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Volumn 48, Issue 12, 2009, Pages 2654-2660

Selectivity in the post-translational, transglutaminase-dependent acylation of lysine residues

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE PANCREATIC RIBONUCLEASE; BOVINE PANCREATIC TRYPSIN INHIBITORS; CHICKEN EGG WHITE LYSOZYMES; LYSINE RESIDUES; LYSINE SIDE CHAINS; POTENTIAL SURFACES; PRIMARY AMINO ACIDS; PROTEIN STRUCTURES; SIDE CHAINS; TRANSGLUTAMINASE; TRANSGLUTAMINASES; TRYPSIN INHIBITORS;

EID: 65249123429     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802323z     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: An enigmatic enzyme with diverse functions
    • Fesus, L., and Piacentini, M. (2002) Transglutaminase 2: An enigmatic enzyme with diverse functions. Trends Biochem. Sci. 27, 534-539.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 2
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • Griffin, M., Casadio, R., and Bergamini, C. M. (2002) Transglutaminases: Nature's biological glues. Biochem. J. 368, 377-396.
    • (2002) Biochem. J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 3
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand, L., and Graham, R. M. (2003) Transglutaminases: Crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4, 140-156.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 4
    • 0030611193 scopus 로고    scopus 로고
    • Hydrolysis of Γ: ε isopeptides by cytosolic transglutaminases and by coagulation factor XIIIa
    • Parameswaran, K. N., Cheng, X. F., Chen, E. C., Velasco, P. T., Wilson, J. H., and Lorand, L. (1997) Hydrolysis of Γ: ε isopeptides by cytosolic transglutaminases and by coagulation factor XIIIa. J. Biol. Chem. 272, 10311-10317.
    • (1997) J. Biol. Chem , vol.272 , pp. 10311-10317
    • Parameswaran, K.N.1    Cheng, X.F.2    Chen, E.C.3    Velasco, P.T.4    Wilson, J.H.5    Lorand, L.6
  • 5
    • 0016169863 scopus 로고
    • Kinetics of transamidating enzymes. Production of thiol in the reactions of thiol esters with fibrinoligase
    • Curtis, C. G., Stenberg, P., Brown, K. L., Baron, A., Chen, K., Gray, A., Simpson, I., and Lorand, L. (1974) Kinetics of transamidating enzymes. Production of thiol in the reactions of thiol esters with fibrinoligase. Biochemistry 13, 3257-3262.
    • (1974) Biochemistry , vol.13 , pp. 3257-3262
    • Curtis, C.G.1    Stenberg, P.2    Brown, K.L.3    Baron, A.4    Chen, K.5    Gray, A.6    Simpson, I.7    Lorand, L.8
  • 6
    • 0019886929 scopus 로고
    • New thioester substrates for fibrinoligase (coagulation factor XIIIa) and for transglutaminase. Transfer of the fluorescently labeled acyl group to amines and alcohols
    • Parameswaran, K. N., and Lorand, L. (1981) New thioester substrates for fibrinoligase (coagulation factor XIIIa) and for transglutaminase. Transfer of the fluorescently labeled acyl group to amines and alcohols. Biochemistry 20, 3703-3711.
    • (1981) Biochemistry , vol.20 , pp. 3703-3711
    • Parameswaran, K.N.1    Lorand, L.2
  • 7
    • 0016641324 scopus 로고
    • Transamidase kinetics. Amide formation in the enzymic reactions of thiol esters with amines
    • Stenberg, P., Curtis, C. G., Wing, D., Tong, Y. S., Credo, R. B., Gray, A., and Lorand, L. (1975) Transamidase kinetics. Amide formation in the enzymic reactions of thiol esters with amines. Biochem. J. 147, 155-163.
    • (1975) Biochem. J , vol.147 , pp. 155-163
    • Stenberg, P.1    Curtis, C.G.2    Wing, D.3    Tong, Y.S.4    Credo, R.B.5    Gray, A.6    Lorand, L.7
  • 12
    • 0026488212 scopus 로고
    • Isolation of transglutaminase-reactive sequences from complex biological systems: A prominent lysine donor sequence in bovine lens
    • Lorand, L., Velasco, P. T., Murthy, S. N., Wilson, J., and Parameswaran, K. N. (1992) Isolation of transglutaminase-reactive sequences from complex biological systems: A prominent lysine donor sequence in bovine lens. Proc. Natl. Acad Sci. U.S.A. 89, 11161-11163.
    • (1992) Proc. Natl. Acad Sci. U.S.A , vol.89 , pp. 11161-11163
    • Lorand, L.1    Velasco, P.T.2    Murthy, S.N.3    Wilson, J.4    Parameswaran, K.N.5
  • 13
    • 0000831938 scopus 로고
    • The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations
    • Smyth, D. G., Stein, W. H., and Moore, S. (1963) The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations. J. Biol. Chem. 238, 227-234.
    • (1963) J. Biol. Chem , vol.238 , pp. 227-234
    • Smyth, D.G.1    Stein, W.H.2    Moore, S.3
  • 14
    • 0001449760 scopus 로고
    • The Basic Trypsin Inhibitor of Bovine Pancreas. IV. The Linear Sequence of the 58 Amino Acids
    • Kassell, B., Radicevic, M., Ansfield, M. J., and Laskowski, M., Sr. (1965) The Basic Trypsin Inhibitor of Bovine Pancreas. IV. The Linear Sequence of the 58 Amino Acids. Biochem. Biophys. Res. Commun. 18, 255-258.
    • (1965) Biochem. Biophys. Res. Commun , vol.18 , pp. 255-258
    • Kassell, B.1    Radicevic, M.2    Ansfield, M.J.3    Laskowski Sr., M.4
  • 15
    • 0000385093 scopus 로고
    • The Amino Acid Sequence of Egg White Lysozyme
    • Canfield, R. E. (1963) The Amino Acid Sequence of Egg White Lysozyme. J. Biol. Chem. 238, 2698-2707.
    • (1963) J. Biol. Chem , vol.238 , pp. 2698-2707
    • Canfield, R.E.1
  • 16
    • 0025195103 scopus 로고
    • Labeling of ε-lysine crosslinking sites in proteins with peptide substrates of factor XIIIa and transglutaminase
    • Parameswaran, K. N., Velasco, P. T., Wilson, J., and Lorand, L. (1990) Labeling of ε-lysine crosslinking sites in proteins with peptide substrates of factor XIIIa and transglutaminase. Proc. Natl. Acad. Sci. U.S.A. 87, 8472-8475.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 8472-8475
    • Parameswaran, K.N.1    Velasco, P.T.2    Wilson, J.3    Lorand, L.4
  • 17
    • 0026018526 scopus 로고
    • Sorting-out of acceptor-donor relationships in the transglutaminase-catalyzed cross-linking of crystallins by the enzyme-directed labeling of potential sites
    • Lorand, L., Parameswaran, K. N., and Velasco, P. T. (1991) Sorting-out of acceptor-donor relationships in the transglutaminase-catalyzed cross-linking of crystallins by the enzyme-directed labeling of potential sites. Proc. Natl. Acad. Sci. U.S.A. 88, 82-83.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 82-83
    • Lorand, L.1    Parameswaran, K.N.2    Velasco, P.T.3
  • 18
    • 0029766569 scopus 로고    scopus 로고
    • Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: Effects on the kinetics and thermodynamics of binding to β-trypsin and α-chymotrypsin
    • Castro, M. J., and Anderson, S. (1996) Alanine point-mutations in the reactive region of bovine pancreatic trypsin inhibitor: Effects on the kinetics and thermodynamics of binding to β-trypsin and α-chymotrypsin. Biochemistry 35, 11435-11446.
    • (1996) Biochemistry , vol.35 , pp. 11435-11446
    • Castro, M.J.1    Anderson, S.2
  • 19
    • 0027416842 scopus 로고
    • Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin
    • Radek, J. T., Jeong, J. M., Murthy, S. N., Ingham, K. C., and Lorand, L. (1993) Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin. Proc. Natl. Acad. Sci. U.S.A. 90, 3152-3156.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 3152-3156
    • Radek, J.T.1    Jeong, J.M.2    Murthy, S.N.3    Ingham, K.C.4    Lorand, L.5
  • 20
    • 0032170231 scopus 로고    scopus 로고
    • Properties of purified lens transglutaminase and regulation of its transamidase/ crosslinking activity by GTP
    • Murthy, S. N., Velasco, P. T., and Lorand, L. (1998) Properties of purified lens transglutaminase and regulation of its transamidase/ crosslinking activity by GTP. Exp. Eye Res. 67, 273-281.
    • (1998) Exp. Eye Res , vol.67 , pp. 273-281
    • Murthy, S.N.1    Velasco, P.T.2    Lorand, L.3
  • 21
    • 0345661167 scopus 로고    scopus 로고
    • The intermediate filament protein, vimentin, in the lens is a target for cross-linking by transglutaminase
    • Clement, S., Velasco, P. T., Murthy, S. N., Wilson, J. H., Lukas, T. J., Goldman, R. D., and Lorand, L. (1998) The intermediate filament protein, vimentin, in the lens is a target for cross-linking by transglutaminase. J. Biol. Chem. 273, 7604-7609.
    • (1998) J. Biol. Chem , vol.273 , pp. 7604-7609
    • Clement, S.1    Velasco, P.T.2    Murthy, S.N.3    Wilson, J.H.4    Lukas, T.J.5    Goldman, R.D.6    Lorand, L.7
  • 22
    • 0040041521 scopus 로고    scopus 로고
    • Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase
    • Murthy, S. N., Wilson, J. H., Lukas, T. J., Kuret, J., and Lorand, L. (1998) Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase. J. Neurochem. 71, 2607-2614.
    • (1998) J. Neurochem , vol.71 , pp. 2607-2614
    • Murthy, S.N.1    Wilson, J.H.2    Lukas, T.J.3    Kuret, J.4    Lorand, L.5
  • 23
    • 0014216873 scopus 로고
    • Effect of alkylation of sperm whale myoglobin on response to extremes of temperature and pH
    • Clark, J. F., and Gurd, F. R. (1967) Effect of alkylation of sperm whale myoglobin on response to extremes of temperature and pH. J. Biol. Chem. 242, 3257-3264.
    • (1967) J. Biol. Chem , vol.242 , pp. 3257-3264
    • Clark, J.F.1    Gurd, F.R.2
  • 24
    • 0013894890 scopus 로고
    • The combination of chymotrypsin and chymotrypsinogen with fluorescent substrates and inhibitors for chymotrypsin
    • Deranleau, D. A., and Neurath, H. (1966) The combination of chymotrypsin and chymotrypsinogen with fluorescent substrates and inhibitors for chymotrypsin. Biochemistry 5, 1413-1425.
    • (1966) Biochemistry , vol.5 , pp. 1413-1425
    • Deranleau, D.A.1    Neurath, H.2
  • 25
    • 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
  • 26
    • 0013904011 scopus 로고
    • Labeling of amine-acceptor cross-linking sites of fibrin by transpeptidation
    • Lorand, L., and Ong, H. H. (1966) Labeling of amine-acceptor cross-linking sites of fibrin by transpeptidation. Biochemistry 5, 1747-1753.
    • (1966) Biochemistry , vol.5 , pp. 1747-1753
    • Lorand, L.1    Ong, H.H.2
  • 27
    • 0015498737 scopus 로고
    • Titration of the acceptor cross-linking sites in fibrin
    • Lorand, L., Chenoweth, D., and Gray, A. (1972) Titration of the acceptor cross-linking sites in fibrin. Ann. N.Y. Acad. Sci. 202, 155- 171.
    • (1972) Ann. N.Y. Acad. Sci , vol.202 , pp. 155-171
    • Lorand, L.1    Chenoweth, D.2    Gray, A.3
  • 28
    • 0028027240 scopus 로고
    • Residue Gln-30 of human erythrocyte anion transporter is a prime site for reaction with intrinsic transglutaminase
    • Murthy, S. N., Wilson, J., Zhang, Y., and Lorand, L. (1994) Residue Gln-30 of human erythrocyte anion transporter is a prime site for reaction with intrinsic transglutaminase. J. Biol. Chem. 269, 22907-22911.
    • (1994) J. Biol. Chem , vol.269 , pp. 22907-22911
    • Murthy, S.N.1    Wilson, J.2    Zhang, Y.3    Lorand, L.4
  • 29
    • 0004756412 scopus 로고
    • Identification of ε-Lysine Cross-Linking Sites in the α Chains of Fibrin and the Tissue Transglutaminase Carrying Role of Fibronectin in Plasma
    • Denmark
    • Lorand, L. (1991) Identification of ε-Lysine Cross-Linking Sites in the α Chains of Fibrin and the Tissue Transglutaminase Carrying Role of Fibronectin in Plasma. 20th Linderstrom-Land Conference, Vingsted, Denmark.
    • (1991) 20th Linderstrom-Land Conference, Vingsted
    • Lorand, L.1
  • 30
    • 0034972479 scopus 로고    scopus 로고
    • Factor XIII: Structure, activation, and interactions with fibrinogen and fibrin
    • Lorand, L. (2001) Factor XIII: Structure, activation, and interactions with fibrinogen and fibrin. Ann. N.Y. Acad. Sci. 936, 291-311.
    • (2001) Ann. N.Y. Acad. Sci , vol.936 , pp. 291-311
    • Lorand, L.1
  • 32
    • 0030040589 scopus 로고    scopus 로고
    • Structure of bovine pancreatic trypsin inhibitor at 125 K definition of carboxyl-terminal residues Gly57 and Ala58
    • Parkin, S., Rupp, B., and Hope, H. (1996) Structure of bovine pancreatic trypsin inhibitor at 125 K definition of carboxyl-terminal residues Gly57 and Ala58. Acta Crystallogr. D52, 18-29.
    • (1996) Acta Crystallogr , vol.D52 , pp. 18-29
    • Parkin, S.1    Rupp, B.2    Hope, H.3
  • 34
    • 25744463981 scopus 로고    scopus 로고
    • How do transglutaminases select the reactive lysine residues in their protein substrates?
    • Abstract 702
    • Murthy, S. N. P., Wilson, J., Lukas, T., and Lorand, L. (1998) How do transglutaminases select the reactive lysine residues in their protein substrates? FASEB J. 12 (8), A1432, Abstract 702.
    • (1998) FASEB J , vol.12 , Issue.8
    • Murthy, S.N.P.1    Wilson, J.2    Lukas, T.3    Lorand, L.4
  • 35
    • 0017235490 scopus 로고
    • A study of the lysyl residues in the basic pancreatic trypsin inhibitor using 1H nuclear magnetic resonance at 360 MHz
    • Brown, L. R., De Marco, A., Wagner, G., and Wuthrich, K. (1976) A study of the lysyl residues in the basic pancreatic trypsin inhibitor using 1H nuclear magnetic resonance at 360 MHz. Eur. J. Biochem. 62, 103-107.
    • (1976) Eur. J. Biochem , vol.62 , pp. 103-107
    • Brown, L.R.1    De Marco, A.2    Wagner, G.3    Wuthrich, K.4
  • 36
    • 0020481290 scopus 로고
    • Analysis of electrostatic interactions and their relationship to conformation and stability of bovine pancreatic trypsin inhibitor
    • March, K. L., Maskalick, D. G., England, R. D., Friend, S. H., and Gurd, F. R. (1982) Analysis of electrostatic interactions and their relationship to conformation and stability of bovine pancreatic trypsin inhibitor. Biochemistry 21, 5241-5251.
    • (1982) Biochemistry , vol.21 , pp. 5241-5251
    • March, K.L.1    Maskalick, D.G.2    England, R.D.3    Friend, S.H.4    Gurd, F.R.5
  • 37
    • 0026585827 scopus 로고
    • The carboxy-terminal lysine of αB-crystallin is an amine-donor substrate for tissue transglutaminase
    • Groenen, P. J., Bloemendal, H., and de Jong, W. W. (1992) The carboxy-terminal lysine of αB-crystallin is an amine-donor substrate for tissue transglutaminase. Eur. J. Biochem. 205, 671-674.
    • (1992) Eur. J. Biochem , vol.205 , pp. 671-674
    • Groenen, P.J.1    Bloemendal, H.2    de Jong, W.W.3
  • 38
    • 52949151510 scopus 로고    scopus 로고
    • Substrate Preference of Transglutaminase 2 Revealed by Logistic Regression Analysis and Intrinsic Disorder Examination
    • Csosz, E., Bagossi, P., Nagy, Z., Dosztanyi, Z., Simon, I., and Fesus, L. (2008) Substrate Preference of Transglutaminase 2 Revealed by Logistic Regression Analysis and Intrinsic Disorder Examination. J. Mol. Biol. 383, 390-402.
    • (2008) J. Mol. Biol , vol.383 , pp. 390-402
    • Csosz, E.1    Bagossi, P.2    Nagy, Z.3    Dosztanyi, Z.4    Simon, I.5    Fesus, L.6
  • 39
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • Liu, S., Cerione, R. A., and Clardy, J. (2002) Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc. Natl. Acad. Sci. U.S.A. 99, 2743-2747.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 40
    • 0141850279 scopus 로고    scopus 로고
    • A model for the reaction mechanism of the transglutaminase 3 enzyme
    • Ahvazi, B., and Steinert, P. M. (2003) A model for the reaction mechanism of the transglutaminase 3 enzyme. Exp. Mol. Med. 35, 228-242.
    • (2003) Exp. Mol. Med , vol.35 , pp. 228-242
    • Ahvazi, B.1    Steinert, P.M.2
  • 41
    • 2942705910 scopus 로고    scopus 로고
    • Crystal structure of transglutaminase 3 in complex with GMP: Structural basis for nucleotide specificity
    • Ahvazi, B., Boeshans, K. M., and Steinert, P. M. (2004) Crystal structure of transglutaminase 3 in complex with GMP: Structural basis for nucleotide specificity. J. Biol. Chem. 279, 26716-26725.
    • (2004) J. Biol. Chem , vol.279 , pp. 26716-26725
    • Ahvazi, B.1    Boeshans, K.M.2    Steinert, P.M.3
  • 42
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas, D. M., Strop, P., Brunger, A. T., and Khosla, C. (2007) Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 5, e327.
    • (2007) PLoS Biol , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 43
    • 0032718477 scopus 로고    scopus 로고
    • Interactions of G(h)/transglutaminase with phospholipase Cδ 1 and with GTP
    • Murthy, S. N., Lomasney, J. W., Mak, E. C., and Lorand, L. (1999) Interactions of G(h)/transglutaminase with phospholipase Cδ 1 and with GTP. Proc. Natl. Acad. Sci. U.S.A. 96, 11815-11819.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 11815-11819
    • Murthy, S.N.1    Lomasney, J.W.2    Mak, E.C.3    Lorand, L.4
  • 44
    • 0037022557 scopus 로고    scopus 로고
    • Conserved tryptophan in the core domain of transglutaminase is essential for catalytic activity
    • Murthy, S. N., Iismaa, S., Begg, G., Freymann, D. M., Graham, R. M., and Lorand, L. (2002) Conserved tryptophan in the core domain of transglutaminase is essential for catalytic activity. Proc. Natl. Acad. Sci. U.S.A. 99, 2738-2742.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 2738-2742
    • Murthy, S.N.1    Iismaa, S.2    Begg, G.3    Freymann, D.M.4    Graham, R.M.5    Lorand, L.6
  • 46
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner, G., Braun, W., Havel, T. F., Schaumann, T., Go, N., and Wuthrich, K. (1987) Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196, 611-639.
    • (1987) J. Mol. Biol , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wuthrich, K.6
  • 47
    • 0029820258 scopus 로고    scopus 로고
    • Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: A molecular dynamics study
    • Schiffer, C. A., and van Gunsteren, W. F. (1996) Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: A molecular dynamics study. Proteins 26, 66-71.
    • (1996) Proteins , vol.26 , pp. 66-71
    • Schiffer, C.A.1    van Gunsteren, W.F.2
  • 50
    • 0036136789 scopus 로고    scopus 로고
    • Identification of tissue transglutaminasereactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase
    • Orru, S., Ruoppolo, M., Francese, S., Vitagliano, L., Marino, G., and Esposito, C. (2002) Identification of tissue transglutaminasereactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase. Protein Sci. 11, 137-146.
    • (2002) Protein Sci , vol.11 , pp. 137-146
    • Orru, S.1    Ruoppolo, M.2    Francese, S.3    Vitagliano, L.4    Marino, G.5    Esposito, C.6


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