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Volumn 2, Issue 1, 2008, Pages 32-49

How (and why) to revive a dead enzyme: The power of chemical rescue

Author keywords

Catalysis; Glycosidase; Pyridoxal 5' phosphate; Ribozyme; Transition state structure

Indexed keywords

ASPARTATE AMINOTRANSFERASE; ENZYME; GLYCOGEN PHOSPHORYLASE; GLYCOSIDASE; HAMMERHEAD RIBOZYME; IMIDAZOLE; LYSOZYME; ORNITHINE CARBAMOYLTRANSFERASE; PEPTIDYLTRANSFERASE; PROTEIN TYROSINE KINASE; RNA; SERINE PROTEINASE; TRYPSIN;

EID: 41749110684     PISSN: 18723136     EISSN: None     Source Type: Journal    
DOI: 10.2174/187231308783334162     Document Type: Review
Times cited : (20)

References (151)
  • 1
    • 0024478059 scopus 로고
    • Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
    • Toney MD, Kirsch JF. Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines. Science 1989; 243: 1485-8.
    • (1989) Science , vol.243 , pp. 1485-1488
    • Toney, M.D.1    Kirsch, J.F.2
  • 2
    • 0026509036 scopus 로고
    • A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene
    • Eriksson AE, Baase WA, Wozniak JA, Matthews BW. A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene. Nature 1992; 355: 371-3.
    • (1992) Nature , vol.355 , pp. 371-373
    • Eriksson, A.E.1    Baase, W.A.2    Wozniak, J.A.3    Matthews, B.W.4
  • 3
    • 0029016268 scopus 로고
    • Energetic origins of specificity of ligand binding in an interior nonpolar cavity of T4 lysozyme
    • Morton A, Baase WA, Matthews BW. Energetic origins of specificity of ligand binding in an interior nonpolar cavity of T4 lysozyme. Biochemistry 1995; 34: 8564-75.
    • (1995) Biochemistry , vol.34 , pp. 8564-8575
    • Morton, A.1    Baase, W.A.2    Matthews, B.W.3
  • 4
    • 0006198801 scopus 로고
    • Type I and II copper sites obtained by external addition of ligands to a His117Gly azurin mutant
    • den Blaauwen T, Van de Kamp M, Canters GW. Type I and II copper sites obtained by external addition of ligands to a His117Gly azurin mutant. J Am Chem Soc 1991; 113: 5050-2.
    • (1991) J Am Chem Soc , vol.113 , pp. 5050-5052
    • den Blaauwen, T.1    Van de Kamp, M.2    Canters, G.W.3
  • 5
    • 0027440118 scopus 로고
    • Resonance Raman spectroscopy of the azurin His117Gly mutant. Interconversion of type 1 and type 2 copper sites through exogenous ligands
    • den Blaauwen T, Hoitink CW, Canters GW, Han J, Loehr TM, Sanders-Loehr J. Resonance Raman spectroscopy of the azurin His117Gly mutant. Interconversion of type 1 and type 2 copper sites through exogenous ligands. Biochemistry 1993; 32: 12455-64.
    • (1993) Biochemistry , vol.32 , pp. 12455-12464
    • den Blaauwen, T.1    Hoitink, C.W.2    Canters, G.W.3    Han, J.4    Loehr, T.M.5    Sanders-Loehr, J.6
  • 6
    • 0028339218 scopus 로고
    • Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His93>Gly
    • Barrick D. Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His93>Gly. Biochemistry 1994; 33: 6546-54.
    • (1994) Biochemistry , vol.33 , pp. 6546-6554
    • Barrick, D.1
  • 7
    • 0028083482 scopus 로고
    • Functional cavities in proteins: A general method for proxymal ligand substitution in myoglobin
    • DePillis GD, Decatur SM, Barrick D, Boxer SG. Functional cavities in proteins: a general method for proxymal ligand substitution in myoglobin. J Am Chem Soc 1994; 116: 6981-2.
    • (1994) J Am Chem Soc , vol.116 , pp. 6981-6982
    • DePillis, G.D.1    Decatur, S.M.2    Barrick, D.3    Boxer, S.G.4
  • 8
    • 0029100766 scopus 로고
    • Depletion and replacement of protein metal ligands
    • Barrick D. Depletion and replacement of protein metal ligands. Curr Opin Biotechnol 1995; 6: 411-8.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 411-418
    • Barrick, D.1
  • 9
    • 0032508393 scopus 로고    scopus 로고
    • Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: A chemical complementation study
    • Hays AM, Vassiliev IR, Golbeck JH, Debus RJ. Role of D1-His190 in proton-coupled electron transfer reactions in photosystem II: a chemical complementation study. Biochemistry 1998; 37: 11352-65.
    • (1998) Biochemistry , vol.37 , pp. 11352-11365
    • Hays, A.M.1    Vassiliev, I.R.2    Golbeck, J.H.3    Debus, R.J.4
  • 10
    • 2442642829 scopus 로고    scopus 로고
    • Mediation by indole analogues of electron transfer during oxygen activation in variants of Escherichia coli ribonucleotide reductase R2 lacking die electron-shuttling tryptophan 48
    • Saleh L, Kelch BA, Pathickal BA, Baldwin J, Ley BA, Bollinger JM, Jr. Mediation by indole analogues of electron transfer during oxygen activation in variants of Escherichia coli ribonucleotide reductase R2 lacking die electron-shuttling tryptophan 48. Biochemistry 2004; 43: 5943-52.
    • (2004) Biochemistry , vol.43 , pp. 5943-5952
    • Saleh, L.1    Kelch, B.A.2    Pathickal, B.A.3    Baldwin, J.4    Ley, B.A.5    Bollinger Jr., J.M.6
  • 11
    • 20444385829 scopus 로고    scopus 로고
    • Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus
    • Venkataraman P, Lamb RA, Pinto LH. Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus. J Biol Chem 2005; 280: 21463-72.
    • (2005) J Biol Chem , vol.280 , pp. 21463-21472
    • Venkataraman, P.1    Lamb, R.A.2    Pinto, L.H.3
  • 12
    • 0029823226 scopus 로고    scopus 로고
    • Chemical rescue of Asp237>Ala and Lys358>Ala mutants in the lactose permease of Escherichia coli
    • Frillingos S, Kaback HR. Chemical rescue of Asp237>Ala and Lys358>Ala mutants in the lactose permease of Escherichia coli. Biochemistry 1996; 35: 13363-7.
    • (1996) Biochemistry , vol.35 , pp. 13363-13367
    • Frillingos, S.1    Kaback, H.R.2
  • 13
    • 1442276492 scopus 로고    scopus 로고
    • Chemical rescue of a site-specific mutant of bacterial copper amine oxidase for generation of the topa quinone cofactor
    • Matsunami H, Okajima T, Hirota S, et al. Chemical rescue of a site-specific mutant of bacterial copper amine oxidase for generation of the topa quinone cofactor. Biochemistry 2004; 43: 2178-87.
    • (2004) Biochemistry , vol.43 , pp. 2178-2187
    • Matsunami, H.1    Okajima, T.2    Hirota, S.3
  • 14
    • 33644684486 scopus 로고    scopus 로고
    • Chemical rescue of a mutant enzyme in living cells
    • Qiao Y, Molina H, Pandey A, Zhang J, Cole PA. Chemical rescue of a mutant enzyme in living cells. Science 2006; 311: 1293-7.
    • (2006) Science , vol.311 , pp. 1293-1297
    • Qiao, Y.1    Molina, H.2    Pandey, A.3    Zhang, J.4    Cole, P.A.5
  • 15
    • 0015730126 scopus 로고
    • 2′ (3′)-O-N- formylmethionyl)-adenosine-5′-phosphate, a new donor substrate in peptidyl transferase catalyzed reactions
    • Cerná J, Rychlik I, Krayevsky AA, Gottikh BP. 2′ (3′)-O-N- formylmethionyl)-adenosine-5′-phosphate, a new donor substrate in peptidyl transferase catalyzed reactions. FEBS Lett 1973; 37: 188-91.
    • (1973) FEBS Lett , vol.37 , pp. 188-191
    • Cerná, J.1    Rychlik, I.2    Krayevsky, A.A.3    Gottikh, B.P.4
  • 16
    • 0016763961 scopus 로고
    • Effect of cytidine-5′-monophosphate on peptidyl transferase activity
    • Cerná J. Effect of cytidine-5′-monophosphate on peptidyl transferase activity. FEBS Lett 1975; 58: 94-8.
    • (1975) FEBS Lett , vol.58 , pp. 94-98
    • Cerná, J.1
  • 17
    • 0344101094 scopus 로고
    • The stimulation of ribosomal peptidyl transferase by cytosine and its derivatives
    • Cerná J, Holy A, Rychlik I. The stimulation of ribosomal peptidyl transferase by cytosine and its derivatives. Collection Czechoslov Chem Commun 1978; 43: 3279-91.
    • (1978) Collection Czechoslov Chem Commun , vol.43 , pp. 3279-3291
    • Cerná, J.1    Holy, A.2    Rychlik, I.3
  • 18
    • 0345099498 scopus 로고    scopus 로고
    • Mononucleotide derivatives as ribosomal P-site substrates reveal an important contribution of the 2′-OH to activity
    • Dorner S, Panuschka C, Schmid W, Barta A. Mononucleotide derivatives as ribosomal P-site substrates reveal an important contribution of the 2′-OH to activity. Nucleic Acids Res 2003; 31: 6536-42.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6536-6542
    • Dorner, S.1    Panuschka, C.2    Schmid, W.3    Barta, A.4
  • 20
    • 0036177483 scopus 로고    scopus 로고
    • A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits
    • Schmeing TM, Seila AC, Hansen JL, et al. A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits. Nat Struct Biol 2002; 9: 225-30.
    • (2002) Nat Struct Biol , vol.9 , pp. 225-230
    • Schmeing, T.M.1    Seila, A.C.2    Hansen, J.L.3
  • 21
    • 0017727274 scopus 로고
    • Effect of phosphate analogues on the activity of pyridoxal-reconstituted glycogen phosphorylase
    • Parrish RF, Uhing RJ, Graves DJ. Effect of phosphate analogues on the activity of pyridoxal-reconstituted glycogen phosphorylase. Biochemistry 1977; 16: 4824-31.
    • (1977) Biochemistry , vol.16 , pp. 4824-4831
    • Parrish, R.F.1    Uhing, R.J.2    Graves, D.J.3
  • 22
    • 0025017865 scopus 로고
    • The role of pyridoxal 5′-phosphate in glycogen phosphorylase catalysis
    • Palm D, Klein HW, Schinzel R, Buehner M, Helmreich EJ. The role of pyridoxal 5′-phosphate in glycogen phosphorylase catalysis. Biochemistry 1990; 29: 1099-107.
    • (1990) Biochemistry , vol.29 , pp. 1099-1107
    • Palm, D.1    Klein, H.W.2    Schinzel, R.3    Buehner, M.4    Helmreich, E.J.5
  • 23
    • 0033199576 scopus 로고    scopus 로고
    • Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: Answers to a long outstanding question
    • Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H, Johnson LN. Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question. EMBO J 1999; 18: 4619-32.
    • (1999) EMBO J , vol.18 , pp. 4619-4632
    • Watson, K.A.1    McCleverty, C.2    Geremia, S.3    Cottaz, S.4    Driguez, H.5    Johnson, L.N.6
  • 24
    • 0021101197 scopus 로고
    • Functions of the 5′-phosphoryl group of pyridoxal 5′-phosphate in phosphorylase: A study using pyridoxal-reconstituted enzyme as a model system
    • Chang YC, McCalmont T, Graves DJ. Functions of the 5′-phosphoryl group of pyridoxal 5′-phosphate in phosphorylase: a study using pyridoxal-reconstituted enzyme as a model system. Biochemistry 1983; 22: 4987-93.
    • (1983) Biochemistry , vol.22 , pp. 4987-4993
    • Chang, Y.C.1    McCalmont, T.2    Graves, D.J.3
  • 25
    • 0023657319 scopus 로고
    • Pyridoxal phosphate site in glycogen phosphorylase b: Structure in native enzyme and in three derivatives with modified cofactors
    • Oikonomakos NG, Johnson LN, Acharya KR, et al. Pyridoxal phosphate site in glycogen phosphorylase b: structure in native enzyme and in three derivatives with modified cofactors. Biochemistry 1987; 26: 8381-9.
    • (1987) Biochemistry , vol.26 , pp. 8381-8389
    • Oikonomakos, N.G.1    Johnson, L.N.2    Acharya, K.R.3
  • 26
    • 0030300075 scopus 로고    scopus 로고
    • Activator anion binding site in pyridoxal phosphorylase b: The binding of phosphite, phosphate, and fluorophosphate in the crystal
    • Oikonomakos NG, Zographos SE, Tsitsanou KE, Johnson LN, Acharya KR. Activator anion binding site in pyridoxal phosphorylase b: the binding of phosphite, phosphate, and fluorophosphate in the crystal. Protein Sci 1996; 5: 2416-28.
    • (1996) Protein Sci , vol.5 , pp. 2416-2428
    • Oikonomakos, N.G.1    Zographos, S.E.2    Tsitsanou, K.E.3    Johnson, L.N.4    Acharya, K.R.5
  • 27
    • 0023384982 scopus 로고
    • Engineering enzyme specificity by 'substrate-assisted catalysis'
    • Carter P, Wells JA. Engineering enzyme specificity by 'substrate-assisted catalysis'. Science 1987; 237: 394-9.
    • (1987) Science , vol.237 , pp. 394-399
    • Carter, P.1    Wells, J.A.2
  • 28
    • 0033957143 scopus 로고    scopus 로고
    • Substrate-assisted catalysis: Molecular basis and biological significance
    • Dall'Acqua W, Carter P. Substrate-assisted catalysis: molecular basis and biological significance. Protein Sci 2000; 9: 1-9.
    • (2000) Protein Sci , vol.9 , pp. 1-9
    • Dall'Acqua, W.1    Carter, P.2
  • 30
    • 0025994932 scopus 로고
    • Thrombin and H64A subtilisin cleavage of fusion proteins for preparation of human recombinant parathyroid hormone
    • Forsberg G, Brobjer M, Holmgren E, et al. Thrombin and H64A subtilisin cleavage of fusion proteins for preparation of human recombinant parathyroid hormone. J Protein Chem 1991; 10: 517-26.
    • (1991) J Protein Chem , vol.10 , pp. 517-526
    • Forsberg, G.1    Brobjer, M.2    Holmgren, E.3
  • 31
    • 0029144689 scopus 로고
    • Trypsin specificity increased through substrate-assisted catalysis
    • Corey DR, Willett WS, Coombs GS, Craik CS. Trypsin specificity increased through substrate-assisted catalysis. Biochemistry 1995; 34:11521-7.
    • (1995) Biochemistry , vol.34 , pp. 11521-11527
    • Corey, D.R.1    Willett, W.S.2    Coombs, G.S.3    Craik, C.S.4
  • 32
    • 37349043876 scopus 로고
    • chemistry and enzymology. New York, Dover
    • Jencks WP. Catalysis in chemistry and enzymology. New York, Dover, 1987.
    • (1987) Catalysis
    • Jencks, W.P.1
  • 33
    • 0029981787 scopus 로고    scopus 로고
    • The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis
    • Goldberg JM, Kirsch JF. The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis. Biochemistry 1996; 35: 5280-91.
    • (1996) Biochemistry , vol.35 , pp. 5280-5291
    • Goldberg, J.M.1    Kirsch, J.F.2
  • 34
    • 0027008407 scopus 로고
    • Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant
    • Toney MD, Kirsch JF. Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant. Protein Sci 1992; 1: 107-19.
    • (1992) Protein Sci , vol.1 , pp. 107-119
    • Toney, M.D.1    Kirsch, J.F.2
  • 35
    • 0025829773 scopus 로고
    • Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine
    • Nishimura K, Tanizawa K, Yoshimura T, et al. Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine. Biochemistry 1991; 30: 4072-7.
    • (1991) Biochemistry , vol.30 , pp. 4072-4077
    • Nishimura, K.1    Tanizawa, K.2    Yoshimura, T.3
  • 36
    • 0027462120 scopus 로고
    • Lysine 87 in the β subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release
    • Lu Z, Nagata S, McPhie P, Miles EW. Lysine 87 in the β subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination, catalysis, and product release. J Biol Chem 1993; 268: 8727-34.
    • (1993) J Biol Chem , vol.268 , pp. 8727-8734
    • Lu, Z.1    Nagata, S.2    McPhie, P.3    Miles, E.W.4
  • 37
    • 0028971010 scopus 로고
    • The tryptophan synthase α2β2 complex: Kinetic studies with a mutant enzyme (βK87T) to provide evidence for allosteric activation by an aminoacrylate intermediate
    • Banik U, Zhu DM, Chock PB, Miles EW. The tryptophan synthase α2β2 complex: kinetic studies with a mutant enzyme (βK87T) to provide evidence for allosteric activation by an aminoacrylate intermediate. Biochemistry 1995; 34: 12704-11.
    • (1995) Biochemistry , vol.34 , pp. 12704-12711
    • Banik, U.1    Zhu, D.M.2    Chock, P.B.3    Miles, E.W.4
  • 38
    • 0033548158 scopus 로고    scopus 로고
    • Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5′-phosphate. Chemical rescue studies of Lys39A1a mutant
    • Watanabe A, Kurokawa Y, Yoshimura T, et al. Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5′-phosphate. Chemical rescue studies of Lys39A1a mutant. J Biol Chem 1999; 274: 4189-94.
    • (1999) J Biol Chem , vol.274 , pp. 4189-4194
    • Watanabe, A.1    Kurokawa, Y.2    Yoshimura, T.3
  • 39
    • 0033649909 scopus 로고    scopus 로고
    • The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes
    • Mehta PK, Christen P. The molecular evolution of pyridoxal-5′-phosphate-dependent enzymes. Adv Enzymol 2000; 74: 129-84.
    • (2000) Adv Enzymol , vol.74 , pp. 129-184
    • Mehta, P.K.1    Christen, P.2
  • 40
    • 0142186241 scopus 로고    scopus 로고
    • A genomic overview of pyridoxal-phosphate-dependent enzymes
    • Percudani R., Peracchi A. A genomic overview of pyridoxal-phosphate-dependent enzymes. EMBO Rep 2003; 4: 850-4.
    • (2003) EMBO Rep , vol.4 , pp. 850-854
    • Percudani, R.1    Peracchi, A.2
  • 41
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: Mechnistic, structural, and evolutionary considerations
    • Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechnistic, structural, and evolutionary considerations. Annu Rev Biochem 2004; 73: 383-415.
    • (2004) Annu Rev Biochem , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2
  • 42
    • 0026092212 scopus 로고
    • General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase
    • Ehrig T, Hurley TD, Edenberg HJ, Bosron WF. General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase. Biochemistry 1991; 30: 1062-8.
    • (1991) Biochemistry , vol.30 , pp. 1062-1068
    • Ehrig, T.1    Hurley, T.D.2    Edenberg, H.J.3    Bosron, W.F.4
  • 43
    • 0027761914 scopus 로고
    • Evidence for lysine 80 as general base catalyst of leucine dehydrogenase
    • Sekimoto T, Matsuyama T, Fukui T, Tanizawa K. Evidence for lysine 80 as general base catalyst of leucine dehydrogenase. J Biol Chem 1993; 268: 27039-45.
    • (1993) J Biol Chem , vol.268 , pp. 27039-27045
    • Sekimoto, T.1    Matsuyama, T.2    Fukui, T.3    Tanizawa, K.4
  • 44
    • 0034719113 scopus 로고    scopus 로고
    • Identification of active site residues in E coli ketopantoate reductase by mutagenesis and chemical rescue
    • Zheng R, Blanchard JS. Identification of active site residues in E coli ketopantoate reductase by mutagenesis and chemical rescue. Biochemistry 2000; 39: 16244-51.
    • (2000) Biochemistry , vol.39 , pp. 16244-16251
    • Zheng, R.1    Blanchard, J.S.2
  • 45
    • 0141959003 scopus 로고    scopus 로고
    • On the role of Brønsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase
    • Klimacek M, Kavanagh KL, Wilson DK, Nidetzky B. On the role of Brønsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase. Biochem J 2003; 375: 141-49.
    • (2003) Biochem J , vol.375 , pp. 141-149
    • Klimacek, M.1    Kavanagh, K.L.2    Wilson, D.K.3    Nidetzky, B.4
  • 46
    • 29244467407 scopus 로고    scopus 로고
    • Guanidine derivatives rescue the Arg418A1a mutation of Tritrichomonas foetus IMP dehydrogenase
    • Guillen Schlippe YV, Hedstrom L. Guanidine derivatives rescue the Arg418A1a mutation of Tritrichomonas foetus IMP dehydrogenase. Biochemistry 2005; 44: 16695-700.
    • (2005) Biochemistry , vol.44 , pp. 16695-16700
    • Guillen Schlippe, Y.V.1    Hedstrom, L.2
  • 47
    • 0030829154 scopus 로고    scopus 로고
    • Identification and characterization of a catalytic base in bacterial luciferase by chemical rescue of a dark mutant
    • Huang S, Tu SC. Identification and characterization of a catalytic base in bacterial luciferase by chemical rescue of a dark mutant. Biochemistry 1997; 36: 14609-15.
    • (1997) Biochemistry , vol.36 , pp. 14609-14615
    • Huang, S.1    Tu, S.C.2
  • 48
    • 17544377403 scopus 로고    scopus 로고
    • Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles
    • Newmyer SL, Ortiz de Montellano PR. Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles. J Biol Chem 1996; 271: 14891-6.
    • (1996) J Biol Chem , vol.271 , pp. 14891-14896
    • Newmyer, S.L.1    Ortiz de Montellano, P.R.2
  • 49
    • 33750709274 scopus 로고    scopus 로고
    • Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to' initiate vitamin K-dependent protein carboxylation
    • Rishavy MA, Hallgren KW, Yakubenko AV, Shtofman, RL, Runge KW, Berkner KL. Brønsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to' initiate vitamin K-dependent protein carboxylation. Biochemistry 2006; 45: 13239-48.
    • (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
  • 50
    • 0037126710 scopus 로고    scopus 로고
    • Determination of proton transfer rates by chemical.rescue: Application to bacterial reaction centers
    • Paddock ML, Adelroth P, Feher G, Okamura-MY, Beatty JT. Determination of proton transfer rates by chemical.rescue: application to bacterial reaction centers. Biochemistry 2002; 41: 14716-25.
    • (2002) Biochemistry , vol.41 , pp. 14716-14725
    • Paddock, M.L.1    Adelroth, P.2    Feher, G.3    MY, O.4    Beatty, J.T.5
  • 51
    • 0035644196 scopus 로고    scopus 로고
    • Dissection of nucleophilic and acid-base catalysis in glycosidases
    • Zechel DL, Withers SG. Dissection of nucleophilic and acid-base catalysis in glycosidases. Curr Opin Chem Biol 2001; 5: 643-9.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 643-649
    • Zechel, D.L.1    Withers, S.G.2
  • 52
    • 0027788229 scopus 로고
    • β-Galactosidases of Escherichia coli with substitutions for Glu-461 can be activated by nucleophiles and can form β-D-galactosyl adducts
    • Huber RE, Chivers PT. β-Galactosidases of Escherichia coli with substitutions for Glu-461 can be activated by nucleophiles and can form β-D-galactosyl adducts. Carbohydr Res 1993; 250: 9-18.
    • (1993) Carbohydr Res , vol.250 , pp. 9-18
    • Huber, R.E.1    Chivers, P.T.2
  • 53
    • 0028303157 scopus 로고
    • The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: Evidence from detailed kinetic studies of mutants
    • MacLeod AM, Lindhorst T, Withers SG, Warren RA. The acid/base catalyst in the exoglucanase/xylanase from Cellulomonas fimi is glutamic acid 127: evidence from detailed kinetic studies of mutants. Biochemistry 1994; 33: 6371-6.
    • (1994) Biochemistry , vol.33 , pp. 6371-6376
    • MacLeod, A.M.1    Lindhorst, T.2    Withers, S.G.3    Warren, R.A.4
  • 54
    • 0028191018 scopus 로고
    • Changing enzymatic reaction mechanisms by mutagenesis: Conversion of a retaining glucosidase to an inverting enzyme
    • Wang Q, Graham RW, Trimbur D, Warren RAJ, Withers SG. Changing enzymatic reaction mechanisms by mutagenesis: conversion of a retaining glucosidase to an inverting enzyme. J Am Chem Soc 1994; 116: 11594-5.
    • (1994) J Am Chem Soc , vol.116 , pp. 11594-11595
    • Wang, Q.1    Graham, R.W.2    Trimbur, D.3    Warren, R.A.J.4    Withers, S.G.5
  • 55
    • 0001463551 scopus 로고
    • Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a retaining glycesidase
    • Withers SG, Warren RAJ, Street IP, Rupitz K, Kempton JB, Aebersold R. Unequivocal demonstration of the involvement of a glutamate residue as a nucleophile in the mechanism of a retaining glycesidase. J Am Chem Soc 1990; 112: 5887-9.
    • (1990) J Am Chem Soc , vol.112 , pp. 5887-5889
    • Withers, S.G.1    Warren, R.A.J.2    Street, I.P.3    Rupitz, K.4    Kempton, J.B.5    Aebersold, R.6
  • 56
    • 0028848613 scopus 로고
    • Identification of the acid/base catalyst in Agrobacterium faecalis β-glucosidase by kinetic analysis of mutants
    • Wang Q, Trimbur D, Graham R, Warren RA, Withers SG. Identification of the acid/base catalyst in Agrobacterium faecalis β-glucosidase by kinetic analysis of mutants. Biochemistry 1995; 34: 14554-62.
    • (1995) Biochemistry , vol.34 , pp. 14554-14562
    • Wang, Q.1    Trimbur, D.2    Graham, R.3    Warren, R.A.4    Withers, S.G.5
  • 57
    • 0034789376 scopus 로고    scopus 로고
    • Enzymatic synthesis of carbon-fluorine bonds
    • Zechel DL, Reid SP, Nashiru O, et al. Enzymatic synthesis of carbon-fluorine bonds. J Am Chem Soc 2001; 123: 4350-1.
    • (2001) J Am Chem Soc , vol.123 , pp. 4350-4351
    • Zechel, D.L.1    Reid, S.P.2    Nashiru, O.3
  • 58
    • 0035895363 scopus 로고    scopus 로고
    • Chemical rescue of phosphoryl transfer in a cavity mutant: A cautionary tale for site-directed mutagenesis
    • Admiraal SJ, Meyer P, Schneider B, Deville-Bonne D, Janin J, Herschlag D. Chemical rescue of phosphoryl transfer in a cavity mutant: a cautionary tale for site-directed mutagenesis. Biochemistry 2001; 40: 403-13.
    • (2001) Biochemistry , vol.40 , pp. 403-413
    • Admiraal, S.J.1    Meyer, P.2    Schneider, B.3    Deville-Bonne, D.4    Janin, J.5    Herschlag, D.6
  • 59
    • 0029818948 scopus 로고    scopus 로고
    • Mechanistic consequences of mutation of active site carboxylates in a retaining β-1,4-glycanase from Cellulomonas fimi
    • MacLeod AM, Tull D, Rupitz K, Warren RA, Withers SG. Mechanistic consequences of mutation of active site carboxylates in a retaining β-1,4-glycanase from Cellulomonas fimi. Biochemistry 1996; 35: 13165-72.
    • (1996) Biochemistry , vol.35 , pp. 13165-13172
    • MacLeod, A.M.1    Tull, D.2    Rupitz, K.3    Warren, R.A.4    Withers, S.G.5
  • 60
    • 0032497939 scopus 로고    scopus 로고
    • Restoration of the activity of active-site mutants of the hyperthermophilic β-glycosidase from Sulfolobus solfataricus: Dependence of the mechanism on the action of external nucleophiles
    • Moracci M, Trincone A, Perugino G, Ciaramella M, Rossi M. Restoration of the activity of active-site mutants of the hyperthermophilic β-glycosidase from Sulfolobus solfataricus: dependence of the mechanism on the action of external nucleophiles. Biochemistry 1998; 37: 17262-70.
    • (1998) Biochemistry , vol.37 , pp. 17262-17270
    • Moracci, M.1    Trincone, A.2    Perugino, G.3    Ciaramella, M.4    Rossi, M.5
  • 61
    • 0032508394 scopus 로고    scopus 로고
    • Probing the mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues
    • Viladot JL, de Ramon E, Durany O, Planas A. Probing the mechanism of Bacillus 1,3-1,4-β-D-glucan 4-glucanohydrolases by chemical rescue of inactive mutants at catalytically essential residues. Biochemistry 1998; 37: 11332-42.
    • (1998) Biochemistry , vol.37 , pp. 11332-11342
    • Viladot, J.L.1    de Ramon, E.2    Durany, O.3    Planas, A.4
  • 63
    • 0346319022 scopus 로고    scopus 로고
    • Detailed kinetic analysis and identification of the nucleophile in α-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase
    • Shallom D, Belakhov V, Solomon D, Shoham G, Baasov T, Shoham Y. Detailed kinetic analysis and identification of the nucleophile in α-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. J Biol Chem 2002; 277: 43667-73.
    • (2002) J Biol Chem , vol.277 , pp. 43667-43673
    • Shallom, D.1    Belakhov, V.2    Solomon, D.3    Shoham, G.4    Baasov, T.5    Shoham, Y.6
  • 64
    • 0038131058 scopus 로고    scopus 로고
    • Mechanism, mutagenesis, and chemical rescue of a β-mannosidase from Cellulomonas fimi
    • Zechel DL, Reid SP, Stoll D, Nashiru O, Warren RA, Withers SG. Mechanism, mutagenesis, and chemical rescue of a β-mannosidase from Cellulomonas fimi. Biochemistry 2003, 42: 7195-204.
    • (2003) Biochemistry , vol.42 , pp. 7195-7204
    • Zechel, D.L.1    Reid, S.P.2    Stoll, D.3    Nashiru, O.4    Warren, R.A.5    Withers, S.G.6
  • 65
    • 0042527531 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile of the family 29 α-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant
    • Cobucci-Ponzano B, Trincone A, Giordano A, Rossi M, Moracci M. Identification of the catalytic nucleophile of the family 29 α-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant. Biochemistry 2003; 42: 9525-31.
    • (2003) Biochemistry , vol.42 , pp. 9525-9531
    • Cobucci-Ponzano, B.1    Trincone, A.2    Giordano, A.3    Rossi, M.4    Moracci, M.5
  • 66
    • 0038035884 scopus 로고    scopus 로고
    • Identification of the catalytic residues in family 52 glycoside hydrolase, a β-xylosidase from Geobacillus stearothermophilus T-6
    • Bravman T, Belakhov V, Solomon D, et al. Identification of the catalytic residues in family 52 glycoside hydrolase, a β-xylosidase from Geobacillus stearothermophilus T-6. J Biol Chem 2003; 278: 26742-9.
    • (2003) J Biol Chem , vol.278 , pp. 26742-26749
    • Bravman, T.1    Belakhov, V.2    Solomon, D.3
  • 67
    • 29144438960 scopus 로고    scopus 로고
    • Cloning and characterization of Thermotoga maritima β-glucuronidase
    • Salleh HM, Mullegger J, Reid SP, et al. Cloning and characterization of Thermotoga maritima β-glucuronidase. Carbohydr Res 2006; 341: 49-59.
    • (2006) Carbohydr Res , vol.341 , pp. 49-59
    • Salleh, H.M.1    Mullegger, J.2    Reid, S.P.3
  • 68
    • 33745358234 scopus 로고    scopus 로고
    • Asp-196>A1a mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate
    • Schwarz A, Nidetzky B. Asp-196>A1a mutant of Leuconostoc mesenteroides sucrose phosphorylase exhibits altered stereochemical course and kinetic mechanism of glucosyl transfer to and from phosphate. FEBS Lett 2006; 580: 3905-10.
    • (2006) FEBS Lett , vol.580 , pp. 3905-3910
    • Schwarz, A.1    Nidetzky, B.2
  • 69
    • 33845584643 scopus 로고    scopus 로고
    • Chemical rescue of 3-galactosyltransferase. Implications in the mechanism of retaining glycosyltransferases
    • Monegal A, Planas A. Chemical rescue of 3-galactosyltransferase. Implications in the mechanism of retaining glycosyltransferases. J Am Chem Soc 2006; 128: 16030-31.
    • (2006) J Am Chem Soc , vol.128 , pp. 16030-16031
    • Monegal, A.1    Planas, A.2
  • 70
    • 0034696084 scopus 로고    scopus 로고
    • A novel thermophilic glycosynthase that effects branching glycosylation
    • Trincone A, Perugino G, Rossi M, Moracci M. A novel thermophilic glycosynthase that effects branching glycosylation. Bioorg Med Chem Lett 2000; 10: 365-8.
    • (2000) Bioorg Med Chem Lett , vol.10 , pp. 365-368
    • Trincone, A.1    Perugino, G.2    Rossi, M.3    Moracci, M.4
  • 72
    • 0024043994 scopus 로고
    • Electrostatic complementarity within the substrate-binding pocket of trypsin
    • Graf L, Jancso A, Szilagyi L, et al. Electrostatic complementarity within the substrate-binding pocket of trypsin. Proc Natl Acad Sci USA 1988; 85: 4961-5.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4961-4965
    • Graf, L.1    Jancso, A.2    Szilagyi, L.3
  • 74
    • 0032545106 scopus 로고    scopus 로고
    • 1.85-Å resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-omithine. Catalytic mechanism and correlation with inherited deficiency
    • Shi D, Morizono H, Ha Y, Aoyagi M, Tuchman M, Allewell NM. 1.85-Å resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-omithine. Catalytic mechanism and correlation with inherited deficiency. J Biol Chem 1998; 273: 34247-54.
    • (1998) J Biol Chem , vol.273 , pp. 34247-34254
    • Shi, D.1    Morizono, H.2    Ha, Y.3    Aoyagi, M.4    Tuchman, M.5    Allewell, N.M.6
  • 75
    • 0034733518 scopus 로고    scopus 로고
    • Mechanism of inactivation of ornithine transcarbamoylase by Nδ - (N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism
    • Langley DB, Templeton MD, Fields BA, Mitchell RE, Collyer CA. Mechanism of inactivation of ornithine transcarbamoylase by Nδ - (N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism. J Biol Chem 2000; 275: 20012-9.
    • (2000) J Biol Chem , vol.275 , pp. 20012-20019
    • Langley, D.B.1    Templeton, M.D.2    Fields, B.A.3    Mitchell, R.E.4    Collyer, C.A.5
  • 76
    • 0029920420 scopus 로고    scopus 로고
    • Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase
    • Murata LB, Schachman HK. Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase. Protein Sci. 1996; 5: 709-18.
    • (1996) Protein Sci , vol.5 , pp. 709-718
    • Murata, L.B.1    Schachman, H.K.2
  • 77
    • 0030445397 scopus 로고    scopus 로고
    • Chemical-rescue by guanidine derivatives of an arginine-substituted site-directed mutant of Escherichia coli ornithine transcarbamylase
    • Rynkiewicz MJ, Seaton BA. Chemical-rescue by guanidine derivatives of an arginine-substituted site-directed mutant of Escherichia coli ornithine transcarbamylase. Biochemistry 1996; 35: 16174-9.
    • (1996) Biochemistry , vol.35 , pp. 16174-16179
    • Rynkiewicz, M.J.1    Seaton, B.A.2
  • 78
    • 0027048612 scopus 로고
    • Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR, and X-ray crystallographic study
    • Stebbins JW, Robertson DE, Roberts MF, Stevens RC, Lipscomb WN, Kantrowitz ER. Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, NMR, and X-ray crystallographic study. Protein Sci 1992; 1: 1435-46.
    • (1992) Protein Sci , vol.1 , pp. 1435-1446
    • Stebbins, J.W.1    Robertson, D.E.2    Roberts, M.F.3    Stevens, R.C.4    Lipscomb, W.N.5    Kantrowitz, E.R.6
  • 79
    • 0024261193 scopus 로고
    • Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: Role of arginine-57 in substrate binding and catalysis
    • Kuo LC, Miller AW, Lee S, Kozuma C. Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis. Biochemistry 1988; 27: 8823-32.
    • (1988) Biochemistry , vol.27 , pp. 8823-8832
    • Kuo, L.C.1    Miller, A.W.2    Lee, S.3    Kozuma, C.4
  • 80
    • 0027194318 scopus 로고
    • Protonation of arginine 57 of Escherichia coli ornithine transcarbamoylase regulates substrate binding and turnover
    • Goldsmith JO, Kuo LC. Protonation of arginine 57 of Escherichia coli ornithine transcarbamoylase regulates substrate binding and turnover. J Biol Chem 1993; 268: 18485-90.
    • (1993) J Biol Chem , vol.268 , pp. 18485-18490
    • Goldsmith, J.O.1    Kuo, L.C.2
  • 81
    • 9744226460 scopus 로고    scopus 로고
    • A twisted base? The role of arginine in enzyme-catalyzed proton abstractions
    • Guillen Schlippe YV, Hedstrom L. A twisted base? The role of arginine in enzyme-catalyzed proton abstractions. Arch BioChem Biophys 2005; 433: 266-78.
    • (2005) Arch BioChem Biophys , vol.433 , pp. 266-278
    • Guillen Schlippe, Y.V.1    Hedstrom, L.2
  • 82
    • 0027049221 scopus 로고
    • Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127
    • Phillips MA, Hedstrom L, Rutter WJ. Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127. Protein Sci 1992; 1: 517-21.
    • (1992) Protein Sci , vol.1 , pp. 517-521
    • Phillips, M.A.1    Hedstrom, L.2    Rutter, W.J.3
  • 83
    • 0028233659 scopus 로고
    • Chemical rescue by exogenous amines of a site-directed mutant of ribulose 1,5-bisphosphate carboxylase/oxygenase that lacks a key lysyl residue
    • Harpel MR, Hartman FC. Chemical rescue by exogenous amines of a site-directed mutant of ribulose 1,5-bisphosphate carboxylase/oxygenase that lacks a key lysyl residue. Biochemistry 1994; 33: 5553-61.
    • (1994) Biochemistry , vol.33 , pp. 5553-5561
    • Harpel, M.R.1    Hartman, F.C.2
  • 84
    • 0034603706 scopus 로고    scopus 로고
    • Identification of essential arginines in the acetate kinase from Methanosarcina thermophila
    • Singh-Wissmann K, Miles RD, Ingram-Smith C, Ferry JG. Identification of essential arginines in the acetate kinase from Methanosarcina thermophila. Biochemistry 2000; 39:3671-7.
    • (2000) Biochemistry , vol.39 , pp. 3671-3677
    • Singh-Wissmann, K.1    Miles, R.D.2    Ingram-Smith, C.3    Ferry, J.G.4
  • 85
    • 0032571307 scopus 로고    scopus 로고
    • Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions
    • Baldwin E, Baase WA, Zhang X, Feher V, Matthews BW. Generation of ligand binding sites in T4 lysozyme by deficiency-creating substitutions. J Mol Biol 1998; 277: 467-85.
    • (1998) J Mol Biol , vol.277 , pp. 467-485
    • Baldwin, E.1    Baase, W.A.2    Zhang, X.3    Feher, V.4    Matthews, B.W.5
  • 87
    • 0033536578 scopus 로고    scopus 로고
    • Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability
    • Wray JW, Baase WA, Lindstrom JD, Weaver LH, Poteete AR, Matthews BW. Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. J Mol Biol 1999; 292: 1111-20.
    • (1999) J Mol Biol , vol.292 , pp. 1111-1120
    • Wray, J.W.1    Baase, W.A.2    Lindstrom, J.D.3    Weaver, L.H.4    Poteete, A.R.5    Matthews, B.W.6
  • 88
    • 0029859191 scopus 로고    scopus 로고
    • Rescue of abasic hammerhead ribozymes by exogenous addition of specific bases
    • Peracchi A, Beigelman L, Usman N, Herschlag D. Rescue of abasic hammerhead ribozymes by exogenous addition of specific bases. Proc Natl Acad Sci USA 1996; 93: 11522-7.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11522-11527
    • Peracchi, A.1    Beigelman, L.2    Usman, N.3    Herschlag, D.4
  • 89
    • 0031758565 scopus 로고    scopus 로고
    • Structure-function relationships in the hammerhead ribozyme probed by base rescue
    • Peracchi A, Matulic-Adamic J, Wang S, Beigelman L, Herschlag D. Structure-function relationships in the hammerhead ribozyme probed by base rescue. RNA 1998; 4: 1332-46.
    • (1998) RNA , vol.4 , pp. 1332-1346
    • Peracchi, A.1    Matulic-Adamic, J.2    Wang, S.3    Beigelman, L.4    Herschlag, D.5
  • 90
    • 0028063567 scopus 로고
    • Three-dimensional structure of a hammerhead ribozyme
    • Pley HW, Flaherty KM, McKay DB. Three-dimensional structure of a hammerhead ribozyme. Nature 1994; 372: 68-74.
    • (1994) Nature , vol.372 , pp. 68-74
    • Pley, H.W.1    Flaherty, K.M.2    McKay, D.B.3
  • 91
    • 0029073091 scopus 로고
    • The crystal structure of an all-RNA hammerhead ribozyme: A proposed mechanism for RNA catalytic cleavage
    • Scott WG, Finch JT, Klug A. The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA catalytic cleavage. Cell 1995; 81: 991-1002.
    • (1995) Cell , vol.81 , pp. 991-1002
    • Scott, W.G.1    Finch, J.T.2    Klug, A.3
  • 92
    • 0032552962 scopus 로고    scopus 로고
    • A core folding model for catalysis by the hammerhead ribozyme accounts for its extraordinary sensitivity to abasic mutations
    • Peracchi A, Karpeisky A, Maloney L, Beigelman L, Herschlag D. A core folding model for catalysis by the hammerhead ribozyme accounts for its extraordinary sensitivity to abasic mutations. Biochemistry 1998; 37: 14765-75.
    • (1998) Biochemistry , vol.37 , pp. 14765-14775
    • Peracchi, A.1    Karpeisky, A.2    Maloney, L.3    Beigelman, L.4    Herschlag, D.5
  • 93
    • 33746228126 scopus 로고    scopus 로고
    • Tertiary contacts distant from the active site prime a ribozyme for catalysis
    • Martick M, Scott WG. Tertiary contacts distant from the active site prime a ribozyme for catalysis. Cell 2006; 126: 309-20.
    • (2006) Cell , vol.126 , pp. 309-320
    • Martick, M.1    Scott, W.G.2
  • 94
    • 33746938267 scopus 로고    scopus 로고
    • When to believe what you see
    • Nelson JA, Uhlenbeck OC. When to believe what you see. Mol Cell 2006; 23: 447-50.
    • (2006) Mol Cell , vol.23 , pp. 447-450
    • Nelson, J.A.1    Uhlenbeck, O.C.2
  • 95
    • 0036237379 scopus 로고    scopus 로고
    • Rescue of an abasic hairpin ribozyme by cationic nucleobases. Evidence for a novel mechanism of RNA catalysis
    • Lebruska LL, Kuzmine, II, Fedor MJ. Rescue of an abasic hairpin ribozyme by cationic nucleobases. Evidence for a novel mechanism of RNA catalysis. Chem Biol 2002; 9: 465-73.
    • (2002) Chem Biol , vol.9 , pp. 465-473
    • Lebruska, L.L.1    Kuzmine, I.2    Fedor, M.J.3
  • 96
    • 2942577491 scopus 로고    scopus 로고
    • Role of an active site guanine in hairpin ribozyme catalysis probed by exogenous nucleobase rescue
    • Kuzmin YI, Da Costa CP, Fedor MJ. Role of an active site guanine in hairpin ribozyme catalysis probed by exogenous nucleobase rescue. J Mol Biol 2004; 340: 233-51.
    • (2004) J Mol Biol , vol.340 , pp. 233-251
    • Kuzmin, Y.I.1    Da Costa, C.P.2    Fedor, M.J.3
  • 97
    • 20344405966 scopus 로고    scopus 로고
    • Role of an active site adenine in hairpin ribozyme catalysis
    • Kuzmin YI, Da Costa CP, Cottrell JW, Fedor MJ. Role of an active site adenine in hairpin ribozyme catalysis. J Mol Biol 2005; 349: 989-1010.
    • (2005) J Mol Biol , vol.349 , pp. 989-1010
    • Kuzmin, Y.I.1    Da Costa, C.P.2    Cottrell, J.W.3    Fedor, M.J.4
  • 98
    • 0033215448 scopus 로고    scopus 로고
    • Imidazole rescue of a cytosine mutation in a self-cleaving ribozyme
    • Perrotta AT, Shih I, Been MD. Imidazole rescue of a cytosine mutation in a self-cleaving ribozyme. Science 1999; 286: 123-6.
    • (1999) Science , vol.286 , pp. 123-126
    • Perrotta, A.T.1    Shih, I.2    Been, M.D.3
  • 99
    • 0034712097 scopus 로고    scopus 로고
    • General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme
    • Nakano S, Chadalavada DM, Bevilacqua PC. General acid-base catalysis in the mechanism of a hepatitis delta virus ribozyme. Science 2000; 287: 1493-7.
    • (2000) Science , vol.287 , pp. 1493-1497
    • Nakano, S.1    Chadalavada, D.M.2    Bevilacqua, P.C.3
  • 100
    • 0035852640 scopus 로고    scopus 로고
    • Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage
    • Shih IH, Been MD. Involvement of a cytosine side chain in proton transfer in the rate-determining step of ribozyme self-cleavage. Proc Natl Acad Sci USA 2001; 98: 1489-94.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1489-1494
    • Shih, I.H.1    Been, M.D.2
  • 101
    • 33745627769 scopus 로고    scopus 로고
    • Chemical rescue, multiple ionizable groups and general acid-base catalysis in the HDV genomic ribozyme
    • Perrotta AT, Wadkins TS, Been MD. Chemical rescue, multiple ionizable groups and general acid-base catalysis in the HDV genomic ribozyme. RNA 2006; 12: 1282-91.
    • (2006) RNA , vol.12 , pp. 1282-1291
    • Perrotta, A.T.1    Wadkins, T.S.2    Been, M.D.3
  • 102
    • 2442641641 scopus 로고    scopus 로고
    • A conformational switch controls hepatitis delta virus ribozyme catalysis
    • Ke A, Zhou K, Ding F, Cate JH, Doudna JA. A conformational switch controls hepatitis delta virus ribozyme catalysis. Nature 2004; 429: 201-5.
    • (2004) Nature , vol.429 , pp. 201-205
    • Ke, A.1    Zhou, K.2    Ding, F.3    Cate, J.H.4    Doudna, J.A.5
  • 103
    • 0032497521 scopus 로고    scopus 로고
    • Crystal structure of a hepatitis delta virus ribozyme
    • Ferre-D'Amare AR, Zhou K, Doudna JA. Crystal structure of a hepatitis delta virus ribozyme. Nature 1998; 395: 567-74.
    • (1998) Nature , vol.395 , pp. 567-574
    • Ferre-D'Amare, A.R.1    Zhou, K.2    Doudna, J.A.3
  • 104
    • 0028446537 scopus 로고
    • A three-dimensional model of hepatitis delta virus ribozyme based on biochemical and mutational analyses
    • Tanner NK, Schaff S, Thill G, Petit-Koskas E, Crain-Denoyelle AM, Westhof E. A three-dimensional model of hepatitis delta virus ribozyme based on biochemical and mutational analyses. Curr Biol 1994; 4: 488-98.
    • (1994) Curr Biol , vol.4 , pp. 488-498
    • Tanner, N.K.1    Schaff, S.2    Thill, G.3    Petit-Koskas, E.4    Crain-Denoyelle, A.M.5    Westhof, E.6
  • 105
    • 0029964591 scopus 로고    scopus 로고
    • Core sequences and a cleavage site wobble pair required for HDV antigenomic ribozyme self-cleavage
    • Perrotta AT, Been MD. Core sequences and a cleavage site wobble pair required for HDV antigenomic ribozyme self-cleavage. Nucleic Acids Res 1996; 24: 1314-21.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1314-1321
    • Perrotta, A.T.1    Been, M.D.2
  • 106
    • 0033214432 scopus 로고    scopus 로고
    • Chemical diversity in RNA cleavage
    • Westhof E. Chemical diversity in RNA cleavage. Science 1999; 286: 61-2.
    • (1999) Science , vol.286 , pp. 61-62
    • Westhof, E.1
  • 107
    • 24644454458 scopus 로고    scopus 로고
    • General acid catalysis by the hepatitis delta virus ribozyme
    • Das SA, Piccirilli JA. General acid catalysis by the hepatitis delta virus ribozyme. Nature Chem Biol 2005; 1: 45-52.
    • (2005) Nature Chem Biol , vol.1 , pp. 45-52
    • Das, S.A.1    Piccirilli, J.A.2
  • 109
    • 33748559498 scopus 로고    scopus 로고
    • Nucleobase catalysis in ribozyme mechanism
    • Bevilacqua PC, Yajima R. Nucleobase catalysis in ribozyme mechanism. Curr Opin Chem Biol 2006; 10: 455-64.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 455-464
    • Bevilacqua, P.C.1    Yajima, R.2
  • 110
    • 0029278886 scopus 로고
    • Structure-function relationships in Src family and related protein tyrosine kinases
    • Superti-Furga G, Courtneidge SA. Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays 1995; 17: 321-30.
    • (1995) Bioessays , vol.17 , pp. 321-330
    • Superti-Furga, G.1    Courtneidge, S.A.2
  • 111
    • 33751272653 scopus 로고    scopus 로고
    • Structural biology of protein tyrosine kinases
    • Cowan-Jacob SW. Structural biology of protein tyrosine kinases. Cell Mol Life Sci 2006; 63: 2608-25.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2608-2625
    • Cowan-Jacob, S.W.1
  • 112
    • 0034623991 scopus 로고    scopus 로고
    • Chemical rescue of a mutant protein-tyrosine kinase
    • Williams DM, Wang D, Cole PA. Chemical rescue of a mutant protein-tyrosine kinase. J Biol Chem 2000; 275: 38127-30.
    • (2000) J Biol Chem , vol.275 , pp. 38127-38130
    • Williams, D.M.1    Wang, D.2    Cole, P.A.3
  • 113
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard SR. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J 1997; 16: 5572-81.
    • (1997) EMBO J , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 114
    • 0036083580 scopus 로고    scopus 로고
    • Csk, a critical link of g protein signals to actin cytoskeletal reorganization
    • Lowry WE, Huang J, Ma YC, et al. Csk, a critical link of g protein signals to actin cytoskeletal reorganization. Dev Cell 2002; 2: 733-44.
    • (2002) Dev Cell , vol.2 , pp. 733-744
    • Lowry, W.E.1    Huang, J.2    Ma, Y.C.3
  • 115
    • 33644869798 scopus 로고    scopus 로고
    • Csk mediates g-protein-coupled lysophosphatidic acid receptor-induced inhibition of membrane-bound guanylyl cyclase activity
    • Madhusoodanan KS, Guo D, McGarrigle DK, Maack T, Huang XY. Csk mediates g-protein-coupled lysophosphatidic acid receptor-induced inhibition of membrane-bound guanylyl cyclase activity. Biochemistry 2006; 45: 3396-403.
    • (2006) Biochemistry , vol.45 , pp. 3396-3403
    • Madhusoodanan, K.S.1    Guo, D.2    McGarrigle, D.K.3    Maack, T.4    Huang, X.Y.5
  • 116
    • 0036889449 scopus 로고    scopus 로고
    • Imidazole-induced cell death, associated with intracellular acidification, caspase-3 activation, DFF-45 cleavage, but not oligonucleosomal DNA fragmentation
    • Iguchi K, Usui S, Ishida R, Hirano K. Imidazole-induced cell death, associated with intracellular acidification, caspase-3 activation, DFF-45 cleavage, but not oligonucleosomal DNA fragmentation. Apoptosis 2002; 7: 519-25.
    • (2002) Apoptosis , vol.7 , pp. 519-525
    • Iguchi, K.1    Usui, S.2    Ishida, R.3    Hirano, K.4
  • 117
    • 39049179466 scopus 로고    scopus 로고
    • Raising enzymes from the dead and the secrets they can tell. ACS
    • Marletta MA. Raising enzymes from the dead and the secrets they can tell. ACS Chem Biol 2006; 1: 73-4.
    • (2006) Chem Biol , vol.1 , pp. 73-74
    • Marletta, M.A.1
  • 118
    • 0033554373 scopus 로고    scopus 로고
    • Role of His159 in yeast enolase catalysis
    • Vinarov DA, Nowak T. Role of His159 in yeast enolase catalysis. Biochemistry 1999; 38: 12138-49.
    • (1999) Biochemistry , vol.38 , pp. 12138-12149
    • Vinarov, D.A.1    Nowak, T.2
  • 119
    • 0036396544 scopus 로고    scopus 로고
    • Functional group requirements in the probable active site of the VS ribozyme
    • Lafontaine DA, Wilson TJ, Zhao ZY, Lilley DM. Functional group requirements in the probable active site of the VS ribozyme. J Mol Biol 2002; 323: 23-34.
    • (2002) J Mol Biol , vol.323 , pp. 23-34
    • Lafontaine, D.A.1    Wilson, T.J.2    Zhao, Z.Y.3    Lilley, D.M.4
  • 120
    • 15444372631 scopus 로고    scopus 로고
    • Reaction of morphinone reductase with 2-cyclohexen-1-one and 1-nitrocyclohexene: Proton donation, ligand binding, and the role of residues Histidine 186 and Asparagine 189
    • Messiha HL, Munro AW, Bruce NC, Barsukov I, Scrutton NS. Reaction of morphinone reductase with 2-cyclohexen-1-one and 1-nitrocyclohexene: proton donation, ligand binding, and the role of residues Histidine 186 and Asparagine 189. J Biol Chem 2005; 280: 10695-709.
    • (2005) J Biol Chem , vol.280 , pp. 10695-10709
    • Messiha, H.L.1    Munro, A.W.2    Bruce, N.C.3    Barsukov, I.4    Scrutton, N.S.5
  • 121
    • 33745307149 scopus 로고    scopus 로고
    • PrrC-anticodon nuclease: Functional organization of a prototypical bacterial restriction RNase
    • Blanga-Kanfi S, Amitsur M, Azem A, Kaufmann G. PrrC-anticodon nuclease: functional organization of a prototypical bacterial restriction RNase. Nucleic Acids Res 2006; 34: 3209-19.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3209-3219
    • Blanga-Kanfi, S.1    Amitsur, M.2    Azem, A.3    Kaufmann, G.4
  • 122
    • 27844577292 scopus 로고    scopus 로고
    • Probing the role of the hyper-reactive histidine residue of arginase
    • Colleluori DM, Reczkowski RS, Emig FA, et al. Probing the role of the hyper-reactive histidine residue of arginase. Arch Biochem Biophys 2005; 444: 15-26.
    • (2005) Arch Biochem Biophys , vol.444 , pp. 15-26
    • Colleluori, D.M.1    Reczkowski, R.S.2    Emig, F.A.3
  • 123
    • 33947240200 scopus 로고    scopus 로고
    • Ziegler K, Noble SM, Mutumanje E, Bishop B, Huddler DP, Born TL. Identification of catalytic cysteine, histidine, and lysine residues in Escherichia coli homoserine transsuccinylase. Biochemistry 2007; 46: in press.
    • Ziegler K, Noble SM, Mutumanje E, Bishop B, Huddler DP, Born TL. Identification of catalytic cysteine, histidine, and lysine residues in Escherichia coli homoserine transsuccinylase. Biochemistry 2007; 46: in press.
  • 124
    • 0029832567 scopus 로고    scopus 로고
    • Activation of E350A mutant maltodextrin phosphorylase by exogenously added acetate
    • Drueckes P, Schinzel R. Activation of E350A mutant maltodextrin phosphorylase by exogenously added acetate. Protein Eng 1996; 9: 701-5.
    • (1996) Protein Eng , vol.9 , pp. 701-705
    • Drueckes, P.1    Schinzel, R.2
  • 125
    • 33645933904 scopus 로고    scopus 로고
    • Direct detection and kinetic analysis of covalent intermediate formation in the 4-amino-4-deoxychorismate synthase catalyzed reaction
    • He Z, Toney MD. Direct detection and kinetic analysis of covalent intermediate formation in the 4-amino-4-deoxychorismate synthase catalyzed reaction. Biochemistry 2006; 45: 5019-28.
    • (2006) Biochemistry , vol.45 , pp. 5019-5028
    • He, Z.1    Toney, M.D.2
  • 126
    • 0028988441 scopus 로고
    • 1H NMR characterization of myoglobins where exogenous ligands replace the proximal histidine
    • Decatur SM, Boxer SG. 1H NMR characterization of myoglobins where exogenous ligands replace the proximal histidine. Biochemistry 1995; 34: 2122-9.
    • (1995) Biochemistry , vol.34 , pp. 2122-2129
    • Decatur, S.M.1    Boxer, S.G.2
  • 127
    • 0033520066 scopus 로고    scopus 로고
    • (S)-Mandelate dehydrogenase from Pseudomonas putida: Mutations of the catalytic base histidine-274 and chemical rescue of activity
    • Lehoux IE, Mitra B. (S)-Mandelate dehydrogenase from Pseudomonas putida: mutations of the catalytic base histidine-274 and chemical rescue of activity. Biochemistry 1999; 38: 9948-55.
    • (1999) Biochemistry , vol.38 , pp. 9948-9955
    • Lehoux, I.E.1    Mitra, B.2
  • 128
    • 25844477108 scopus 로고    scopus 로고
    • Chemical rescue of I-site cleavage in living cells and in vitro discriminates between the cytomegalovirus protease, assemblin, and its precursor, pUL80a
    • McCartney SA, Brignole EJ, Kolegraff KN, Loveland AN, Ussin LM, Gibson W. Chemical rescue of I-site cleavage in living cells and in vitro discriminates between the cytomegalovirus protease, assemblin, and its precursor, pUL80a. J Biol Chem 2005; 280: 33206-12.
    • (2005) J Biol Chem , vol.280 , pp. 33206-33212
    • McCartney, S.A.1    Brignole, E.J.2    Kolegraff, K.N.3    Loveland, A.N.4    Ussin, L.M.5    Gibson, W.6
  • 130
    • 0035852857 scopus 로고    scopus 로고
    • Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II
    • Duda D, Tu C, Qian M, et al. Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II. Biochemistry 2001; 40: 1741-8.
    • (2001) Biochemistry , vol.40 , pp. 1741-1748
    • Duda, D.1    Tu, C.2    Qian, M.3
  • 131
    • 0034636838 scopus 로고    scopus 로고
    • Role of Lys100 in human dihydroorotate dehydrogenase: Mutagenesis studies and chemical rescue by external amines
    • Jiang W, Locke G, Harpel MR, Copeland RA, Marcinkeviciene J. Role of Lys100 in human dihydroorotate dehydrogenase: mutagenesis studies and chemical rescue by external amines. Biochemistry 2000; 39: 7990-7.
    • (2000) Biochemistry , vol.39 , pp. 7990-7997
    • Jiang, W.1    Locke, G.2    Harpel, M.R.3    Copeland, R.A.4    Marcinkeviciene, J.5
  • 132
    • 0037022810 scopus 로고    scopus 로고
    • Chemical rescue in catalysis by human carbonic anhydrases II and III
    • An H, Tu C, Duda D, et al. Chemical rescue in catalysis by human carbonic anhydrases II and III. Biochemistry 2002; 41: 3235-42.
    • (2002) Biochemistry , vol.41 , pp. 3235-3242
    • An, H.1    Tu, C.2    Duda, D.3
  • 135
    • 20444457978 scopus 로고    scopus 로고
    • Why enzymes are proficient catalysts: Beyond the Pauling paradigm
    • Zhang X, Houk KN. Why enzymes are proficient catalysts: beyond the Pauling paradigm. Acc Chem Res 2005; 38: 379-85.
    • (2005) Acc Chem Res , vol.38 , pp. 379-385
    • Zhang, X.1    Houk, K.N.2
  • 136
    • 0035425380 scopus 로고    scopus 로고
    • Enzyme catalysis: Removing chemically 'essential' residues by site-directed mutagenesis
    • Peracchi A. Enzyme catalysis: removing chemically 'essential' residues by site-directed mutagenesis. Trends Biochem Sci 2001; 26: 497-503.
    • (2001) Trends Biochem Sci , vol.26 , pp. 497-503
    • Peracchi, A.1
  • 139
    • 0034727638 scopus 로고    scopus 로고
    • Reviving a dead enzyme: Cytosine deaminations promoted by an inactive DNA methyltransferase and an S-adenosylmethionine analogue
    • Sharath AN, Weinhold E, Bhagwat AS. Reviving a dead enzyme: cytosine deaminations promoted by an inactive DNA methyltransferase and an S-adenosylmethionine analogue. Biochemistry 2000; 39: 14611-6.
    • (2000) Biochemistry , vol.39 , pp. 14611-14616
    • Sharath, A.N.1    Weinhold, E.2    Bhagwat, A.S.3
  • 140
  • 142
    • 0031964940 scopus 로고    scopus 로고
    • Piebaldism with deafness: Molecular evidence for an expanded syndrome
    • Spritz RA, Beighton P. Piebaldism with deafness: molecular evidence for an expanded syndrome. Am J Med Genet 1998; 75: 101-3.
    • (1998) Am J Med Genet , vol.75 , pp. 101-103
    • Spritz, R.A.1    Beighton, P.2
  • 143
    • 0028577730 scopus 로고
    • Structural basis for chromosome X-linked agammaglobulinemia: A tyrosine kinase disease
    • Vihinen M, Vetrie D, Maniar HS, et al. Structural basis for chromosome X-linked agammaglobulinemia: a tyrosine kinase disease. Proc Natl Acad Sci USA 1994; 91: 12803-7.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12803-12807
    • Vihinen, M.1    Vetrie, D.2    Maniar, H.S.3
  • 144
    • 0035925207 scopus 로고    scopus 로고
    • A subtype-selective thyromimetic designed to bind a mutant thyroid hormone receptor implicated in resistance to thyroid hormone
    • Ye HF, O'Reilly KE, Koh JT. A subtype-selective thyromimetic designed to bind a mutant thyroid hormone receptor implicated in resistance to thyroid hormone. J Am Chem Soc 2001; 123: 1521-2.
    • (2001) J Am Chem Soc , vol.123 , pp. 1521-1522
    • Ye, H.F.1    O'Reilly, K.E.2    Koh, J.T.3
  • 145
    • 18144428778 scopus 로고    scopus 로고
    • Design and synthesis of complementing ligands for mutant thyroid hormone receptor TRβ(R320H): A tailor-made approach toward the treatment of resistance to thyroid hormone
    • Hashimoto A, Shi Y, Drake K, Koh JT. Design and synthesis of complementing ligands for mutant thyroid hormone receptor TRβ(R320H): a tailor-made approach toward the treatment of resistance to thyroid hormone. Bioorg Med Chem 2005; 13: 3627-39.
    • (2005) Bioorg Med Chem , vol.13 , pp. 3627-3639
    • Hashimoto, A.1    Shi, Y.2    Drake, K.3    Koh, J.T.4
  • 146
    • 33745966042 scopus 로고    scopus 로고
    • A functionally orthogonal ligand-receptor pair created by targeting the allosteric mechanism of the thyroid hormone receptor
    • Hassan AQ, Koh JT. A functionally orthogonal ligand-receptor pair created by targeting the allosteric mechanism of the thyroid hormone receptor. J Am Chem Soc 2006; 128: 8868-74.
    • (2006) J Am Chem Soc , vol.128 , pp. 8868-8874
    • Hassan, A.Q.1    Koh, J.T.2
  • 147
    • 15444367413 scopus 로고    scopus 로고
    • Mutant-selective thyromimetics for the chemical rescue of thyroid hormone receptor mutants associated with resistance to thyroid hormone
    • Shi Y, Ye H, Link KH, et al. Mutant-selective thyromimetics for the chemical rescue of thyroid hormone receptor mutants associated with resistance to thyroid hormone. Biochemistry 2005; 44: 4612-26.
    • (2005) Biochemistry , vol.44 , pp. 4612-4626
    • Shi, Y.1    Ye, H.2    Link, K.H.3
  • 148
    • 26444485692 scopus 로고    scopus 로고
    • Primary hyperoxaluria: From gene defects to designer drugs?
    • Danpure CJ. Primary hyperoxaluria: from gene defects to designer drugs? Nephrol Dial Transplant 2005; 20: 1525-9.
    • (2005) Nephrol Dial Transplant , vol.20 , pp. 1525-1529
    • Danpure, C.J.1
  • 149
    • 0032973185 scopus 로고    scopus 로고
    • Classical galactosemia and mutations at the galactose-1-phosphate uridyl transferase (GALT) gene
    • Tyfield L, Reichardt J, Fridovich-Keil J, et al. Classical galactosemia and mutations at the galactose-1-phosphate uridyl transferase (GALT) gene. Hum Mutat 1999; 13: 417-30.
    • (1999) Hum Mutat , vol.13 , pp. 417-430
    • Tyfield, L.1    Reichardt, J.2    Fridovich-Keil, J.3
  • 151
    • 0035822113 scopus 로고    scopus 로고
    • Chemical co-substrate rescue' of phytanoyl-CoA 2-hydroxylase mutants causing Refsum's Disease
    • Mukherji M, Kershaw NJ, MacKinnon CH, et al. 'Chemical co-substrate rescue' of phytanoyl-CoA 2-hydroxylase mutants causing Refsum's Disease. Chem Commun 2001; 11: 972-3.
    • (2001) Chem Commun , vol.11 , pp. 972-973
    • Mukherji, M.1    Kershaw, N.J.2    MacKinnon, C.H.3


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