메뉴 건너뛰기




Volumn 44, Issue 33, 2005, Pages 11188-11200

Staphylococcus aureus sortase transpeptidase SrtA: Insight into the kinetic mechanism and evidence for a reverse protonation catalytic mechanism

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CELLS; HYDROLYSIS; IONIZATION; ISOTOPES; MASS SPECTROMETRY; PH EFFECTS; PHYSIOLOGY; PROTONS;

EID: 23944522769     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050141j     Document Type: Article
Times cited : (122)

References (65)
  • 1
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S. K., Liu, G., Ton-That, H., and Schneewind, O. (1999) Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall, Science 285, 760-3.
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 2
    • 0037013286 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Suiphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring
    • Perry, A. M., Ton-That, H., Mazmanian, S. K., and Schneewind, O. (2002) Anchoring of surface proteins to the cell wall of Suiphylococcus aureus. III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed surface protein anchoring, J. Biol. Chem. 277, 16241-8.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16241-16248
    • Perry, A.M.1    Ton-That, H.2    Mazmanian, S.K.3    Schneewind, O.4
  • 3
    • 0036210885 scopus 로고    scopus 로고
    • Further evidence that a cell wall precursor [C(55)-MurNAc-(peptide)- GlcNAc] serves as an acceptor in a sorting reaction
    • Ruzin, A., Severin, A., Ritacco, F., Tabei, K., Singh, G., Bradford, P. A., Siegel, M. M., Projan, S. J., and Shlaes, D. M. (2002) Further evidence that a cell wall precursor [C(55)-MurNAc-(peptide)-GlcNAc] serves as an acceptor in a sorting reaction, J. Bacteriol. 184, 2141-7.
    • (2002) J. Bacteriol. , vol.184 , pp. 2141-2147
    • Ruzin, A.1    Severin, A.2    Ritacco, F.3    Tabei, K.4    Singh, G.5    Bradford, P.A.6    Siegel, M.M.7    Projan, S.J.8    Shlaes, D.M.9
  • 4
    • 0035283403 scopus 로고    scopus 로고
    • An embarrassment of sortases: A richness of substrates?
    • Pallen, M. J., Lam, A. C., Antonio, M., and Dunbar, K. (2001) An embarrassment of sortases: A richness of substrates? Trends Microbiol. 9, 97-102.
    • (2001) Trends Microbiol. , vol.9 , pp. 97-102
    • Pallen, M.J.1    Lam, A.C.2    Antonio, M.3    Dunbar, K.4
  • 5
    • 2142808787 scopus 로고    scopus 로고
    • A comparative genome analysis identifies distinct sorting pathways in Gram-positive bacteria
    • Comfort, D., and Clubb, R. T. (2004) A comparative genome analysis identifies distinct sorting pathways in Gram-positive bacteria, Infect. Immun. 72, 2710-22.
    • (2004) Infect. Immun. , vol.72 , pp. 2710-2722
    • Comfort, D.1    Clubb, R.T.2
  • 6
    • 0037133213 scopus 로고    scopus 로고
    • An iron-regulated sortase anchors a class of surface protein during Staphylococcns aureus pathogenesis
    • Mazmanian, S. K., Ton-That, H., Su, K., and Schneewind, O. (2002) An iron-regulated sortase anchors a class of surface protein during Staphylococcns aureus pathogenesis, Proc. Natl. Acad. Sci. U.S.A. 99, 2293-8.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2293-2298
    • Mazmanian, S.K.1    Ton-That, H.2    Su, K.3    Schneewind, O.4
  • 7
    • 0034625174 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections
    • Mazmanian, S. K., Liu, G., Jensen, E. R., Lenoy, E., and Schneewind, O. (2000) Staphylococcus aureus sortase mutants defective in the display of surface proteins and in the pathogenesis of animal infections, Proc. Natl. Acad. Sci. U.S.A. 97, 5510-5.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5510-5515
    • Mazmanian, S.K.1    Liu, G.2    Jensen, E.R.3    Lenoy, E.4    Schneewind, O.5
  • 8
    • 0035169610 scopus 로고    scopus 로고
    • Inactivation of the srtA gene in Streptococcus gordonii inhibits cell wall anchoring of surface proteins and decreases in vitro and in vivo adhesion
    • Bolken, T. C., Franke, C. A., Jones, K. F., Zeller, G. O., Jones, C. H., Dutton, E. K., and Hruby, D. E. (2001) Inactivation of the srtA gene in Streptococcus gordonii inhibits cell wall anchoring of surface proteins and decreases in vitro and in vivo adhesion, Infect. Immun. 69, 75-80.
    • (2001) Infect. Immun. , vol.69 , pp. 75-80
    • Bolken, T.C.1    Franke, C.A.2    Jones, K.F.3    Zeller, G.O.4    Jones, C.H.5    Dutton, E.K.6    Hruby, D.E.7
  • 9
    • 0036178935 scopus 로고    scopus 로고
    • The sortase SrtA of Listeria monocytogenes is involved in processing of internalin and in virulence
    • Garandeau, C., Reglier-Poupet, H., Dubail, I., Beretti, J. L., Berche, P., and Charbit, A. (2002) The sortase SrtA of Listeria monocytogenes is involved in processing of internalin and in virulence, Infect. Immun. 70, 1382-90.
    • (2002) Infect. Immun. , vol.70 , pp. 1382-1390
    • Garandeau, C.1    Reglier-Poupet, H.2    Dubail, I.3    Beretti, J.L.4    Berche, P.5    Charbit, A.6
  • 10
    • 0036154791 scopus 로고    scopus 로고
    • Characterization of Streptococcus suis genes encoding proteins homologous to sortase of Gram-positive bacteria
    • Osaki, M., Takamatsu, D., Shimoji, Y., and Sekizaki, T. (2002) Characterization of Streptococcus suis genes encoding proteins homologous to sortase of Gram-positive bacteria, J. Bacteriol. 184, 971-82.
    • (2002) J. Bacteriol. , vol.184 , pp. 971-982
    • Osaki, M.1    Takamatsu, D.2    Shimoji, Y.3    Sekizaki, T.4
  • 11
    • 0037406692 scopus 로고    scopus 로고
    • Inactivation of the srtA gene affects localization of surface proteins and decreases adhesion of Streptococcus pneumoniae to human pharyngeal cells in vitro
    • Kharat, A. S., and Tomasz, A. (2003) Inactivation of the srtA gene affects localization of surface proteins and decreases adhesion of Streptococcus pneumoniae to human pharyngeal cells in vitro, Infect. Immun. 71, 2758-65.
    • (2003) Infect. Immun. , vol.71 , pp. 2758-2765
    • Kharat, A.S.1    Tomasz, A.2
  • 12
    • 0037305827 scopus 로고    scopus 로고
    • Roles of sortase in surface expression of the major protein adhesin P1, saliva-induced aggregation and adherence, and cariogenicity of Streptococcus mutans
    • Lee, S. F., and Boran, T. L. (2003) Roles of sortase in surface expression of the major protein adhesin P1, saliva-induced aggregation and adherence, and cariogenicity of Streptococcus mutans, Infect. Immun. 71, 676-81.
    • (2003) Infect. Immun. , vol.71 , pp. 676-681
    • Lee, S.F.1    Boran, T.L.2
  • 13
    • 0036207211 scopus 로고    scopus 로고
    • Differential recognition of surface proteins in Streptococcus pyogenes by two sortase gene homologs
    • Barnett, T. C., and Scott, J. R. (2002) Differential recognition of surface proteins in Streptococcus pyogenes by two sortase gene homologs, J. Bacteriol. 184, 2181-91.
    • (2002) J. Bacteriol. , vol.184 , pp. 2181-2191
    • Barnett, T.C.1    Scott, J.R.2
  • 14
    • 0037106334 scopus 로고    scopus 로고
    • Irreversible inhibition of the bacterial cysteine protease-transpeptidase sortase (SrtA) by substrate-derived affinity labels
    • Scott, C. J., McDowell, A., Martin, S. L., Lynas, J. F., Vandenbroeck, K., and Walker, B. (2002) Irreversible inhibition of the bacterial cysteine protease-transpeptidase sortase (SrtA) by substrate-derived affinity labels, Biochem. J. 366, 953-8.
    • (2002) Biochem. J. , vol.366 , pp. 953-958
    • Scott, C.J.1    McDowell, A.2    Martin, S.L.3    Lynas, J.F.4    Vandenbroeck, K.5    Walker, B.6
  • 15
    • 1642345800 scopus 로고    scopus 로고
    • Sortase from S. aureus does not contain a thiolate-imidazolium ion pair in its active site
    • Connolly, K. M., Smith, B. T., Pilpa, R., Ilangovan, U., Jung, M. E., and Clubb, R. T. (2003) Sortase from S. aureus does not contain a thiolate-imidazolium ion pair in its active site, J. Biol. Chem. 24, 24.
    • (2003) J. Biol. Chem. , vol.24 , pp. 24
    • Connolly, K.M.1    Smith, B.T.2    Pilpa, R.3    Ilangovan, U.4    Jung, M.E.5    Clubb, R.T.6
  • 16
    • 2942546536 scopus 로고    scopus 로고
    • Inhibition of the Staphylococcus aureus sortase transpeptidase SrtA by phosphinic peptidomimetics
    • Kruger, R. G., Barkallah, S., Frankel, B. A., and McCafferty, D. G. (2004) Inhibition of the Staphylococcus aureus sortase transpeptidase SrtA by phosphinic peptidomimetics, Bioorg. Med. Chem. 12, 3723-9.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 3723-3729
    • Kruger, R.G.1    Barkallah, S.2    Frankel, B.A.3    McCafferty, D.G.4
  • 17
    • 3342972835 scopus 로고    scopus 로고
    • Localization and mutagenesis of the sorting signal binding site on sortase a from Staphylococcus aureus
    • Liew, C. K., Smith, B. T., Pilpa, R., Suree, N., Ilangovan, U., Connolly, K. M., Jung, M. E., and Clubb, R. T. (2004) Localization and mutagenesis of the sorting signal binding site on sortase A from Staphylococcus aureus, FEBS Lett. 571, 221-6.
    • (2004) FEBS Lett. , vol.571 , pp. 221-226
    • Liew, C.K.1    Smith, B.T.2    Pilpa, R.3    Suree, N.4    Ilangovan, U.5    Connolly, K.M.6    Jung, M.E.7    Clubb, R.T.8
  • 18
    • 2942622529 scopus 로고    scopus 로고
    • Inhibition of sortase, a bacterial surface protein anchoring transpeptidase, by β-sitosterol-3-O-glucopyranoside from Fritillaria venicillata
    • Kim, S. H., Shin, D. S., Oh, M. N., Chung, S. C., Lee, J. S., Chang, I. M., and Oh, K. B. (2003) Inhibition of sortase, a bacterial surface protein anchoring transpeptidase, by β-sitosterol-3-O-glucopyranoside from Fritillaria venicillata. Biosci., Biotechnol., Biochem. 67, 2477-9.
    • (2003) Biosci., Biotechnol., Biochem. , vol.67 , pp. 2477-2479
    • Kim, S.H.1    Shin, D.S.2    Oh, M.N.3    Chung, S.C.4    Lee, J.S.5    Chang, I.M.6    Oh, K.B.7
  • 19
    • 2942555515 scopus 로고    scopus 로고
    • Inhibition of the bacterial surface protein anchoring transpeptidase sortase by isoquinoline alkaloids
    • Kim, S. H., Shin, D. S., Oh, M. N., Chung, S. C., Lee, J. S., and Oh, K. B. (2004) Inhibition of the bacterial surface protein anchoring transpeptidase sortase by isoquinoline alkaloids, Biosci., Biotechnol., Biochem. 68, 421-4.
    • (2004) Biosci., Biotechnol., Biochem. , vol.68 , pp. 421-424
    • Kim, S.H.1    Shin, D.S.2    Oh, M.N.3    Chung, S.C.4    Lee, J.S.5    Oh, K.B.6
  • 20
    • 0042201886 scopus 로고    scopus 로고
    • Inhibition of the bacterial surface protein anchoring transpeptidase sortase by medicinal plants
    • Kim, S. W., Chang, I. M., and Oh, K. B. (2002) Inhibition of the bacterial surface protein anchoring transpeptidase sortase by medicinal plants, Biosci., Biotechnol., Biochem. 66, 2751-4.
    • (2002) Biosci., Biotechnol., Biochem. , vol.66 , pp. 2751-2754
    • Kim, S.W.1    Chang, I.M.2    Oh, K.B.3
  • 21
    • 1642304933 scopus 로고    scopus 로고
    • Vinyl Sulfones: Inhibitors of SrtA, a transpeptidase required for cell wall protein anchoring and virulence in Staphylococcus aureus
    • Frankel, B. A., Bentley, M., Kruger, R. G., and McCafferty, D. G. (2004) Vinyl Sulfones: Inhibitors of SrtA, a transpeptidase required for cell wall protein anchoring and virulence in Staphylococcus aureus, J. Am. Chem. Soc. 126, 3404-5.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3404-3405
    • Frankel, B.A.1    Bentley, M.2    Kruger, R.G.3    McCafferty, D.G.4
  • 22
    • 0033588339 scopus 로고    scopus 로고
    • Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction
    • Ton-That, H., and Schneewind, O. (1999) Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the cell wall sorting reaction, J. Biol. Chem. 274, 24316-20.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24316-24320
    • Ton-That, H.1    Schneewind, O.2
  • 23
    • 2342598417 scopus 로고    scopus 로고
    • Discovery of diarylacrylonitriles as a novel series of small molecule sortase A inhibitors
    • Oh, K. B., Kim, S. H., Lee, J., Cho, W. J., Lee, T., and Kim, S. (2004) Discovery of diarylacrylonitriles as a novel series of small molecule sortase A inhibitors, J. Med. Chem. 47, 2418-21.
    • (2004) J. Med. Chem. , vol.47 , pp. 2418-2421
    • Oh, K.B.1    Kim, S.H.2    Lee, J.3    Cho, W.J.4    Lee, T.5    Kim, S.6
  • 24
    • 0035932982 scopus 로고    scopus 로고
    • Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus
    • Ilangovan, U., Ton-That, H., Iwahara, J., Schneewind, O., and Clubb, R. T. (2001) Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus, Proc. Natl. Acad. Sci. U.S.A. 98, 6056-61.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6056-6061
    • Ilangovan, U.1    Ton-That, H.2    Iwahara, J.3    Schneewind, O.4    Clubb, R.T.5
  • 25
    • 0036510385 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Cysteine 184 and histidine 120 of sortase form a thiolate-imidazolium ion pair for catalysis
    • Ton-That, H., Mazmanian, S. K., Alksne, L., and Schneewind, O. (2002) Anchoring of surface proteins to the cell wall of Staphylococcus aureus. Cysteine 184 and histidine 120 of sortase form a thiolate-imidazolium ion pair for catalysis, J. Biol. Chem. 277, 7447-52.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7447-7452
    • Ton-That, H.1    Mazmanian, S.K.2    Alksne, L.3    Schneewind, O.4
  • 26
    • 3543073805 scopus 로고    scopus 로고
    • Crystal structures of Staphylococcus aureus sortase A and its substrate complex
    • Zong, Y., Bice, T. W., Ton-That, H., Schneewind, O., and Narayana, S. V. (2004) Crystal structures of Staphylococcus aureus sortase A and its substrate complex, J. Biol. Chem. 279, 31383-9.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31383-31389
    • Zong, Y.1    Bice, T.W.2    Ton-That, H.3    Schneewind, O.4    Narayana, S.V.5
  • 27
    • 1642534360 scopus 로고    scopus 로고
    • The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall
    • Zong, Y., Mazmanian, S. K., Schneewind, O., and Narayana, S. V. (2004) The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall, Structure 12, 105-12.
    • (2004) Structure , vol.12 , pp. 105-112
    • Zong, Y.1    Mazmanian, S.K.2    Schneewind, O.3    Narayana, S.V.4
  • 28
    • 3142649047 scopus 로고    scopus 로고
    • Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site
    • Zhang, R., Wu, R., Joachimiak, G., Mazmanian, S. K., Missiakas, D. M., Gornicki, P., Schneewind, O., and Joachimiak, A. (2004) Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site, Structure 12, 1147-56.
    • (2004) Structure , vol.12 , pp. 1147-1156
    • Zhang, R.1    Wu, R.2    Joachimiak, G.3    Mazmanian, S.K.4    Missiakas, D.M.5    Gornicki, P.6    Schneewind, O.7    Joachimiak, A.8
  • 30
    • 0842346118 scopus 로고    scopus 로고
    • Development of a high-performance liquid chromatography assay and revision of kinetic parameters for the Staphylococcus aureus sortase transpeptidase SrtA
    • Kruger, R. G., Dostal, P., and McCafferty, D. G. (2004) Development of a high-performance liquid chromatography assay and revision of kinetic parameters for the Staphylococcus aureus sortase transpeptidase SrtA, Anal. Biochem. 326, 42-8.
    • (2004) Anal. Biochem. , vol.326 , pp. 42-48
    • Kruger, R.G.1    Dostal, P.2    McCafferty, D.G.3
  • 31
    • 1042288291 scopus 로고    scopus 로고
    • Analysis of the substrate specificity of the Staphylococcus aureus sortase transpeptidase SrtA
    • Kruger, R. G., Otvos, B., Frankel, B. A., Bentley, M., Dostal, P., and McCafferty, D. G. (2004) Analysis of the substrate specificity of the Staphylococcus aureus sortase transpeptidase SrtA, Biochemistry 43, 1541-51.
    • (2004) Biochemistry , vol.43 , pp. 1541-1551
    • Kruger, R.G.1    Otvos, B.2    Frankel, B.A.3    Bentley, M.4    Dostal, P.5    McCafferty, D.G.6
  • 34
    • 0017303557 scopus 로고
    • Kinetic studies of sheep kidney γ-glutamyl transpeptidase
    • Karkowsky, A. M., Bergamini, M. V., and Orlowski, M. (1976) Kinetic studies of sheep kidney γ-glutamyl transpeptidase, J. Biol. Chem. 251, 4736-43.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4736-4743
    • Karkowsky, A.M.1    Bergamini, M.V.2    Orlowski, M.3
  • 36
    • 33845379336 scopus 로고
    • Tailored excitation for Fourier-transform ion cyclotron mass spectrometry
    • Marshall, A. G., Wang, T. C. L., and Ricca, T. L. (1985) Tailored excitation for Fourier-transform ion cyclotron mass spectrometry, J. Am. Chem. Soc. 107, 7893-7.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7893-7897
    • Marshall, A.G.1    Wang, T.C.L.2    Ricca, T.L.3
  • 37
    • 0027997748 scopus 로고
    • Infrared muhiphoton dissociation of large multiply charged ions for biomolecule sequencing
    • Little, D. P., Speir, J. P., Senko, M. W., O'Connor, P. B., and McLafferty, F. W. (1994) Infrared muhiphoton dissociation of large multiply charged ions for biomolecule sequencing, Anal. Chem. 66, 2809-15.
    • (1994) Anal. Chem. , vol.66 , pp. 2809-2815
    • Little, D.P.1    Speir, J.P.2    Senko, M.W.3    O'Connor, P.B.4    McLafferty, F.W.5
  • 38
    • 0034582319 scopus 로고    scopus 로고
    • Automated reduction and interpretation of high-resolution electrospray mass spectra of large molecules
    • Horn, D. M., Zubarev, R. A., and McLafferty, F. W. (2000) Automated reduction and interpretation of high-resolution electrospray mass spectra of large molecules, J. Am. Soc. Mass Spectrom. 11, 320-32.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 320-332
    • Horn, D.M.1    Zubarev, R.A.2    McLafferty, F.W.3
  • 39
    • 0041474713 scopus 로고    scopus 로고
    • Web and database software for identification of intact proteins using "top down" mass spectrometry
    • Taylor, G. K., Kim, Y. B., Forbes, A. J., Meng, F., McCarthy, R., and Kelleher, N. L. (2003) Web and database software for identification of intact proteins using "top down" mass spectrometry, Anal. Chem. 75, 4081-6.
    • (2003) Anal. Chem. , vol.75 , pp. 4081-4086
    • Taylor, G.K.1    Kim, Y.B.2    Forbes, A.J.3    Meng, F.4    McCarthy, R.5    Kelleher, N.L.6
  • 40
    • 73649151319 scopus 로고
    • Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
    • Kitz, R., and Wilson, I. B. (1962) Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase, J. Biol. Chem. 237, 3245-9.
    • (1962) J. Biol. Chem. , vol.237 , pp. 3245-3249
    • Kitz, R.1    Wilson, I.B.2
  • 41
    • 0033607265 scopus 로고    scopus 로고
    • Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif
    • Ton-That, H., Liu, G., Mazmanian, S. K., Faull, K. F., and Schneewind, O. (1999) Purification and characterization of sortase, the transpeptidase that cleaves surface proteins of Staphylococcus aureus at the LPXTG motif, Proc. Natl. Acad. Sci. U.S.A. 96, 12424-9.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 12424-12429
    • Ton-That, H.1    Liu, G.2    Mazmanian, S.K.3    Faull, K.F.4    Schneewind, O.5
  • 42
    • 0015500905 scopus 로고
    • Kinetic studies with transglutaminases. The human blood enzymes activated coagulation factor 13 and the guinea pig hair follicle enzyme
    • Chung, S. I., and Folk, J. E. (1972) Kinetic studies with transglutaminases. The human blood enzymes activated coagulation factor 13 and the guinea pig hair follicle enzyme, J. Biol. Chem. 247, 2798-807.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2798-2807
    • Chung, S.I.1    Folk, J.E.2
  • 43
    • 0000754119 scopus 로고
    • Liver microsomal glucose 6-phosphatase, inorganic pyrophosphatase, and pyrophosphate-glucose phosphotransferase. II. Kinetic studies
    • Arion, W. J., and Nordlie, R. C. (1964) Liver microsomal glucose 6-phosphatase, inorganic pyrophosphatase, and pyrophosphate-glucose phosphotransferase. II. Kinetic studies, J. Biol. Chem. 239, 2752-7.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2752-2757
    • Arion, W.J.1    Nordlie, R.C.2
  • 45
    • 0029896448 scopus 로고    scopus 로고
    • Arazoformyl dipeptide substrates for thermolysin. Confirmation of a reverse protonation catalytic mechanism
    • Mock, W. L., and Stanford, D. J. (1996) Arazoformyl dipeptide substrates for thermolysin. Confirmation of a reverse protonation catalytic mechanism, Biochemistry 35, 7369-77.
    • (1996) Biochemistry , vol.35 , pp. 7369-7377
    • Mock, W.L.1    Stanford, D.J.2
  • 47
    • 0001192303 scopus 로고
    • Kinetics of papain-catalyzed hydrolysis of α-N-benzoyl-L-arginine ethyl ester and α-N-benzoyl-L-argininamide
    • Whitaker, J. R., and Bender, M. L. (1965) Kinetics of papain-catalyzed hydrolysis of α-N-benzoyl-L-arginine ethyl ester and α-N-benzoyl-L- argininamide, J. Am. Chem. Soc. 87, 2728-37.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2728-2737
    • Whitaker, J.R.1    Bender, M.L.2
  • 48
    • 0035807060 scopus 로고    scopus 로고
    • Thiolate-imidazolium ion pair is not an obligatory catalytic entity of cysteine peptidases: The active site of picornain 3C
    • Sarkany, Z., Szeltner, Z., and Polgar, L. (2001) Thiolate-imidazolium ion pair is not an obligatory catalytic entity of cysteine peptidases: The active site of picornain 3C, Biochemistry 40, 10601-6.
    • (2001) Biochemistry , vol.40 , pp. 10601-10606
    • Sarkany, Z.1    Szeltner, Z.2    Polgar, L.3
  • 49
    • 0002018792 scopus 로고
    • Solvent isotope effects on enzymic reactions
    • (Cleland, W. W., OLeary, M. H., and Northrop, D. B., Eds.), University Park Press, Baltimore
    • Schowen, R. L. (1977) Solvent isotope effects on enzymic reactions, in Isotope effects on enzyme-catalyzed reactions (Cleland, W. W., OLeary, M. H., and Northrop, D. B., Eds.) pp 64-99, University Park Press, Baltimore.
    • (1977) Isotope Effects on Enzyme-catalyzed Reactions , pp. 64-99
    • Schowen, R.L.1
  • 51
    • 0342409311 scopus 로고    scopus 로고
    • Characterization of the active site thiol group of rhinovirus 2A proteinase
    • Sarkany, Z., Skern, T., and Polgar, L. (2000) Characterization of the active site thiol group of rhinovirus 2A proteinase, FEBS Lett. 481, 289-92.
    • (2000) FEBS Lett. , vol.481 , pp. 289-292
    • Sarkany, Z.1    Skern, T.2    Polgar, L.3
  • 52
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A. C., and Menard, R. (1994) Catalytic mechanism in papain family of cysteine peptidases, Methods Enzymol. 244, 486-500.
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Menard, R.2
  • 53
    • 1642452670 scopus 로고    scopus 로고
    • A new catalytic dyad regulates anchoring of molecules to the Gram-positive cell wall by sortases
    • Dessen, A. (2004) A new catalytic dyad regulates anchoring of molecules to the Gram-positive cell wall by sortases, Structure 12, 6-7.
    • (2004) Structure , vol.12 , pp. 6-7
    • Dessen, A.1
  • 54
    • 0036882394 scopus 로고    scopus 로고
    • Serine protease mechanism and specificity
    • Hedstrom, L. (2002) Serine protease mechanism and specificity, Chem. Rev. 102, 4501-24.
    • (2002) Chem. Rev. , vol.102 , pp. 4501-4524
    • Hedstrom, L.1
  • 55
    • 3042513718 scopus 로고    scopus 로고
    • Probing the mechanism of hamster arylamine N-acetyltransferase 2 acetylation by active site modification, site-directed mutagenesis, and pre-steady state and steady-state kinetic studies
    • Wang, H., Vath, G. M., Gleason, K. J., Hanna, P. E., and Wagner, C. R. (2004) Probing the mechanism of hamster arylamine N-acetyltransferase 2 acetylation by active site modification, site-directed mutagenesis, and pre-steady state and steady-state kinetic studies, Biochemistry 43, 8234-46.
    • (2004) Biochemistry , vol.43 , pp. 8234-8246
    • Wang, H.1    Vath, G.M.2    Gleason, K.J.3    Hanna, P.E.4    Wagner, C.R.5
  • 56
    • 0347895099 scopus 로고    scopus 로고
    • Conserved residues in the putative catalytic triad of human bile acid coenzyme A:amino acid N-acyltransferase
    • Sfakianos, M. K., Wilson, L., Sakalian, M., Falany, C. N., and Barnes, S. (2002) Conserved residues in the putative catalytic triad of human bile acid coenzyme A:amino acid N-acyltransferase, J. Biol. Chem. 277, 47270-5.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47270-47275
    • Sfakianos, M.K.1    Wilson, L.2    Sakalian, M.3    Falany, C.N.4    Barnes, S.5
  • 57
    • 0037457917 scopus 로고    scopus 로고
    • The unusual catalytic triad of poliovirus protease 3C
    • Sarkany, Z., and Polgar, L. (2003) The unusual catalytic triad of poliovirus protease 3C, Biochemistry 42, 516-22.
    • (2003) Biochemistry , vol.42 , pp. 516-522
    • Sarkany, Z.1    Polgar, L.2
  • 58
    • 4444348183 scopus 로고    scopus 로고
    • Anchoring of surface proteins to the cell wall of Staphylococcus aureus. A conserved arginine residue is required for efficient catalysis of sortase A
    • Marraffini, L. A., Ton-That, H., Zong, Y., Narayana, S. V., and Schneewind, O. (2004) Anchoring of surface proteins to the cell wall of Staphylococcus aureus. A conserved arginine residue is required for efficient catalysis of sortase A, J. Biol. Chem. 279, 37763-70.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37763-37770
    • Marraffini, L.A.1    Ton-That, H.2    Zong, Y.3    Narayana, S.V.4    Schneewind, O.5
  • 59
    • 0037489365 scopus 로고    scopus 로고
    • Reverse protonation is the key to general acid-base catalysis in enolase
    • Sims, P. A., Larsen, T. M., Poyner, R. R., Cleland, W. W., and Reed, G. H. (2003) Reverse protonation is the key to general acid-base catalysis in enolase, Biochemistry 42, 8298-306.
    • (2003) Biochemistry , vol.42 , pp. 8298-8306
    • Sims, P.A.1    Larsen, T.M.2    Poyner, R.R.3    Cleland, W.W.4    Reed, G.H.5
  • 60
    • 0017339091 scopus 로고
    • Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies
    • Cleland, W. W. (1977) Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies, Adv. Enzymol. Relat. Areas Mol. Biol. 45, 273-387.
    • (1977) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.45 , pp. 273-387
    • Cleland, W.W.1
  • 61
    • 0037031264 scopus 로고    scopus 로고
    • A case for reverse protonation: Identification of Glu 160 as an acid/base catalyst in Thermoanaerobacterium saccharolyticum β-xylosidase and detailed kinetic analysis of a site-directed mutant
    • Vocadlo, D. J., Wicki, J., Rupitz, K., and Withers, S. G. (2002) A case for reverse protonation: Identification of Glu 160 as an acid/base catalyst in Thermoanaerobacterium saccharolyticum β-xylosidase and detailed kinetic analysis of a site-directed mutant, Biochemistry 41, 9736-46.
    • (2002) Biochemistry , vol.41 , pp. 9736-9746
    • Vocadlo, D.J.1    Wicki, J.2    Rupitz, K.3    Withers, S.G.4
  • 62
    • 0021856089 scopus 로고
    • The pH dependence of the reductive carboxylation of pyruvate by malic enzyme
    • Nuiry, I. I., and Cook, P. F. (1985) The pH dependence of the reductive carboxylation of pyruvate by malic enzyme, Biochim. Biophys. Acta 829, 295-8.
    • (1985) Biochim. Biophys. Acta , vol.829 , pp. 295-298
    • Nuiry, I.I.1    Cook, P.F.2
  • 63
    • 0030589731 scopus 로고    scopus 로고
    • Kinetic and chemical mechanisms of the sheep liver 6-phosphogluconate dehydrogenase
    • Price, N. E., and Cook, P. F. (1996) Kinetic and chemical mechanisms of the sheep liver 6-phosphogluconate dehydrogenase, Arch. Biochem. Biophys. 336, 215-23.
    • (1996) Arch. Biochem. Biophys. , vol.336 , pp. 215-223
    • Price, N.E.1    Cook, P.F.2
  • 64
    • 0015923982 scopus 로고
    • On the mode of activation of the catalytically essential sulfhydryl group of papain
    • Polgar, L. (1973) On the mode of activation of the catalytically essential sulfhydryl group of papain, Eur. J. Biochem. 33, 104-9.
    • (1973) Eur. J. Biochem. , vol.33 , pp. 104-109
    • Polgar, L.1
  • 65
    • 0016115206 scopus 로고
    • Mercaptide-imidazolium ion-pair: The reactive nucleophile in papain catalysis
    • Polgar, L. (1974) Mercaptide-imidazolium ion-pair: The reactive nucleophile in papain catalysis, FEBS Lett. 47, 15-8.
    • (1974) FEBS Lett. , vol.47 , pp. 15-18
    • Polgar, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.