메뉴 건너뛰기




Volumn 50, Issue 43, 2011, Pages 9283-9295

A tale of two isomerases: Compact versus extended active sites in ketosteroid isomerase and phosphoglucose isomerase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CATALYTIC EFFICIENCIES; DIRECT CONTACT; ENZYME CATALYSIS; ISOMERASES; KINETIC ANALYSIS; NEAREST NEIGHBORS; PHOSPHOGLUCOSE ISOMERASE; PSEUDOMONAS PUTIDA; SINGLE-POINT MUTATION; SITE DIRECTED MUTAGENESIS; STRUCTURAL STUDIES; WILD TYPES;

EID: 80054974028     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201089v     Document Type: Article
Times cited : (32)

References (81)
  • 1
    • 0035543093 scopus 로고    scopus 로고
    • The Depth of Chemical Time and the Power of Enzymes as Catalysts
    • Wolfenden, R. and Snider, M. J. (2001) The Depth of Chemical Time and the Power of Enzymes as Catalysts Acc. Chem. Res. 34, 938-945
    • (2001) Acc. Chem. Res. , vol.34 , pp. 938-945
    • Wolfenden, R.1    Snider, M.J.2
  • 2
    • 20444457978 scopus 로고    scopus 로고
    • Why enzymes are proficient catalysts: Beyond the pauling paradigm
    • DOI 10.1021/ar040257s
    • Zhang, X. and Houk, K. N. (2005) Why Enzymes Are Proficient Catalysts: Beyond the Pauling Paradigm Acc. Chem. Res. 38, 379-385 (Pubitemid 40816649)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.5 , pp. 379-385
    • Zhang, X.1    Houk, K.N.2
  • 4
    • 0035843170 scopus 로고    scopus 로고
    • Industrial biocatalysis today and tomorrow
    • DOI 10.1038/35051736
    • Schmid, A., Dordick, J. S., Hauer, B., Kiener, A., Wubbolts, M., and Witholt, B. (2001) Industrial biocatalysis today and tomorrow Nature 409, 258-268 (Pubitemid 32144296)
    • (2001) Nature , vol.409 , Issue.6817 , pp. 258-268
    • Schmid, A.1    Dordick, J.S.2    Hauer, B.3    Kiener, A.4    Wubbolts, M.5    Witholt, B.6
  • 5
    • 45849108388 scopus 로고    scopus 로고
    • How enzymes work
    • DOI 10.1126/science.1159747
    • Ringe, D. and Petsko, G. A. (2008) How Enzymes Work Science 320, 1428-1429 (Pubitemid 351934157)
    • (2008) Science , vol.320 , Issue.5882 , pp. 1428-1429
    • Ringe, D.1    Petsko, G.A.2
  • 6
    • 0041821836 scopus 로고    scopus 로고
    • A perspective on enzyme catalysis
    • DOI 10.1126/science.1085515
    • Benkovic, S. J. and Hammes-Schiffer, S. (2003) A Perspective on Enzyme Catalysis Science 301, 1196-1202 (Pubitemid 37052200)
    • (2003) Science , vol.301 , Issue.5637 , pp. 1196-1202
    • Benkovic, S.J.1    Hammes-Schiffer, S.2
  • 8
    • 59149090849 scopus 로고    scopus 로고
    • Partial Order Optimum Likelihood (POOL): Maximum Likelihood Prediction of Protein Active Site Residues Using 3D Structure and Sequence Properties
    • Tong, W. X., Wei, Y., Murga, L. F., Ondrechen, M. J., and Williams, R. J. (2009) Partial Order Optimum Likelihood (POOL): Maximum Likelihood Prediction of Protein Active Site Residues Using 3D Structure and Sequence Properties PLoS Comput. Biol. 5, 15
    • (2009) PLoS Comput. Biol. , vol.5 , pp. 15
    • Tong, W.X.1    Wei, Y.2    Murga, L.F.3    Ondrechen, M.J.4    Williams, R.J.5
  • 10
    • 77749239790 scopus 로고    scopus 로고
    • Ketosteroid isomerase provides further support for the idea that enzymes work by electrostatic preorganization
    • Kamerlin, S. C. L., Sharma, P. K., Chu, Z. T., and Warshel, A. (2010) Ketosteroid isomerase provides further support for the idea that enzymes work by electrostatic preorganization Proc. Natl. Acad. Sci. U.S.A. 107, 4075-4080
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4075-4080
    • Kamerlin, S.C.L.1    Sharma, P.K.2    Chu, Z.T.3    Warshel, A.4
  • 11
    • 33847006589 scopus 로고    scopus 로고
    • Electrostatic Contributions to Binding of Transition State Analogues Can Be Very Different from the Corresponding Contributions to Catalysis: Phenolates Binding to the Oxyanion Hole of Ketosteroid Isomerase
    • Warshel, A., Sharma, P. K., Chu, Z. T., and Åqvist, J. (2007) Electrostatic Contributions to Binding of Transition State Analogues Can Be Very Different from the Corresponding Contributions to Catalysis: Phenolates Binding to the Oxyanion Hole of Ketosteroid Isomerase Biochemistry 46, 1466-1476
    • (2007) Biochemistry , vol.46 , pp. 1466-1476
    • Warshel, A.1    Sharma, P.K.2    Chu, Z.T.3    Åqvist, J.4
  • 12
    • 70449399334 scopus 로고    scopus 로고
    • Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics
    • Chakravorty, D. K., Soudackov, A. V., and Hammes-Schiffer, S. (2009) Hybrid Quantum/Classical Molecular Dynamics Simulations of the Proton Transfer Reactions Catalyzed by Ketosteroid Isomerase: Analysis of Hydrogen Bonding, Conformational Motions, and Electrostatics Biochemistry 48, 10608-10619
    • (2009) Biochemistry , vol.48 , pp. 10608-10619
    • Chakravorty, D.K.1    Soudackov, A.V.2    Hammes-Schiffer, S.3
  • 13
    • 33646262869 scopus 로고    scopus 로고
    • Testing electrostatic complementarity in enzyme catalysis: Hydrogen bonding in the ketosteroid isomerase oxyanion hole
    • Kraut, D. A., Sigala, P. A., Pybus, B., Liu, C. W., Ringe, D., Petsko, G. A., and Herschlag, D. (2006) Testing electrostatic complementarity in enzyme catalysis: Hydrogen bonding in the ketosteroid isomerase oxyanion hole PLoS Biol. 4, 501-519
    • (2006) PLoS Biol. , vol.4 , pp. 501-519
    • Kraut, D.A.1    Sigala, P.A.2    Pybus, B.3    Liu, C.W.4    Ringe, D.5    Petsko, G.A.6    Herschlag, D.7
  • 14
    • 65649131517 scopus 로고    scopus 로고
    • Evaluating the Potential for Halogen Bonding in the Oxyanion Hole of Ketosteroid Isomerase Using Unnatural Amino Acid Mutagenesis
    • Kraut, D. A., Churchill, M. J., Dawson, P. E., and Herschlag, D. (2009) Evaluating the Potential for Halogen Bonding in the Oxyanion Hole of Ketosteroid Isomerase Using Unnatural Amino Acid Mutagenesis ACS Chem. Biol. 4, 269-273
    • (2009) ACS Chem. Biol. , vol.4 , pp. 269-273
    • Kraut, D.A.1    Churchill, M.J.2    Dawson, P.E.3    Herschlag, D.4
  • 15
    • 76649126435 scopus 로고    scopus 로고
    • Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole
    • Kraut, D. A., Sigala, P. A., Fenn, T. D., and Herschlag, D. (2010) Dissecting the paradoxical effects of hydrogen bond mutations in the ketosteroid isomerase oxyanion hole Proc. Natl. Acad. Sci. U.S.A. 107, 1960-1965
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1960-1965
    • Kraut, D.A.1    Sigala, P.A.2    Fenn, T.D.3    Herschlag, D.4
  • 17
    • 0025115592 scopus 로고
    • Combined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction
    • Kuliopulos, A., Talalay, P., and Mildvan, A. S. (1990) Combined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction Biochemistry 29, 10271-10280 (Pubitemid 20384534)
    • (1990) Biochemistry , vol.29 , Issue.44 , pp. 10271-10280
    • Kuliopulos, A.1    Talalay, P.2    Mildvan, A.S.3
  • 19
    • 0020854456 scopus 로고
    • The degradation of cholesterol by Pseudomonas sp. NCIB 10590 under aerobic conditions
    • Owen, R. W., Mason, A. N., and Bilton, R. F. (1983) The degradation of cholesterol by Pseudomonas sp. NCIB 10590 under aerobic conditions J. Lipid Res. 24, 1500-1511
    • (1983) J. Lipid Res. , vol.24 , pp. 1500-1511
    • Owen, R.W.1    Mason, A.N.2    Bilton, R.F.3
  • 20
    • 0032499672 scopus 로고    scopus 로고
    • 5-3- ketosteroid isomerase from Pseudomonas testosteroni
    • DOI 10.1021/bi9801614
    • 5-3-Ketosteroid Isomerase from Pseudomonas testosteroni Biochemistry 37, 8325-8330 (Pubitemid 28275451)
    • (1998) Biochemistry , vol.37 , Issue.23 , pp. 8325-8330
    • Cho, H.-S.1    Choi, G.2    Choi, K.Y.3    Oh, B.-H.4
  • 22
    • 0029041240 scopus 로고
    • 5-3-ketosteroid isomerase from Pseudomonas putida biotype B
    • 5-3-ketosteroid isomerase from Pseudomonas putida biotype B J. Bacteriol. 177, 2602-2605
    • (1995) J. Bacteriol. , vol.177 , pp. 2602-2605
    • Kim, S.1    Choi, K.2
  • 23
    • 0001033697 scopus 로고    scopus 로고
    • Mutational analysis of the three cysteines and active-site aspartic acid 103 of ketosteroid isomerase from Pseudomonas putida biotype B
    • Kim, S., Joo, S., Choi, G., Cho, H., Oh, B., and Choi, K. (1997) Mutational analysis of the three cysteines and active-site aspartic acid 103 of ketosteroid isomerase from Pseudomonas putida biotype B J. Bacteriol. 179, 7742-7747 (Pubitemid 27525704)
    • (1997) Journal of Bacteriology , vol.179 , Issue.24 , pp. 7742-7747
    • Kim, S.W.1    Joo, S.2    Choi, G.3    Cho, H.-S.4    Oh, B.-H.5    Choi, K.Y.6
  • 24
    • 0040777049 scopus 로고    scopus 로고
    • Contribution of the hydrogen-bond network involving a tyro sine triad in the active site to the structure and function of a highly proficient ketosteroid isomerase from Pseudomonas putida biotype B
    • DOI 10.1021/bi992119u
    • Kim, D.-H., Jang, D. S., Nam, G. H., Choi, G., Kim, J.-S., Ha, N.-C., Kim, M.-S., Oh, B.-H., and Choi, K. Y. (2000) Contribution of the Hydrogen-Bond Network Involving a Tyrosine Triad in the Active Site to the Structure and Function of a Highly Proficient Ketosteroid Isomerase from Pseudomonas putida Biotype B Biochemistry 39, 4581-4589 (Pubitemid 30225321)
    • (2000) Biochemistry , vol.39 , Issue.16 , pp. 4581-4589
    • Kim, D.-H.1    Jang, D.S.2    Nam, G.H.3    Choi, G.4    Kim, J.-S.5    Ha, N.-C.6    Kim, M.-S.7    Oh, B.-H.8    Choi, K.Y.9
  • 26
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • DOI 10.1016/S0968-0004(98)01335-8, PII S0968000498013358
    • Jeffery, C. J. (1999) Moonlighting proteins Trends Biochem. Sci. 24, 8-11 (Pubitemid 29074455)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.1 , pp. 8-11
    • Jeffery, C.J.1
  • 27
    • 0023840114 scopus 로고
    • Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3' sequences
    • DOI 10.1038/332455a0
    • Faik, P., Walker, J. I. H., Redmill, A. A. M., and Morgan, M. J. (1988) Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3 sequences Nature 332, 455-456 (Pubitemid 18090249)
    • (1988) Nature , vol.332 , Issue.6163 , pp. 455-456
    • Faik, P.1    Walker, J.I.H.2    Redmill, A.A.M.3    Morgan, M.J.4
  • 28
    • 0023867160 scopus 로고
    • The neurotrophic factor neuroleukin is 90% homologous with phosphohexose isomerase
    • DOI 10.1038/332454a0
    • Chaput, M., Claes, V., Portetelle, D., Cludts, I., Cravador, A., Burny, A., Gras, H., and Tartar, A. (1988) The neurotrophic factor neuroleukin is 90% homologous with phosphohexose isomerase Nature 332, 454-455 (Pubitemid 18090248)
    • (1988) Nature , vol.332 , Issue.6163 , pp. 454-455
    • Chaput, M.1    Claes, V.2    Portetelle, D.3    Cludts, I.4    Cravador, A.5    Burny, A.6    Gras, H.7    Tartar, A.8
  • 29
    • 0030012538 scopus 로고    scopus 로고
    • Tumor cell autocrine motility factor is the neuroleukin/phosphohexose isomerase polypeptide
    • Watanabe, H., Takehana, K., Date, M., Shinozaki, T., and Raz, A. (1996) Tumor Cell Autocrine Motility Factor Is the Neuroleukin/Phosphohexose Isomerase Polypeptide Cancer Res. 56, 2960-2963 (Pubitemid 26199739)
    • (1996) Cancer Research , vol.56 , Issue.13 , pp. 2960-2963
    • Watanabe, H.1    Takehana, K.2    Date, M.3    Shinozaki, T.4    Raz, A.5
  • 30
    • 0029898821 scopus 로고    scopus 로고
    • The differentiation and maturation mediator for human myeloid leukemia cells shares homology with neuroleukin or phosphoglucose isomerase
    • Xu, W., Seiter, K., Feldman, E., Ahmed, T., and Chiao, J. (1996) The differentiation and maturation mediator for human myeloid leukemia cells shares homology with neuroleukin or phosphoglucose isomerase Blood 87, 4502-4506 (Pubitemid 26162355)
    • (1996) Blood , vol.87 , Issue.11 , pp. 4502-4506
    • Xu, W.1    Seiter, K.2    Feldman, E.3    Ahmed, T.4    Chiao, J.W.5
  • 31
    • 0014321644 scopus 로고
    • Hereditary Hemolytic Anemia Associated with Glucosephosphate Isomerase (GPI) Deficiency a New Enzyme Defect of Human Erythrocytes
    • Baughan, M. A., Valentine, W. N., Paglia, D. E., Ways, P. O., Simons, E. R., and Demarsh, Q. B. (1968) Hereditary Hemolytic Anemia Associated with Glucosephosphate Isomerase (GPI) Deficiency a New Enzyme Defect of Human Erythrocytes Blood 32, 236-249
    • (1968) Blood , vol.32 , pp. 236-249
    • Baughan, M.A.1    Valentine, W.N.2    Paglia, D.E.3    Ways, P.O.4    Simons, E.R.5    Demarsh, Q.B.6
  • 32
    • 0031409786 scopus 로고    scopus 로고
    • Glucosephosphate isomerase (GPI) deficiency mutations associated with hereditary nonspherocytic hemolytic anemia (HNSHA)
    • DOI 10.1006/bcmd.1997.0157
    • Beutler, E., West, C., Britton, H. A., Harris, J., and Forman, L. (1997) Glucosephosphate Isomerase (GPI) Deficiency Mutations Associated with Hereditary Nonspherocytic Hemolytic Anemia (HNSHA) Blood Cells, Mol., Dis. 23, 402-409 (Pubitemid 28123722)
    • (1997) Blood Cells, Molecules and Diseases , vol.23 , Issue.3 , pp. 402-409
    • Beutler, E.1    West, C.2    Britton, H.A.3    Harris, J.4    Forman, L.5
  • 33
    • 11244324729 scopus 로고    scopus 로고
    • Novel roles of the autocrine motility factor/phosphoglucose isomerase in tumor malignancy
    • DOI 10.1677/erc.1.00811
    • Yanagawa, T., Funasaka, T., Tsutsumi, S., Watanabe, H., and Raz, A. (2004) Novel roles of the autocrine motility factor/phosphoglucose isomerase in tumor malignancy Endocr.-Relat. Cancer 11, 749-759 (Pubitemid 40065548)
    • (2004) Endocrine-Related Cancer , vol.11 , Issue.4 , pp. 749-759
    • Yanagawa, T.1    Funasaka, T.2    Tsutsumi, S.3    Watanabe, H.4    Raz, A.5
  • 34
    • 0036397874 scopus 로고    scopus 로고
    • Conformational changes in phosphoglucose isomerase induced by ligand binding
    • DOI 10.1016/S0022-2836(02)00892-6
    • Arsenieva, D. and Jeffery, C. J. (2002) Conformational Changes in Phosphoglucose Isomerase Induced by Ligand Binding J. Mol. Biol. 323, 77-84 (Pubitemid 35168481)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.1 , pp. 77-84
    • Arsenieva, D.1    Jeffery, C.J.2
  • 35
    • 0034620506 scopus 로고    scopus 로고
    • Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator
    • DOI 10.1021/bi991604m
    • Jeffery, C. J., Bahnson, B. J., Chien, W., Ringe, D., and Petsko, G. A. (2000) Crystal Structure of Rabbit Phosphoglucose Isomerase, a Glycolytic Enzyme That Moonlights as Neuroleukin, Autocrine Motility Factor, and Differentiation Mediator Biochemistry 39, 955-964 (Pubitemid 30075322)
    • (2000) Biochemistry , vol.39 , Issue.5 , pp. 955-964
    • Jeffery, C.J.1    Bahnson, B.J.2    Chien, W.3    Ringe, D.4    Petsko, G.A.5
  • 36
    • 0035852828 scopus 로고    scopus 로고
    • Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonate identifies the role of Glu357 in catalysis
    • DOI 10.1021/bi0018483
    • Jeffery, C. J., Hardre, R., and Salmon, L. (2001) Crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho- d -arabinonate identifies the role of Glu357 in catalysis Biochemistry 40, 1560-1566 (Pubitemid 32144024)
    • (2001) Biochemistry , vol.40 , Issue.6 , pp. 1560-1566
    • Jeffery, C.J.1    Hardre, R.2    Salmon, L.3
  • 37
    • 0037348344 scopus 로고    scopus 로고
    • Structure of native phosphoglucose isomerase from rabbit: Conformational changes associated with catalytic function
    • DOI 10.1107/S0907444902023387
    • Davies, C. and Muirhead, H. (2003) Structure of native phosphoglucose isomerase from rabbit: Conformational changes associated with catalytic function Acta Crystallogr. D59, 453-465 (Pubitemid 36360417)
    • (2003) Acta Crystallographica Section D: Biological Crystallography , vol.59 , Issue.3 , pp. 453-465
    • Davies, C.1    Muirhead, H.2
  • 38
    • 0035800048 scopus 로고    scopus 로고
    • Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate
    • DOI 10.1021/bi002916o
    • Lee, J. H., Chang, K. Z., Patel, V., and Jeffery, C. J. (2001) Crystal Structure of Rabbit Phosphoglucose Isomerase Complexed with Its Substrate d -Fructose 6-Phosphate Biochemistry 40, 7799-7805 (Pubitemid 32622970)
    • (2001) Biochemistry , vol.40 , Issue.26 , pp. 7799-7805
    • Ji Hyun Lee1    Chang, K.Z.2    Patel, V.3    Jeffery, C.J.4
  • 39
    • 0035369540 scopus 로고    scopus 로고
    • The crystal structure of human phosphoglucose isomerase at 1.6 Å resolution: Implications for catalytic mechanism, cytokine activity and haemolytic anaemia
    • DOI 10.1006/jmbi.2001.4680
    • Read, J., Pearce, J., Li, X., Muirhead, H., Chirgwin, J., and Davies, C. (2001) The crystal structure of human phosphoglucose isomerase at 1.6 Å resolution: Implications for catalytic mechanism, cytokine activity and haemolytic anaemia J. Mol. Biol. 309, 447-463 (Pubitemid 32564905)
    • (2001) Journal of Molecular Biology , vol.309 , Issue.2 , pp. 447-463
    • Read, J.1    Pearce, J.2    Li, X.3    Muirhead, H.4    Chirgwin, J.5    Davies, C.6
  • 40
    • 4444298888 scopus 로고    scopus 로고
    • The crystal structure of mouse phosphoglucose isomerase at 1.6 Å resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening
    • DOI 10.1016/j.jmb.2004.07.085, PII S0022283604009258
    • Solomons, J. T. G., Zimmerly, E. M., Burns, S., Krishnamurthy, N., Swan, M. K., Krings, S., Muirhead, H., Chirgwin, J., and Davies, C. (2004) The crystal structure of mouse phosphoglucose isomerase at 1.6 Å resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening J. Mol. Biol. 342, 847-860 (Pubitemid 39165654)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.3 , pp. 847-860
    • Graham Solomons, J.T.1    Zimmerly, E.M.2    Burns, S.3    Krishnamurthy, N.4    Swan, M.K.5    Krings, S.6    Muirhead, H.7    Chirgwin, J.8    Davies, C.9
  • 41
    • 0034725594 scopus 로고    scopus 로고
    • The crystal structure of phosphoglucose isomerase/autocrine motility factor/neuroleukin complexed with its carbohydrate phosphate inhibitors suggests its substrate/receptor recognition
    • DOI 10.1074/jbc.M002017200
    • Chou, C.-C., Sun, Y.-J., Meng, M., and Hsiao, C.-D. (2000) The Crystal Structure of Phosphoglucose Isomerase/Autocrine Motility Factor/Neuroleukin Complexed with Its Carbohydrate Phosphate Inhibitors Suggests Its Substrate/Receptor Recognition J. Biol. Chem. 275, 23154-23160 (Pubitemid 30646209)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 23154-23160
    • Chou, C.-C.1    Sun, Y.-J.2    Meng, H.3    Hsiao, C.-D.4
  • 43
    • 0016602072 scopus 로고    scopus 로고
    • Mechanism of the Aldose-Ketose Isomerase Reactions
    • John Wiley & Sons, Inc. New York.
    • Rose, I. A. (2006) Mechanism of the Aldose-Ketose Isomerase Reactions. In Advances in Enzymology and Related Areas of Molecular Biology, pp 491-517, John Wiley & Sons, Inc., New York.
    • (2006) Advances in Enzymology and Related Areas of Molecular Biology , pp. 491-517
    • Rose, I.A.1
  • 45
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA - A self-parameterizing force field
    • DOI 10.1002/prot.10104
    • Krieger, E., Koraimann, G., and Vriend, G. (2002) Increasing the precision of comparative models with YASARA NOVA: A self-parameterizing force field Proteins: Struct., Funct., Genet. 47, 393-402 (Pubitemid 34438688)
    • (2002) Proteins: Structure, Function and Genetics , vol.47 , Issue.3 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 46
    • 34250671141 scopus 로고    scopus 로고
    • Selective prediction of interaction sites in protein structures with THEMATICS
    • Wei, Y., Ko, J., Murga, L. F., and Ondrechen, M. J. (2007) Selective prediction of interaction sites in protein structures with THEMATICS BMC Bioinf. 8, 15
    • (2007) BMC Bioinf. , vol.8 , pp. 15
    • Wei, Y.1    Ko, J.2    Murga, L.F.3    Ondrechen, M.J.4
  • 47
    • 67849101184 scopus 로고    scopus 로고
    • INTREPID: A web server for prediction of functionally important residues by evolutionary analysis
    • Sankararaman, S., Kolaczkowski, B., and Sjolander, K. (2009) INTREPID: A web server for prediction of functionally important residues by evolutionary analysis Nucleic Acids Res. 37, W390-W395
    • (2009) Nucleic Acids Res. , vol.37
    • Sankararaman, S.1    Kolaczkowski, B.2    Sjolander, K.3
  • 48
    • 80051764768 scopus 로고    scopus 로고
    • High-performance prediction of functional residues in proteins with machine learning and computed input features
    • Somarowthu, S., Yang, H., Hildebrand, D. G. C., and Ondrechen, M. J. (2011) High-performance prediction of functional residues in proteins with machine learning and computed input features Biopolymers 95, 390-400
    • (2011) Biopolymers , vol.95 , pp. 390-400
    • Somarowthu, S.1    Yang, H.2    Hildebrand, D.G.C.3    Ondrechen, M.J.4
  • 49
    • 13044272912 scopus 로고    scopus 로고
    • Automated analysis of interatomic contacts in proteins
    • DOI 10.1093/bioinformatics/15.4.327
    • Sobolev, V., Sorokine, A., Prilusky, J., Abola, E., and Edelman, M. (1999) Automated analysis of interatomic contacts in proteins Bioinformatics 15, 327-332 (Pubitemid 29213759)
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 327-332
    • Sobolev, V.1    Sorokine, A.2    Prilusky, J.3    Abola, E.E.4    Edelman, M.5
  • 51
    • 62749167980 scopus 로고    scopus 로고
    • MCCE2: Improving protein p K a calculations with extensive side chain rotamer sampling
    • Song, Y., Mao, J., and Gunner, M. R. (2009) MCCE2: Improving protein p K a calculations with extensive side chain rotamer sampling J. Comput. Chem. 30, 2231-2247
    • (2009) J. Comput. Chem. , vol.30 , pp. 2231-2247
    • Song, Y.1    Mao, J.2    Gunner, M.R.3
  • 53
    • 0027477251 scopus 로고
    • Multiple-site titration and molecular modeling: Two rapid methods for computing energies and forces for ionizable groups in proteins
    • Gilson, M. K. (1993) Multiple-site titration and molecular modeling: Two rapid methods for computing energies and forces for ionizable groups in proteins Proteins: Struct., Funct., Genet. 15, 266-282 (Pubitemid 23079293)
    • (1993) Proteins: Structure, Function and Genetics , vol.15 , Issue.3 , pp. 266-282
    • Gilson, M.K.1
  • 54
    • 58149193188 scopus 로고    scopus 로고
    • Effects of inherited mutations on catalytic activity and structural stability of human glucose-6-phosphate isomerase expressed in Escherichia coli
    • Lin, H. Y., Kao, Y. H., Chen, S. T., and Meng, M. (2009) Effects of inherited mutations on catalytic activity and structural stability of human glucose-6-phosphate isomerase expressed in Escherichia coli Biochim. Biophys. Acta 1794, 315-323
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 315-323
    • Lin, H.Y.1    Kao, Y.H.2    Chen, S.T.3    Meng, M.4
  • 57
    • 79952780138 scopus 로고    scopus 로고
    • The Dimeric SOS Mutagenesis Protein UmuD Is Active as a Monomer
    • Ollivierre, J. N., Sikora, J. L., and Beuning, P. J. (2011) The Dimeric SOS Mutagenesis Protein UmuD Is Active as a Monomer J. Biol. Chem. 286, 3607-3617
    • (2011) J. Biol. Chem. , vol.286 , pp. 3607-3617
    • Ollivierre, J.N.1    Sikora, J.L.2    Beuning, P.J.3
  • 58
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • DOI 10.1016/j.ab.2006.07.027, PII S0003269706005355
    • Ericsson, U. B., Hallberg, B. M., DeTitta, G. T., Dekker, N., and Nordlund, P. (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies Anal. Biochem. 357, 289-298 (Pubitemid 44430091)
    • (2006) Analytical Biochemistry , vol.357 , Issue.2 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    DeTitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 59
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 62
    • 0035856578 scopus 로고    scopus 로고
    • Maintenance of α-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B
    • Nam, G. H., Jang, D. S., Cha, S. S., Lee, T. H., Kim, D. H., Hong, B. H., Yun, Y. S., Oh, B. H., and Choi, K. Y. (2001) Maintenance of α-helical structures by phenyl rings in the active-site tyrosine triad contributes to catalysis and stability of ketosteroid isomerase from Pseudomonas putida biotype B Biochemistry 40, 13529-13537
    • (2001) Biochemistry , vol.40 , pp. 13529-13537
    • Nam, G.H.1    Jang, D.S.2    Cha, S.S.3    Lee, T.H.4    Kim, D.H.5    Hong, B.H.6    Yun, Y.S.7    Oh, B.H.8    Choi, K.Y.9
  • 64
    • 0000243829 scopus 로고
    • Procheck: A Program to Check the Stereochemical Quality of Protein Structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) Procheck: A Program to Check the Stereochemical Quality of Protein Structures J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 65
    • 0028948565 scopus 로고
    • Radiation Damage in Protein Crystallography
    • Nave, C. (1995) Radiation Damage in Protein Crystallography Radiat. Phys. Chem. 45, 483-490
    • (1995) Radiat. Phys. Chem. , vol.45 , pp. 483-490
    • Nave, C.1
  • 66
    • 0032699223 scopus 로고    scopus 로고
    • Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N- bromoacetylethanolamine phosphate
    • Meng, M., Chane, T.-L., Sun, Y.-J., and Hsiao, C.-D. (1999) Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate Protein Sci. 8, 2438-2443 (Pubitemid 29536410)
    • (1999) Protein Science , vol.8 , Issue.11 , pp. 2438-2443
    • Meng, M.1    Chane, T.-L.2    Sun, Y.-J.3    Hsiao, C.-D.4
  • 68
    • 0000421878 scopus 로고
    • Nature of Forces between Large Molecules of Biological Interest
    • Pauling, L. (1948) Nature of Forces between Large Molecules of Biological Interest Nature 161, 707-709
    • (1948) Nature , vol.161 , pp. 707-709
    • Pauling, L.1
  • 69
    • 0032538627 scopus 로고    scopus 로고
    • Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites
    • DOI 10.1074/jbc.273.42.27035
    • Warshel, A. (1998) Electrostatic Origin of the Catalytic Power of Enzymes and the Role of Preorganized Active Sites J. Biol. Chem. 273, 27035-27038 (Pubitemid 28500403)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27035-27038
    • Warshel, A.1
  • 70
    • 0032475836 scopus 로고    scopus 로고
    • The low barrier hydrogen bond in enzymatic catalysis
    • DOI 10.1074/jbc.273.40.25529
    • Cleland, W. W., Frey, P. A., and Gerlt, J. A. (1998) The Low Barrier Hydrogen Bond in Enzymatic Catalysis J. Biol. Chem. 273, 25529-25532 (Pubitemid 28475766)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25529-25532
    • Cleland, W.W.1    Frey, P.A.2    Gerlt, J.A.3
  • 71
    • 0036009145 scopus 로고    scopus 로고
    • A View at the Millennium: The Efficiency of Enzymatic Catalysis
    • Bruice, T. C. (2002) A View at the Millennium: The Efficiency of Enzymatic Catalysis Acc. Chem. Res. 35, 139-148
    • (2002) Acc. Chem. Res. , vol.35 , pp. 139-148
    • Bruice, T.C.1
  • 73
    • 0024573393 scopus 로고
    • Hydrogen tunneling in enzyme reactions
    • Cha, Y., Murray, C., and Klinman, J. (1989) Hydrogen tunneling in enzyme reactions Science 243, 1325-1330 (Pubitemid 19085368)
    • (1989) Science , vol.243 , Issue.4896 , pp. 1325-1330
    • Cha, Y.1    Murray, C.J.2    Klinman, J.P.3
  • 76
    • 0030002507 scopus 로고    scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase: Structure and mechanistic properties of the D270N mutant
    • DOI 10.1021/bi960174m
    • Schafer, S. L., Barrett, W. C., Kallarakal, A. T., Mitra, B., Kozarich, J. W., Gerlt, J. A., Clifton, J. G., Petsko, G. A., and Kenyon, G. L. (1996) Mechanism of the Reaction Catalyzed by Mandelate Racemase: Structure and Mechanistic Properties of the D270N Mutant Biochemistry 35, 5662-5669 (Pubitemid 26143661)
    • (1996) Biochemistry , vol.35 , Issue.18 , pp. 5662-5669
    • Schafer, S.L.1    Barrett, W.C.2    Kallarakal, A.T.3    Mitra, B.4    Kozarich, J.W.5    Gerlt, J.A.6    Clifton, J.G.7    Petsko, G.A.8    Kenyon, G.L.9
  • 77
    • 0026779802 scopus 로고
    • Segmental movement: Definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase
    • Sampson, N. S. and Knowles, J. R. (1992) Segmental movement: Definition of the structural requirements for loop closure in catalysis by triosephosphate isomerase Biochemistry 31, 8482-8487
    • (1992) Biochemistry , vol.31 , pp. 8482-8487
    • Sampson, N.S.1    Knowles, J.R.2
  • 78
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better?
    • DOI 10.1016/j.tibtech.2005.03.005
    • Morley, K. L. and Kazlauskas, R. J. (2005) Improving enzyme properties: When are closer mutations better? Trends Biotechnol. 23, 231-237 (Pubitemid 40615535)
    • (2005) Trends in Biotechnology , vol.23 , Issue.5 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 80
    • 33745830892 scopus 로고    scopus 로고
    • Role of invariant Thr80 in human immunodeficiency virus type 1 protease structure, function, and viral infectivity
    • DOI 10.1128/JVI.01900-05
    • Foulkes, J. E., Prabu-Jeyabalan, M., Cooper, D., Henderson, G. J., Harris, J., Swanstrom, R., and Schiffer, C. A. (2006) Role of Invariant Thr80 in Human Immunodeficiency Virus Type 1 Protease Structure, Function, and Viral Infectivity J. Virol. 80, 6906-6916 (Pubitemid 44026424)
    • (2006) Journal of Virology , vol.80 , Issue.14 , pp. 6906-6916
    • Foulkes, J.E.1    Prabu-Jeyabalan, M.2    Cooper, D.3    Henderson, G.J.4    Harris, J.5    Swanstrom, R.6    Schiffer, C.A.7
  • 81
    • 79958071654 scopus 로고    scopus 로고
    • X-ray solution scattering studies of the structural diversity intrinsic to protein ensembles
    • Makowski, L., Gore, D., Mandava, S., Minh, D., Park, S., Rodi, D. J., and Fischetti, R. F. (2011) X-ray solution scattering studies of the structural diversity intrinsic to protein ensembles Biopolymers 95, 531-542
    • (2011) Biopolymers , vol.95 , pp. 531-542
    • Makowski, L.1    Gore, D.2    Mandava, S.3    Minh, D.4    Park, S.5    Rodi, D.J.6    Fischetti, R.F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.