메뉴 건너뛰기




Volumn 47, Issue 37, 2008, Pages 9836-9846

Insight into the coupling mechanism of the vitamin K-dependent carboxylase: Mutation of histidine 160 disrupts glutamic acid carbanion formation and efficient coupling of vitamin K epoxidation to glutamic acid carboxylation

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; FOOD ADDITIVES; MECHANISMS; STOICHIOMETRY; TRITIUM;

EID: 51849094451     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800296r     Document Type: Article
Times cited : (16)

References (47)
  • 1
    • 23944489821 scopus 로고    scopus 로고
    • The vitamin K-dependent carboxylase
    • Berkner, K. L. (2005) The vitamin K-dependent carboxylase. Annu. Rev. Nutr. 25, 127-149.
    • (2005) Annu. Rev. Nutr , vol.25 , pp. 127-149
    • Berkner, K.L.1
  • 2
    • 0033559305 scopus 로고    scopus 로고
    • Vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid
    • Furie, B., Bouchard, B. A., and Furie, B. C. (1999) Vitamin K-dependent biosynthesis of gamma-carboxyglutamic acid. Blood 93, 1798-1808.
    • (1999) Blood , vol.93 , pp. 1798-1808
    • Furie, B.1    Bouchard, B.A.2    Furie, B.C.3
  • 3
    • 0035964295 scopus 로고    scopus 로고
    • Tethered processivity of the vitamin K-dependent carboxylase: Factor IX is efficiently modified in a mechanism which distinguishes Gla's from Glu's and which accounts for comprehensive carboxylation in vivo
    • Stenina, O., Pudota, B. N., McNally, B. A., Hommema, E. L., and Berkner, K. L. (2001) Tethered processivity of the vitamin K-dependent carboxylase: factor IX is efficiently modified in a mechanism which distinguishes Gla's from Glu's and which accounts for comprehensive carboxylation in vivo. Biochemistry 40, 10301-10309.
    • (2001) Biochemistry , vol.40 , pp. 10301-10309
    • Stenina, O.1    Pudota, B.N.2    McNally, B.A.3    Hommema, E.L.4    Berkner, K.L.5
  • 4
    • 0029586502 scopus 로고
    • Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate
    • Morris, D. P., Stevens, R. D., Wright, D. J., and Stafford, D. W. (1995) Processive post-translational modification. Vitamin K-dependent carboxylation of a peptide substrate. J. Biol. Chem. 270, 30491-30498.
    • (1995) J. Biol. Chem , vol.270 , pp. 30491-30498
    • Morris, D.P.1    Stevens, R.D.2    Wright, D.J.3    Stafford, D.W.4
  • 5
    • 0023656864 scopus 로고
    • Vitamin K-dependent carboxylase. Control of enzyme activity by the "propeptide" region of factor X
    • Knobloch, J. E., and Suttie, J. W. (1987) Vitamin K-dependent carboxylase. Control of enzyme activity by the "propeptide" region of factor X. J. Biol. Chem. 262, 15334-15337.
    • (1987) J. Biol. Chem , vol.262 , pp. 15334-15337
    • Knobloch, J.E.1    Suttie, J.W.2
  • 6
    • 0026463896 scopus 로고
    • Congenital deficiency of all vitamin K-dependent blood coagulation factors due to a defective vitamin K-dependent carboxylase in Devon Rex cats
    • Soute, B. A., Ulrich, M. M., Watson, A. D., Maddison, J. E., Ebberink, R. H., and Vermeer, C. (1992) Congenital deficiency of all vitamin K-dependent blood coagulation factors due to a defective vitamin K-dependent carboxylase in Devon Rex cats. Thromb. Haemostasis 68, 521-525.
    • (1992) Thromb. Haemostasis , vol.68 , pp. 521-525
    • Soute, B.A.1    Ulrich, M.M.2    Watson, A.D.3    Maddison, J.E.4    Ebberink, R.H.5    Vermeer, C.6
  • 7
    • 0032535284 scopus 로고    scopus 로고
    • A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors
    • Brenner, B., Sanchez-Vega, B., Wu, S. M., Lanir, N., Stafford, D. W., and Solera, J. (1998) A missense mutation in gamma-glutamyl carboxylase gene causes combined deficiency of all vitamin K-dependent blood coagulation factors. Blood 92, 4554-4559.
    • (1998) Blood , vol.92 , pp. 4554-4559
    • Brenner, B.1    Sanchez-Vega, B.2    Wu, S.M.3    Lanir, N.4    Stafford, D.W.5    Solera, J.6
  • 8
    • 33748693300 scopus 로고    scopus 로고
    • Compound heterozygosity of novel missense mutations in the γ-carboxylase gene causes hereditary combined vitamin K-dependent coagulation factor deficiency
    • Darghouth, D., Hallgren, K. W., Shtofman, R. L., Mrad, A., Gharbi, Y., Maherzi, A., Kastally, R., LeRicousse, S., Berkner, K. L., and Rosa, J.-P. (2006) Compound heterozygosity of novel missense mutations in the γ-carboxylase gene causes hereditary combined vitamin K-dependent coagulation factor deficiency. Blood 108, 1925-1931.
    • (2006) Blood , vol.108 , pp. 1925-1931
    • Darghouth, D.1    Hallgren, K.W.2    Shtofman, R.L.3    Mrad, A.4    Gharbi, Y.5    Maherzi, A.6    Kastally, R.7    LeRicousse, S.8    Berkner, K.L.9    Rosa, J.-P.10
  • 9
    • 4143112300 scopus 로고    scopus 로고
    • Compound heterozygous mutations in the gamma-glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors
    • Rost, S., Fregin, A., Koch, D., Compes, M., Muller, C. R., and Oldenburg, J. (2004) Compound heterozygous mutations in the gamma-glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors. Br. J. Haematol. 126, 546-549.
    • (2004) Br. J. Haematol , vol.126 , pp. 546-549
    • Rost, S.1    Fregin, A.2    Koch, D.3    Compes, M.4    Muller, C.R.5    Oldenburg, J.6
  • 10
    • 0034669988 scopus 로고    scopus 로고
    • Novel mutation in the gamma-glutamyl carboxylase gene resulting in congenital combined deficiency of all vitamin K-dependent blood coagulation factors
    • Spronk, H. M., Farah, R. A., Buchanan, G. R., Vermeer, C., and Soute, B. A. (2000) Novel mutation in the gamma-glutamyl carboxylase gene resulting in congenital combined deficiency of all vitamin K-dependent blood coagulation factors. Blood 96, 3650-3652.
    • (2000) Blood , vol.96 , pp. 3650-3652
    • Spronk, H.M.1    Farah, R.A.2    Buchanan, G.R.3    Vermeer, C.4    Soute, B.A.5
  • 12
    • 0038272020 scopus 로고    scopus 로고
    • The evolution of vertebrate blood coagulation as viewed from a comparison of puffer fish and sea squirt genomes
    • Jiang, Y., and Doolittle, R. F. (2003) The evolution of vertebrate blood coagulation as viewed from a comparison of puffer fish and sea squirt genomes. Proc. Natl. Acad. Sci. U.S.A. 100, 7527-7532.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 7527-7532
    • Jiang, Y.1    Doolittle, R.F.2
  • 13
    • 0037022383 scopus 로고    scopus 로고
    • gamma-Glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates
    • Bandyopadhyay, P. K., Garrett, J. E., Shetty, R. P., Keate, T., Walker, C. S., and Olivera, B. M. (2002) gamma-Glutamyl carboxylation: An extracellular posttranslational modification that antedates the divergence of molluscs, arthropods, and chordates. Proc. Natl. Acad. Sci. U.S.A. 99, 1264-1269.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 1264-1269
    • Bandyopadhyay, P.K.1    Garrett, J.E.2    Shetty, R.P.3    Keate, T.4    Walker, C.S.5    Olivera, B.M.6
  • 14
    • 0036452863 scopus 로고    scopus 로고
    • Expression and characterization of recombinant vitamin K-dependent gamma-glutamyl carboxylase from an invertebrate, Conus textile
    • Czerwiec, E., Begley, G. S., Bronstein, M., Stenflo, J., Taylor, K., Furie, B. C., and Furie, B. (2002) Expression and characterization of recombinant vitamin K-dependent gamma-glutamyl carboxylase from an invertebrate, Conus textile. Eur. J. Biochem. 269, 6162-6172.
    • (2002) Eur. J. Biochem , vol.269 , pp. 6162-6172
    • Czerwiec, E.1    Begley, G.S.2    Bronstein, M.3    Stenflo, J.4    Taylor, K.5    Furie, B.C.6    Furie, B.7
  • 15
    • 33750462753 scopus 로고    scopus 로고
    • Vitamin K-dependent proteins in Ciona intestinalis, a basal chordate lacking a blood coagulation cascade
    • Kulman, J. D., Harris, J. E., Nakazawa, N., Ogasawara, M., Satake, M., and Davie, E. W. (2006) Vitamin K-dependent proteins in Ciona intestinalis, a basal chordate lacking a blood coagulation cascade. Proc. Natl. Acad. Sci. U.S.A. 103, 15794-15799.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 15794-15799
    • Kulman, J.D.1    Harris, J.E.2    Nakazawa, N.3    Ogasawara, M.4    Satake, M.5    Davie, E.W.6
  • 16
    • 0034674448 scopus 로고    scopus 로고
    • Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase
    • Li, T., Yang, C. T., Jin, D., and Stafford, D. W. (2000) Identification of a Drosophila vitamin K-dependent gamma-glutamyl carboxylase. J. Biol. Chem. 275, 18291-18296.
    • (2000) J. Biol. Chem , vol.275 , pp. 18291-18296
    • Li, T.1    Yang, C.T.2    Jin, D.3    Stafford, D.W.4
  • 17
    • 0035896551 scopus 로고    scopus 로고
    • On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems: Evidence for a gamma-glutamyl carboxylase in Drosophila
    • Walker, C. S., Shetty, R. P., Clark, K. A., Kazuko, S. G., Letsou, A., Olivera, B. M., and Bandyopadhyay, P. K. (2001) On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems: Evidence for a gamma-glutamyl carboxylase in Drosophila. J. Biol. Chem. 276, 7769-7774.
    • (2001) J. Biol. Chem , vol.276 , pp. 7769-7774
    • Walker, C.S.1    Shetty, R.P.2    Clark, K.A.3    Kazuko, S.G.4    Letsou, A.5    Olivera, B.M.6    Bandyopadhyay, P.K.7
  • 18
    • 0141818959 scopus 로고    scopus 로고
    • Identification of a gene encoding a typical gamma-carboxyglutamic acid domain in the tunicate Halocynthia roretzi
    • Wang, C. P., Yagi, K., Lin, P. J., Jin, D. Y., Makabe, K. W., and Stafford, D. W. (2003) Identification of a gene encoding a typical gamma-carboxyglutamic acid domain in the tunicate Halocynthia roretzi. J. Thromb. Haemostasis 1, 118-123.
    • (2003) J. Thromb. Haemostasis , vol.1 , pp. 118-123
    • Wang, C.P.1    Yagi, K.2    Lin, P.J.3    Jin, D.Y.4    Makabe, K.W.5    Stafford, D.W.6
  • 20
    • 27144510338 scopus 로고    scopus 로고
    • The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylation
    • Rishavy, M. A., Hallgren, K. W., Yakubenko, A. V., Zuerner, R. L., Runge, K. W., and Berkner, K. L. (2005) The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylation. J. Biol. Chem. 280, 34870-34877.
    • (2005) J. Biol. Chem , vol.280 , pp. 34870-34877
    • Rishavy, M.A.1    Hallgren, K.W.2    Yakubenko, A.V.3    Zuerner, R.L.4    Runge, K.W.5    Berkner, K.L.6
  • 21
    • 0029130392 scopus 로고
    • Vitamin K and energy transduction: A base strength amplification mechanism
    • Dowd, P., Hershline, R., Ham, S. W., and Naganathan, S. (1995) Vitamin K and energy transduction: a base strength amplification mechanism. Science 269, 1684-1691.
    • (1995) Science , vol.269 , pp. 1684-1691
    • Dowd, P.1    Hershline, R.2    Ham, S.W.3    Naganathan, S.4
  • 23
    • 0021100306 scopus 로고
    • Fate of the activated gamma-carbon-hydrogen bond in the uncoupled vitamin K-dependent gamma-glutamyl carboxylation reaction
    • Anton, D. L., and Friedman, P. A. (1983) Fate of the activated gamma-carbon-hydrogen bond in the uncoupled vitamin K-dependent gamma-glutamyl carboxylation reaction. J. Biol. Chem. 258, 14084-14087.
    • (1983) J. Biol. Chem , vol.258 , pp. 14084-14087
    • Anton, D.L.1    Friedman, P.A.2
  • 24
    • 0025267730 scopus 로고
    • Vitamin K-dependent carboxylation. Mechanistic studies with 3-fiuoroglutamate-containing substrates
    • Vidal-Cros, A., Gaudry, M., and Marquet, A. (1990) Vitamin K-dependent carboxylation. Mechanistic studies with 3-fiuoroglutamate-containing substrates. Biochem. J. 266, 749-755.
    • (1990) Biochem. J , vol.266 , pp. 749-755
    • Vidal-Cros, A.1    Gaudry, M.2    Marquet, A.3
  • 25
    • 33846235560 scopus 로고    scopus 로고
    • Two-dimensional crystallization of human vitamin K-dependent gamma-glutamyl carboxylase
    • Schmidt-Krey, I., Haase, W., Mutucumarana, V., Stafford, D. W., and Kuhlbrandt, W. (2007) Two-dimensional crystallization of human vitamin K-dependent gamma-glutamyl carboxylase. J. Struct. Biol. 157, 437-442.
    • (2007) J. Struct. Biol , vol.157 , pp. 437-442
    • Schmidt-Krey, I.1    Haase, W.2    Mutucumarana, V.3    Stafford, D.W.4    Kuhlbrandt, W.5
  • 26
    • 33750709274 scopus 로고    scopus 로고
    • Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation
    • Rishavy, M. A., Hallgren, K. W., Yakubenko, A. V., Shtofman, R. L., Runge, K. W., and Berkner, K. L. (2006) Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation. Biochemistry 45, 13239-13248.
    • (2006) Biochemistry , vol.45 , pp. 13239-13248
    • Rishavy, M.A.1    Hallgren, K.W.2    Yakubenko, A.V.3    Shtofman, R.L.4    Runge, K.W.5    Berkner, K.L.6
  • 27
    • 0019868670 scopus 로고
    • Vitamin K-dependent carboxylase. Stoichiometry of carboxylation and vitamin K 2,3-epoxide formation
    • Larson, A. E., Friedman, P. A., and Suttie, J. W. (1981) Vitamin K-dependent carboxylase. Stoichiometry of carboxylation and vitamin K 2,3-epoxide formation. J. Biol. Chem. 256, 11032-11035.
    • (1981) J. Biol. Chem , vol.256 , pp. 11032-11035
    • Larson, A.E.1    Friedman, P.A.2    Suttie, J.W.3
  • 28
    • 0027460941 scopus 로고
    • Expression of recombinant vitamin K-dependent proteins in mammalian cells: Factors IX and VII
    • Berkner, K. L. (1993) Expression of recombinant vitamin K-dependent proteins in mammalian cells: Factors IX and VII. Methods Enzymol. 222, 450-477.
    • (1993) Methods Enzymol , vol.222 , pp. 450-477
    • Berkner, K.L.1
  • 29
    • 0027293993 scopus 로고
    • Expression of bovine vitamin K-dependent carboxylase activity in baculovirus-infected insect cells
    • Roth, D. A., Rehemtulla, A., Kaufman, R. J., Walsh, C. T., Furie, B., and Furie, B. C. (1993) Expression of bovine vitamin K-dependent carboxylase activity in baculovirus-infected insect cells. Proc. Natl. Acad. Sci. U.S.A. 90, 8372-8376.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 8372-8376
    • Roth, D.A.1    Rehemtulla, A.2    Kaufman, R.J.3    Walsh, C.T.4    Furie, B.5    Furie, B.C.6
  • 31
    • 0018805377 scopus 로고
    • Specific tritium labeling of gamma-carboxyglutamic acid in proteins
    • Hauschka, P. V. (1979) Specific tritium labeling of gamma-carboxyglutamic acid in proteins. Biochemistry 18, 4992-4999.
    • (1979) Biochemistry , vol.18 , pp. 4992-4999
    • Hauschka, P.V.1
  • 32
    • 0018778534 scopus 로고
    • Vitamin K-dependent gamma-carbon-hydrogen bond cleavage and nonmandatory concurrent carboxylation of peptide-bound glutamic acid residues
    • Friedman, P. A., Shia, M. A., Gallop, P. M., and Griep, A. E. (1979) Vitamin K-dependent gamma-carbon-hydrogen bond cleavage and nonmandatory concurrent carboxylation of peptide-bound glutamic acid residues. Proc. Natl. Acad. Sci. U.S.A. 76, 3126-3129.
    • (1979) Proc. Natl. Acad. Sci. U.S.A , vol.76 , pp. 3126-3129
    • Friedman, P.A.1    Shia, M.A.2    Gallop, P.M.3    Griep, A.E.4
  • 35
    • 0345306692 scopus 로고    scopus 로고
    • A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate
    • Mutucumarana, V. P., Acher, F., Straight, D. L., Jin, D. Y., and Stafford, D. W. (2003) A conserved region of human vitamin K-dependent carboxylase between residues 393 and 404 is important for its interaction with the glutamate substrate. J. Biol. Chem. 278, 46488-46493.
    • (2003) J. Biol. Chem , vol.278 , pp. 46488-46493
    • Mutucumarana, V.P.1    Acher, F.2    Straight, D.L.3    Jin, D.Y.4    Stafford, D.W.5
  • 36
    • 0034693128 scopus 로고    scopus 로고
    • Expression and characterization of the naturally occurring mutation L394R in human gamma-glutamyl carboxylase
    • Mutucumarana, V. P., Stafford, D. W., Stanley, T. B., Jin, D. Y., Solera, J., Brenner, B., Azerad, R., and Wu, S. M. (2000) Expression and characterization of the naturally occurring mutation L394R in human gamma-glutamyl carboxylase. J. Biol. Chem. 275, 32572-32577.
    • (2000) J. Biol. Chem , vol.275 , pp. 32572-32577
    • Mutucumarana, V.P.1    Stafford, D.W.2    Stanley, T.B.3    Jin, D.Y.4    Solera, J.5    Brenner, B.6    Azerad, R.7    Wu, S.M.8
  • 37
    • 0030741381 scopus 로고    scopus 로고
    • Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state
    • Sugiura, I., Furie, B., Walsh, C. T., and Furie, B. C. (1997) Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state. Proc. Natl. Acad. Sci. U.S.A. 94, 9069-9074.
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 9069-9074
    • Sugiura, I.1    Furie, B.2    Walsh, C.T.3    Furie, B.C.4
  • 38
    • 0019323903 scopus 로고
    • Vitamin K epoxidase: Dependence of epoxidase activity on substrates of the vitamin K-dependent carboxylation reaction
    • Suttie, J. W., Geweke, L. O., Martin, S. L., and Willingham, A. K. (1980) Vitamin K epoxidase: dependence of epoxidase activity on substrates of the vitamin K-dependent carboxylation reaction. FEBS Lett. 109, 267-270.
    • (1980) FEBS Lett , vol.109 , pp. 267-270
    • Suttie, J.W.1    Geweke, L.O.2    Martin, S.L.3    Willingham, A.K.4
  • 39
    • 0021773305 scopus 로고
    • Nature of products formed in the vitamin K-dependent carboxylation of synthetic peptides
    • Decottignies, L. M. e. P., Le, M. e. P., and Azerad, R. (1984) Nature of products formed in the vitamin K-dependent carboxylation of synthetic peptides. Biochem. Biophys. Res. Commun. 119, 836-840.
    • (1984) Biochem. Biophys. Res. Commun , vol.119 , pp. 836-840
    • Decottignies, L.M.E.P.1    Le, M.E.P.2    Azerad, R.3
  • 40
    • 0026325216 scopus 로고
    • Vitamin K dependent carboxylation: Determination of the stereochemical course using 4-fluoroglutamyl-containing substrate
    • Dubois, J., Dugave, C., Foures, C., Kaminsky, M., Tabet, J. C., Bory, S., Gaudry, M., and Marquet, A. (1991) Vitamin K dependent carboxylation: determination of the stereochemical course using 4-fluoroglutamyl-containing substrate. Biochemistry 30, 10506-10512.
    • (1991) Biochemistry , vol.30 , pp. 10506-10512
    • Dubois, J.1    Dugave, C.2    Foures, C.3    Kaminsky, M.4    Tabet, J.C.5    Bory, S.6    Gaudry, M.7    Marquet, A.8
  • 41
    • 0027420398 scopus 로고
    • Understanding the rates of certain enzyme-catalyzed reactions: Proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters
    • Gerlt, J. A., and Gassman, P. G. (1993) Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters. Biochemistry 32, 11943-11952.
    • (1993) Biochemistry , vol.32 , pp. 11943-11952
    • Gerlt, J.A.1    Gassman, P.G.2
  • 42
    • 0028030684 scopus 로고
    • Low-barrier hydrogen bonds and enzymic catalysis
    • Cleland, W. W., and Kreevoy, M. M. (1994) Low-barrier hydrogen bonds and enzymic catalysis. Science 264, 1887-1890.
    • (1994) Science , vol.264 , pp. 1887-1890
    • Cleland, W.W.1    Kreevoy, M.M.2
  • 43
    • 0028040716 scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases
    • Frey, P. A., Whitt, S. A., and Tobin, J. B. (1994) A low-barrier hydrogen bond in the catalytic triad of serine proteases. Science 264, 1927-1930.
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3
  • 44
    • 0023679884 scopus 로고
    • Vitamin K-dependent carboxylase from calf liver: Studies on the steady-state kinetic mechanism
    • Uotila, L. (1988) Vitamin K-dependent carboxylase from calf liver: studies on the steady-state kinetic mechanism. Arch. Biochem. Biophys. 264, 135-143.
    • (1988) Arch. Biochem. Biophys , vol.264 , pp. 135-143
    • Uotila, L.1
  • 45
    • 0037047297 scopus 로고    scopus 로고
    • The putative vitamin K-dependent gamma-glutamyl carboxylase internal propeptide appears to be the propeptide binding site
    • Lin, P. J., Jin, D. Y., Tie, J. K., Presnell, S. R., Straight, D. L., and Stafford, D. W. (2002) The putative vitamin K-dependent gamma-glutamyl carboxylase internal propeptide appears to be the propeptide binding site. J. Biol. Chem. 277, 28584-28591.
    • (2002) J. Biol. Chem , vol.277 , pp. 28584-28591
    • Lin, P.J.1    Jin, D.Y.2    Tie, J.K.3    Presnell, S.R.4    Straight, D.L.5    Stafford, D.W.6
  • 46
    • 0035797889 scopus 로고    scopus 로고
    • A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase
    • Presnell, S. R., Tripathy, A., Lentz, B. R., Jin, D. Y., and Stafford, D. W. (2001) A novel fluorescence assay to study propeptide interaction with gamma-glutamyl carboxylase. Biochemistry 40, 11723-11733.
    • (2001) Biochemistry , vol.40 , pp. 11723-11733
    • Presnell, S.R.1    Tripathy, A.2    Lentz, B.R.3    Jin, D.Y.4    Stafford, D.W.5
  • 47
    • 0346687596 scopus 로고    scopus 로고
    • HTTM, a horizontally transferred transmembrane domain
    • Schultz, J. (2004) HTTM, a horizontally transferred transmembrane domain. Trends Biochem. Sci. 29, 4-7.
    • (2004) Trends Biochem. Sci , vol.29 , pp. 4-7
    • Schultz, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.