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Volumn 401, Issue , 2005, Pages 449-467

Gamma-glutamyl transpeptidase substrate specificity and catalytic mechanism

Author keywords

[No Author keywords available]

Indexed keywords

GAMMA GLUTAMYLTRANSFERASE; LEUKOTRIENE;

EID: 30144443591     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)01027-X     Document Type: Review
Times cited : (89)

References (43)
  • 1
    • 0022272471 scopus 로고
    • γ-Glutamyl transpeptidase: Kinetics and mechanism
    • Allison R.D. γ-Glutamyl transpeptidase: Kinetics and mechanism Methods Enzymol. 113 1985 419 437
    • (1985) Methods Enzymol. , vol.113 , pp. 419-437
    • Allison, R.D.1
  • 2
    • 0019887846 scopus 로고
    • Evidence that transpeptidation is a significant function of γ-glutamyl transpeptidase
    • Allison R.D., and Meister A. Evidence that transpeptidation is a significant function of γ-glutamyl transpeptidase J. Biol. Chem 256 1981 2988 2992
    • (1981) J. Biol. Chem , vol.256 , pp. 2988-2992
    • Allison, R.D.1    Meister, A.2
  • 3
    • 0020014194 scopus 로고
    • γ-Glutamyl transpeptidase, a leukotriene metabolizing enzyme
    • Bernström K., Örning L., and Hammarström S. γ-Glutamyl transpeptidase, a leukotriene metabolizing enzyme Methods Enzymol. 86 1982 38 45
    • (1982) Methods Enzymol. , vol.86 , pp. 38-45
    • Bernström, K.1    Örning, L.2    Hammarström, S.3
  • 4
    • 0036973492 scopus 로고    scopus 로고
    • Mapping of the active site of γ-glutamyl transpeptidase using activated esters and their amide derivatives
    • Castonguay R., Lherbet C., and Keillor J.W. Mapping of the active site of γ-glutamyl transpeptidase using activated esters and their amide derivatives Bioorg. Med. Chem. 10 2002 4185 4191
    • (2002) Bioorg. Med. Chem. , vol.10 , pp. 4185-4191
    • Castonguay, R.1    Lherbet, C.2    Keillor, J.W.3
  • 5
    • 0141483289 scopus 로고    scopus 로고
    • Kinetic studies of rat kidney γ-glutamyl transpeptidase deacylation reveal a general-base-catalyzed mechanism
    • Castonguay R., Lherbet C., and Keillor J.W. Kinetic studies of rat kidney γ-glutamyl transpeptidase deacylation reveal a general-base-catalyzed mechanism Biochemistry 42 2003 11504 11513
    • (2003) Biochemistry , vol.42 , pp. 11504-11513
    • Castonguay, R.1    Lherbet, C.2    Keillor, J.W.3
  • 6
    • 0022404996 scopus 로고
    • The effect of pH on the transpeptidation and hydrolytic reactions of rat kidney γ-glutamyltransferase
    • Cook N.D., and Peters T.J. The effect of pH on the transpeptidation and hydrolytic reactions of rat kidney γ-glutamyltransferase Biochim. Biophys. Acta 832 1985 205 212
    • (1985) Biochim. Biophys. Acta , vol.832 , pp. 205-212
    • Cook, N.D.1    Peters, T.J.2
  • 7
    • 0023183609 scopus 로고
    • The donor specificity and kinetics of the hydrolysis reaction of γ-glutamyltransferase
    • Cook N.D., Upperton K.P., Challis B.C., and Peters T.J. The donor specificity and kinetics of the hydrolysis reaction of γ- glutamyltransferase Biochim. Biophys. Acta 914 1987 240 245
    • (1987) Biochim. Biophys. Acta , vol.914 , pp. 240-245
    • Cook, N.D.1    Upperton, K.P.2    Challis, B.C.3    Peters, T.J.4
  • 8
    • 0032905740 scopus 로고    scopus 로고
    • Hydrogen peroxide produced during γ-glutamyl transpeptidase activity is involved in prevention of apoptosis and maintenance of proliferation in U937 cells
    • Del Bello B., Paolicchi A., Comporti M., Pompella A., and Maellaro E. Hydrogen peroxide produced during γ-glutamyl transpeptidase activity is involved in prevention of apoptosis and maintenance of proliferation in U937 cells FASEB J. 13 1999 69 79
    • (1999) FASEB J. , vol.13 , pp. 69-79
    • Del Bello, B.1    Paolicchi, A.2    Comporti, M.3    Pompella, A.4    Maellaro, E.5
  • 9
    • 0018981291 scopus 로고
    • Active-site amino acid residues in γ-glutamyltransferase and the nature of the γ-glutamyl-enzyme bond
    • Elce J.S. Active-site amino acid residues in γ-glutamyltransferase and the nature of the γ-glutamyl-enzyme bond Biochem. J. 185 1980 473 481
    • (1980) Biochem. J. , vol.185 , pp. 473-481
    • Elce, J.S.1
  • 11
    • 33947094308 scopus 로고
    • Mechanisms of general acid and base catalysis of the reactions of water and alcohols with formaldehyde
    • Funderburk L.H., Aldwin L., and Jencks W.P. Mechanisms of general acid and base catalysis of the reactions of water and alcohols with formaldehyde J. Am. Chem. Soc. 100 1978 5444 5459
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 5444-5459
    • Funderburk, L.H.1    Aldwin, L.2    Jencks, W.P.3
  • 12
    • 0026594392 scopus 로고
    • High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis
    • Godwin A.K., Meister A., O'Dwyer P.J., Huang C.S., Hamilton T.C., and Anderson M.E. High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis Proc. Natl. Acad. Sci. USA 89 1992 3070 3074
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3070-3074
    • Godwin, A.K.1    Meister, A.2    O'Dwyer, P.J.3    Huang, C.S.4    Hamilton, T.C.5    Anderson, M.E.6
  • 13
    • 0001045727 scopus 로고
    • A method for the colorimetric determination of gamma-glutamyl transpeptidase in human serum; Enzymatic activity in health and disease
    • Goldbarg J.A., Pineda E.P., Smith E.E., Friedman O.M., and Rutenburg A.M. A method for the colorimetric determination of gamma-glutamyl transpeptidase in human serum; enzymatic activity in health and disease Gastroenterology 44 1963 127 133
    • (1963) Gastroenterology , vol.44 , pp. 127-133
    • Goldbarg, J.A.1    Pineda, E.P.2    Smith, E.E.3    Friedman, O.M.4    Rutenburg, A.M.5
  • 14
    • 0028670561 scopus 로고
    • γ-Glutamyltranspeptidase-catalysed acyl-transfer to the added acceptor does not proceed via the ping-pong mechanism
    • Gololobov M.Y., and Bateman R.C. Jr. γ-Glutamyltranspeptidase- catalysed acyl-transfer to the added acceptor does not proceed via the ping-pong mechanism Biochem. J. 304 1994 869 876
    • (1994) Biochem. J. , vol.304 , pp. 869-876
    • Gololobov, M.Y.1    Bateman Jr., R.C.2
  • 15
    • 0029142817 scopus 로고
    • Apoptosis in human lymphoblastoid cells induced by acivicin, a specific γ-glutamyltransferase inhibitor
    • Graber R., and Losa G.A. Apoptosis in human lymphoblastoid cells induced by acivicin, a specific γ-glutamyltransferase inhibitor Int. J. Cancer 62 1995 443 448
    • (1995) Int. J. Cancer , vol.62 , pp. 443-448
    • Graber, R.1    Losa, G.A.2
  • 16
    • 0018168953 scopus 로고
    • Evidence that the γ-glutamyl cycle functions in vivo using intracellular glutathione: Effects of amino acids and selective inhibition of enzymes
    • Griffith O.W., Bridges R.J., and Meister A. Evidence that the γ-glutamyl cycle functions in vivo using intracellular glutathione: Effects of amino acids and selective inhibition of enzymes Proc. Natl. Acad. Sci. USA 75 1978 5405 5408
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5405-5408
    • Griffith, O.W.1    Bridges, R.J.2    Meister, A.3
  • 17
    • 0012924310 scopus 로고
    • Selective inhibition of gamma-glutamyl-cycle enzymes by substrate analogs
    • Griffith O.W., and Meister A. Selective inhibition of gamma-glutamyl-cycle enzymes by substrate analogs Proc. Natl. Acad. Sci. USA 74 1977 3330 3334
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3330-3334
    • Griffith, O.W.1    Meister, A.2
  • 18
    • 0021998639 scopus 로고
    • Gamma-glutamyl transpeptidase - Its role in hepatocarcinogenesis
    • Hanigan M.H., and Pitot H.C. Gamma-glutamyl transpeptidase - its role in hepatocarcinogenesis Carcinogenesis 6 1985 165 172
    • (1985) Carcinogenesis , vol.6 , pp. 165-172
    • Hanigan, M.H.1    Pitot, H.C.2
  • 19
    • 0025743162 scopus 로고
    • Identification of a human gamma-glutamyl cleaving enzyme related to, but distinct from gamma-glutamyl transpeptidase
    • Heisterkamp N., Rajpert-De Meyts E., Uribe L., Forman H.J., and Groffen J. Identification of a human gamma-glutamyl cleaving enzyme related to, but distinct from gamma-glutamyl transpeptidase Proc. Natl. Acad. Sci. USA 88 1991 6303 6307
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6303-6307
    • Heisterkamp, N.1    Rajpert-De Meyts, E.2    Uribe, L.3    Forman, H.J.4    Groffen, J.5
  • 20
    • 0032570485 scopus 로고    scopus 로고
    • Biocatalytic and chemical preparation of all diastereoisomers of methionine sulfoxide
    • Holland H.L., and Brown F.M. Biocatalytic and chemical preparation of all diastereoisomers of methionine sulfoxide Tetrahedron: Asymmetry 10 1998 535 538
    • (1998) Tetrahedron: Asymmetry , vol.10 , pp. 535-538
    • Holland, H.L.1    Brown, F.M.2
  • 21
    • 0033618639 scopus 로고    scopus 로고
    • Biocatalytic and chemical routes to all the stereoisomers of methionine and ethionine sulfoxide
    • Holland H.L., Andreana P.R., and Brown F.M. Biocatalytic and chemical routes to all the stereoisomers of methionine and ethionine sulfoxide Tetrahedron: Asymmetry 10 1999 2833 2843
    • (1999) Tetrahedron: Asymmetry , vol.10 , pp. 2833-2843
    • Holland, H.L.1    Andreana, P.R.2    Brown, F.M.3
  • 22
    • 0028977997 scopus 로고
    • Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit
    • Ikeda Y., Fujii J., Taniguchi N., and Meister A. Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit J. Biol. Chem. 270 1995 12471 12475
    • (1995) J. Biol. Chem. , vol.270 , pp. 12471-12475
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3    Meister, A.4
  • 23
    • 0029082677 scopus 로고
    • Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase
    • Ikeda Y., Fujii J., Anderson M.E., Taniguchi N., and Meister A. Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase J. Biol. Chem. 270 1995 22223 22228
    • (1995) J. Biol. Chem. , vol.270 , pp. 22223-22228
    • Ikeda, Y.1    Fujii, J.2    Anderson, M.E.3    Taniguchi, N.4    Meister, A.5
  • 24
    • 0015451295 scopus 로고
    • Structure-reactivity correlations and general acid-base catalysis in enzymic transacylation reactions
    • Jencks W.P. Structure-reactivity correlations and general acid-base catalysis in enzymic transacylation reactions Cold Sp. Har. Sym. Quant. Biol. 36 1971 1 11
    • (1971) Cold Sp. Har. Sym. Quant. Biol. , vol.36 , pp. 1-11
    • Jencks, W.P.1
  • 25
    • 0018862544 scopus 로고
    • Chemistry and biochemistry of γ-glutamyl derivatives from plants including mushrooms (basidiomycetes)
    • Kasai T., and Larsen P.O. Chemistry and biochemistry of γ-glutamyl derivatives from plants including mushrooms (basidiomycetes) Proc. Chem. Org. Nat. Prod. 39 1980 173 285
    • (1980) Proc. Chem. Org. Nat. Prod. , vol.39 , pp. 173-285
    • Kasai, T.1    Larsen, P.O.2
  • 26
    • 2942735409 scopus 로고    scopus 로고
    • Pre-steady state kinetic studies of rat kidney γ-glutamyl transpeptidase confirm its ping-pong mechanism
    • Keillor J.W., Ménard A., Castonguay R., Lherbet C., and Rivard C. Pre-steady state kinetic studies of rat kidney γ-glutamyl transpeptidase confirm its ping-pong mechanism J. Phys. Org. Chem. 17 2004 529 536
    • (2004) J. Phys. Org. Chem. , vol.17 , pp. 529-536
    • Keillor, J.W.1    Ménard, A.2    Castonguay, R.3    Lherbet, C.4    Rivard, C.5
  • 28
    • 0037463779 scopus 로고    scopus 로고
    • Synthesis of aza- and oxaglutamyl-p-nitroanilide derivatives and their kinetic studies with gamma-glutamyl-transpeptidase
    • Lherbet C., Morin M., Castonguay R., and Keillor J.W. Synthesis of aza- and oxaglutamyl-p-nitroanilide derivatives and their kinetic studies with gamma-glutamyl-transpeptidase Bioorg. Med. Chem. Lett. 13 2003 997 1000
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 997-1000
    • Lherbet, C.1    Morin, M.2    Castonguay, R.3    Keillor, J.W.4
  • 29
    • 1642443170 scopus 로고    scopus 로고
    • Probing the stereochemistry of the active site of gamma-glutamyl transpeptidase using sulphur derivatives of l-glutamic acid
    • Lherbet C., and Keillor J.W. Probing the stereochemistry of the active site of gamma-glutamyl transpeptidase using sulphur derivatives of l-glutamic acid Org. Biomol. Chem. 2 2004 238 245
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 238-245
    • Lherbet, C.1    Keillor, J.W.2
  • 30
    • 2942585593 scopus 로고    scopus 로고
    • Synthesis of S-alkyl l-homocysteine analogues of glutathione and their kinetics with l-γ-glutamyl transpeptidase
    • Lherbet C., Gravel C., and Keillor J.W. Synthesis of S-alkyl l-homocysteine analogues of glutathione and their kinetics with l-γ-glutamyl transpeptidase Bioorg. Med. Chem. Lett. 14 2004 3451 3455
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 3451-3455
    • Lherbet, C.1    Gravel, C.2    Keillor, J.W.3
  • 31
    • 0015915903 scopus 로고
    • On the enzymology of amino acid transport
    • Meister A. On the enzymology of amino acid transport Science 180 1973 33 39
    • (1973) Science , vol.180 , pp. 33-39
    • Meister, A.1
  • 32
    • 0035940466 scopus 로고    scopus 로고
    • Nonlinear free energy relationship in the general-acid-catalyzed acylation of rat kidney γ-glutamyl transpeptidase by a series of γ-glutamyl anilide substrate analogues
    • Ménard A., Castonguay R., Lherbet C., Rivard C., Roupioz Y., and Keillor J.W. Nonlinear free energy relationship in the general-acid-catalyzed acylation of rat kidney γ-glutamyl transpeptidase by a series of γ-glutamyl anilide substrate analogues Biochemistry 40 2001 12678 12685
    • (2001) Biochemistry , vol.40 , pp. 12678-12685
    • Ménard, A.1    Castonguay, R.2    Lherbet, C.3    Rivard, C.4    Roupioz, Y.5    Keillor, J.W.6
  • 33
    • 0009090078 scopus 로고
    • Leukotriene D: A slow reacting substance from rat basophilic leukemia cells
    • Örning L., Hammarström S., and Samuelsson B. Leukotriene D: A slow reacting substance from rat basophilic leukemia cells Proc. Natl. Acad. Sci. USA 77 1980 2014 2017
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2014-2017
    • Örning, L.1    Hammarström, S.2    Samuelsson, B.3
  • 34
    • 0015497445 scopus 로고
    • Subtilisin: A stereochemical mechanism involving transition-state stabilization
    • Robertus J.D., Kraut J., Alden R.A., and Birktoft J.J. Subtilisin: A stereochemical mechanism involving transition-state stabilization Biochemistry 11 1972 4293 4303
    • (1972) Biochemistry , vol.11 , pp. 4293-4303
    • Robertus, J.D.1    Kraut, J.2    Alden, R.A.3    Birktoft, J.J.4
  • 35
    • 0025064289 scopus 로고
    • Characterization of the S'-subsite specificity of bovine pancreatic α-chymotrypsin via acyl transfer to added nucleophiles
    • Schellenberger V., Schellenberger U., Mitin Y.V., and Jakubke H.-D. Characterization of the S'-subsite specificity of bovine pancreatic α-chymotrypsin via acyl transfer to added nucleophiles Eur. J. Biochem 187 1990 163 167
    • (1990) Eur. J. Biochem , vol.187 , pp. 163-167
    • Schellenberger, V.1    Schellenberger, U.2    Mitin, Y.V.3    Jakubke, H.-D.4
  • 38
    • 30144435845 scopus 로고
    • Interaction of gamma-glutamyl transpeptidase with glutathione involves specific arginine and lysine residues of the heavy subunit
    • Stole E., and Meister A. Interaction of gamma-glutamyl transpeptidase with glutathione involves specific arginine and lysine residues of the heavy subunit J. Biol. Chem. 252 1991 6042 6045
    • (1991) J. Biol. Chem. , vol.252 , pp. 6042-6045
    • Stole, E.1    Meister, A.2
  • 39
    • 0031627519 scopus 로고    scopus 로고
    • γ-Glutamyl transpeptidase: Catalytic mechanism and gene expression
    • Taniguchi N., and Ikeda Y. γ-Glutamyl transpeptidase: Catalytic mechanism and gene expression Adv. Enzymol. Relat. Areas Mol. Biol. 72 1998 239 278
    • (1998) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.72 , pp. 239-278
    • Taniguchi, N.1    Ikeda, Y.2
  • 40
    • 0007006086 scopus 로고
    • Stimulation of the hydrolysis activity and decrease of the transpeptidase activity of γ-glutamyl transpeptidase by maleate; Identity of a rat kidney maleate-stimulated glutaminase and γ-glutamyl transpeptidase
    • Tate S.S., and Meister A. Stimulation of the hydrolysis activity and decrease of the transpeptidase activity of γ-glutamyl transpeptidase by maleate; identity of a rat kidney maleate-stimulated glutaminase and γ-glutamyl transpeptidase Proc. Natl. Acad. Sci. USA 71 1974 3329 3333
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3329-3333
    • Tate, S.S.1    Meister, A.2
  • 41
    • 0022272470 scopus 로고
    • γ-Glutamyl transpeptidase from kidney
    • Tate S.S., and Meister A. γ-Glutamyl transpeptidase from kidney Methods Enzymol. 113 1985 400 419
    • (1985) Methods Enzymol. , vol.113 , pp. 400-419
    • Tate, S.S.1    Meister, A.2
  • 42
    • 0017143736 scopus 로고
    • Hydrolysis and transfer reactions catalyzed by γ-glutamyl transpeptidase; Evidence for separate substrate sites and for high affinity of l-cystine
    • Thompson G.A., and Meister A. Hydrolysis and transfer reactions catalyzed by γ-glutamyl transpeptidase; evidence for separate substrate sites and for high affinity of l-cystine Biochem. Biophys. Res. Comm. 71 1976 32 36
    • (1976) Biochem. Biophys. Res. Comm. , vol.71 , pp. 32-36
    • Thompson, G.A.1    Meister, A.2
  • 43
    • 0017666965 scopus 로고
    • Interrelationships between the binding sites for amino acids, dipeptides, and γ-glutamyl donors in γ-glutamyl transpeptidase
    • Thompson G.A., and Meister A. Interrelationships between the binding sites for amino acids, dipeptides, and γ-glutamyl donors in γ-glutamyl transpeptidase J. Biol. Chem. 252 1977 6792 6798
    • (1977) J. Biol. Chem. , vol.252 , pp. 6792-6798
    • Thompson, G.A.1    Meister, A.2


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