-5.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5824-5825
    • Taylor, E.A.1    Palmer, D.R.2    Gerlt, J.A.3
  • 8
    • 0031034356 scopus 로고    scopus 로고
    • Mandelate racemase in pieces: Effective concentrations of enzyme functional groups in the transition state
    • Bearne, S. L., and Wolfenden, R. (1997) Mandelate racemase in pieces: effective concentrations of enzyme functional groups in the transition state, Biochemistry 36, 1646-56.
    • (1997) Biochemistry , vol.36 , pp. 1646-1656
    • Bearne, S.L.1    Wolfenden, R.2
  • 9
    • 0028836452 scopus 로고
    • Enzyme hydration of an olefin: The burden borne by fumarase
    • Bearne, S. L., and Wolfenden, R. (1995) Enzyme hydration of an olefin: the burden borne by fumarase, J. Am. Chem. Soc. 117, 9588-89.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 9588-9589
    • Bearne, S.L.1    Wolfenden, R.2
  • 10
    • 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
  • 11
    • 0028906783 scopus 로고
    • Cloning, DNA sequencing, and heterologous expression of the gene for thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60 in Escherichia coli
    • Tokuyama, S., and Hatano, K. (1995) Cloning, DNA sequencing, and heterologous expression of the gene for thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60 in Escherichia coli, Appl. Microbiol. Biotechnol. 42, 884-9.
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 884-889
    • Tokuyama, S.1    Hatano, K.2
  • 12
    • 0028898770 scopus 로고
    • Purification and properties of thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60
    • Tokuyama, S., and Hatano, K. (1995) Purification and properties of thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60, Appl. Microbiol. Biotechnol. 42, 853-9.
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 853-859
    • Tokuyama, S.1    Hatano, K.2
  • 13
    • 0034609515 scopus 로고    scopus 로고
    • Evolution of enzymatic activity in the enolase superfamily: Structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg(II) and o-succinylbenzoate
    • Thompson, T. B., Garrett, J. B., Taylor, E. A., Meganathan, R., Gerlt, J. A., and Rayment, I. (2000) Evolution of enzymatic activity in the enolase superfamily: Structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg(II) and o-succinylbenzoate, Biochemistry 39, 10662-76.
    • (2000) Biochemistry , vol.39 , pp. 10662-10676
    • Thompson, T.B.1    Garrett, J.B.2    Taylor, E.A.3    Meganathan, R.4    Gerlt, J.A.5    Rayment, I.6
  • 14
    • 0347752397 scopus 로고    scopus 로고
    • Evolution of Enzymatic Activity in the Enolase Superfamily: Structural and Mutagenic Studies of the Mechanism of the Reaction Catalyzed by o-Succinylbenzoate Synthase from Escherichia coli
    • Klenchin, D., Taylor Ringia, E. A., Gerlt, J. A., and Rayment, I. (2003) Evolution of Enzymatic Activity in the Enolase Superfamily: Structural and Mutagenic Studies of the Mechanism of the Reaction Catalyzed by o-Succinylbenzoate Synthase from Escherichia coli, Biochemistry 42, 14427-33.
    • (2003) Biochemistry , vol.42 , pp. 14427-14433
    • Klenchin, D.1    Taylor Ringia, E.A.2    Gerlt, J.A.3    Rayment, I.4
  • 16
    • 0026002950 scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant
    • Landro, J. A., Kallarakal, A. T., Ransom, S. C., Gerlt, J. A., Kozarich, J. W., Neidhart, D. J., and Kenyon, G. L. (1991) Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant, Biochemistry 30, 9274-81.
    • (1991) Biochemistry , vol.30 , pp. 9274-9281
    • Landro, J.A.1    Kallarakal, A.T.2    Ransom, S.C.3    Gerlt, J.A.4    Kozarich, J.W.5    Neidhart, D.J.6    Kenyon, G.L.7
  • 17
    • 0014349686 scopus 로고
    • Purification and mechanism of action of proline racemase
    • Cardinale, G. J., and Abeles, R. H. (1968) Purification and mechanism of action of proline racemase, Biochemistry 7, 3970-3978.
    • (1968) Biochemistry , vol.7 , pp. 3970-3978
    • Cardinale, G.J.1    Abeles, R.H.2
  • 18
    • 0025941721 scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism
    • Powers, V. M., Koo, C. W., Kenyon, G. L., Gerlt, J. A., and Kozarich, J. W. (1991) Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism, Biochemistry 30, 9255-63.
    • (1991) Biochemistry , vol.30 , pp. 9255-9263
    • Powers, V.M.1    Koo, C.W.2    Kenyon, G.L.3    Gerlt, J.A.4    Kozarich, J.W.5
  • 19
    • 0001304246 scopus 로고
    • Mandelate Racemase: Structure-function studies of a pseudosymmetric enzyme
    • Kenyon, G. L., Gerlt, J. A., Petsko, G. A., and Kozarich, J. W. (1995) Mandelate Racemase: Structure-function studies of a pseudosymmetric enzyme, Acc. Chem. Res. 28, 178-86.
    • (1995) Acc. Chem. Res. , vol.28 , pp. 178-186
    • Kenyon, G.L.1    Gerlt, J.A.2    Petsko, G.A.3    Kozarich, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.