메뉴 건너뛰기




Volumn 7, Issue 2, 2003, Pages 252-264

Evolution of function in (β/α)8-barrel enzymes

Author keywords

[No Author keywords available]

Indexed keywords

3 METHYLASPARTATE AMMONIA LYASE; AMIDASE; AMMONIA LYASE; BARREL ENZYME; CARBOXYLYASE; CYTOSINE DEAMINASE; DEXTRO GALACTONATE DEHYDRATASE; DEXTRO GLUCARATE DEHYDRATASE; DEXTRO RIBULOSE 5 PHOSPHATE 3 EPIMERASE; DIHYDROOROTASE; DIHYDROPYRIMIDINASE; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; HISTIDINE; HYDROLYASE; IMIDAZOLE GLYCEROLPHOSPHATE SYNTHASE; INDOLE 3 GLYCEROL PHOSPHATE SYNTHASE; ISOENZYME; N (5' PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; NEURAMINATE PHOSPHATE SYNTHASE; NEURAMINIC ACID DERIVATIVE; PENTOSE PHOSPHATE; PHOSPHORIBOSYLFORMIMINO 5 AMINOIMIDAZOLE CARBOXAMIDE RIBONUCLEOTIDE SYNTHASE; PHOSPHOTRIESTERASE; PORPHOBILINOGEN SYNTHASE; PYRIMIDINE NUCLEOTIDE; RHAMNONATE DEHYDRATASE; SACCHARIC ACID; TRYPTOPHAN SYNTHASE; UNCLASSIFIED DRUG; UREASE;

EID: 0037396345     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(03)00019-X     Document Type: Review
Times cited : (133)

References (52)
  • 2
    • 0035896377 scopus 로고    scopus 로고
    • The TIM-barrel fold: A versatile framework for efficient enzymes
    • Wierenga R.K. The TIM-barrel fold: a versatile framework for efficient enzymes. FEBS Lett. 492:2001;193-198.
    • (2001) FEBS Lett. , vol.492 , pp. 193-198
    • Wierenga, R.K.1
  • 3
    • 0030667789 scopus 로고    scopus 로고
    • Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities
    • Babbitt P.C., Gerlt J.A. Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities. J. Biol. Chem. 272:1997;30591-30594.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30591-30594
    • Babbitt, P.C.1    Gerlt, J.A.2
  • 5
    • 0034601917 scopus 로고    scopus 로고
    • 8 barrels: Implications for the evolution of metabolic pathways
    • 8 barrels: implications for the evolution of metabolic pathways. J. Mol. Biol. 303:2000;627-641.
    • (2000) J. Mol. Biol. , vol.303 , pp. 627-641
    • Copley, R.R.1    Bork, P.2
  • 8
    • 0027964654 scopus 로고
    • 2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution
    • 2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution. Biochemistry. 33:1994;9333-9342.
    • (1994) Biochemistry , vol.33 , pp. 9333-9342
    • Wedekind, J.E.1    Poyner, R.R.2    Reed, G.H.3    Rayment, I.4
  • 9
    • 0031568330 scopus 로고    scopus 로고
    • A new function for a common fold: The crystal structure of quinolinic acid phosphoribosyltransferase
    • Eads J.C., Ozturk D., Wexler T.B., Grubmeyer C., Sacchettini J.C. A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase. Structure. 5:1997;47-58.
    • (1997) Structure , vol.5 , pp. 47-58
    • Eads, J.C.1    Ozturk, D.2    Wexler, T.B.3    Grubmeyer, C.4    Sacchettini, J.C.5
  • 10
    • 0037116603 scopus 로고    scopus 로고
    • A common evolutionary origin of two elementary enzyme folds
    • Hocker B., Schmidt S., Sterner R. A common evolutionary origin of two elementary enzyme folds. FEBS Lett. 510:2002;133-135.
    • (2002) FEBS Lett. , vol.510 , pp. 133-135
    • Hocker, B.1    Schmidt, S.2    Sterner, R.3
  • 11
    • 0033528659 scopus 로고    scopus 로고
    • Unexpected divergence of enzyme function and sequence: "N-acylamino acid racemase" is o-succinylbenzoate synthase
    • Palmer D.R., Garrett J.B., Sharma V., Meganathan R., Babbitt P.C., Gerlt J.A. Unexpected divergence of enzyme function and sequence: "N-acylamino acid racemase" is o-succinylbenzoate synthase. Biochemistry. 38:1999;4252-4258.
    • (1999) Biochemistry , vol.38 , pp. 4252-4258
    • Palmer, D.R.1    Garrett, J.B.2    Sharma, V.3    Meganathan, R.4    Babbitt, P.C.5    Gerlt, J.A.6
  • 12
    • 0037177237 scopus 로고    scopus 로고
    • Homologous (beta/alpha)8-barrel enzymes that catalyze unrelated reactions: Orotidine 5′-monophosphate decarboxylase and 3-keto-L-gulonate 6-phosphate decarboxylase
    • 2+-dependent reaction that stabilizes an enediolate anion intermediate.
    • (2002) Biochemistry , vol.41 , pp. 3861-3869
    • Wise, E.1    Yew, W.S.2    Babbitt, P.C.3    Gerlt, J.A.4    Rayment, I.5
  • 13
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies
    • Gerlt J.A., Babbitt P.C. Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies. Annu. Rev. Biochem. 70:2001;209-246.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 15
    • 0035951059 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: Functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases
    • Schmidt D.M., Hubbard B.K., Gerlt J.A. Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases. Biochemistry. 40:2001;15707-15715.
    • (2001) Biochemistry , vol.40 , pp. 15707-15715
    • Schmidt, D.M.1    Hubbard, B.K.2    Gerlt, J.A.3
  • 16
    • 0035951075 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: Crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis
    • Gulick A.M., Schmidt D.M., Gerlt J.A., Rayment I. Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis. Biochemistry. 40:2001;15716-15724.
    • (2001) Biochemistry , vol.40 , pp. 15716-15724
    • Gulick, A.M.1    Schmidt, D.M.2    Gerlt, J.A.3    Rayment, I.4
  • 17
    • 0033549133 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: Identification of a "new" general acid catalyst in the active site of D-galactonate dehydratase from Escherichia coli
    • Wieczorek S.W., Kalivoda K.A., Clifton J.G., Ringe D., Petsko G.A., Gerlt J.A. Evolution of enzymatic activities in the enolase superfamily: identification of a "new" general acid catalyst in the active site of D-galactonate dehydratase from Escherichia coli. J. Am. Chem. Soc. 121:1999;4540-4541.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4540-4541
    • Wieczorek, S.W.1    Kalivoda, K.A.2    Clifton, J.G.3    Ringe, D.4    Petsko, G.A.5    Gerlt, J.A.6
  • 18
    • 0034712668 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: Crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli
    • Gulick A.M., Hubbard B.K., Gerlt J.A., Rayment I. Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli. Biochemistry. 39:2000;4590-4602.
    • (2000) Biochemistry , vol.39 , pp. 4590-4602
    • Gulick, A.M.1    Hubbard, B.K.2    Gerlt, J.A.3    Rayment, I.4
  • 19
    • 0035964183 scopus 로고    scopus 로고
    • Evolution of enzymatic activities in the enolase superfamily: Identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli
    • Gulick A.M., Hubbard B.K., Gerlt J.A., Rayment I. Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli. Biochemistry. 40:2001;10054-10062.
    • (2001) Biochemistry , vol.40 , pp. 10054-10062
    • Gulick, A.M.1    Hubbard, B.K.2    Gerlt, J.A.3    Rayment, I.4
  • 20
    • 0037040988 scopus 로고    scopus 로고
    • The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step
    • Asuncion M., Blankenfeldt W., Barlow J.N., Gani D., Naismith J.H. The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. J. Biol. Chem. 277:2002;8306-8311.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8306-8311
    • Asuncion, M.1    Blankenfeldt, W.2    Barlow, J.N.3    Gani, D.4    Naismith, J.H.5
  • 21
  • 22
    • 0031000649 scopus 로고    scopus 로고
    • An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
    • Holm L., Sander C. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins. 28:1997;72-82.
    • (1997) Proteins , vol.28 , pp. 72-82
    • Holm, L.1    Sander, C.2
  • 23
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: A paradigm for catalysis through the use of a binuclear metal center
    • Thoden J.B., Phillips G.N. Jr., Neal T.M., Raushel F.M., Holden H.M. Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry. 40:2001;6989-6997. • The structure of DHO was determined in the presence of substrate and product to a resolution of 1.7 Å where dihydroorotate was bound to one subunit and carbamoyl aspartate was bound to the other subunit within a single dimeric species. This has provided an unprecedented view of the molecular interactions between substrate and product with the enzyme before and after the chemical transformation.
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips G.N., Jr.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 24
    • 0034720769 scopus 로고    scopus 로고
    • Self-assembly of the binuclear metal center of phosphotriesterase
    • Shim H., Raushel F.M. Self-assembly of the binuclear metal center of phosphotriesterase. Biochemistry. 39:2000;7357-7364.
    • (2000) Biochemistry , vol.39 , pp. 7357-7364
    • Shim, H.1    Raushel, F.M.2
  • 25
    • 0032515956 scopus 로고    scopus 로고
    • Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family
    • Buchbinder J.L., Stephenson R.C., Dresser M.J., Pitera J.W., Scanlan T.S., Fletterick R.J. Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family. Biochemistry. 37:1998;5096-5106.
    • (1998) Biochemistry , vol.37 , pp. 5096-5106
    • Buchbinder, J.L.1    Stephenson, R.C.2    Dresser, M.J.3    Pitera, J.W.4    Scanlan, T.S.5    Fletterick, R.J.6
  • 27
    • 0036382767 scopus 로고    scopus 로고
    • Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis
    • Nitanai Y., Satow Y., Adachi H., Tsujimoto M. Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis. J. Mol. Biol. 321:2002;177-184.
    • (2002) J. Mol. Biol. , vol.321 , pp. 177-184
    • Nitanai, Y.1    Satow, Y.2    Adachi, H.3    Tsujimoto, M.4
  • 28
    • 0001849211 scopus 로고    scopus 로고
    • 70 years of crystalline urease: What have we learned?
    • Karplus P.A., Pearson M.A., Hausinger R.P. 70 years of crystalline urease: what have we learned? Acc. Chem. Res. 30:1997;330-337.
    • (1997) Acc. Chem. Res. , vol.30 , pp. 330-337
    • Karplus, P.A.1    Pearson, M.A.2    Hausinger, R.P.3
  • 29
    • 0035814923 scopus 로고    scopus 로고
    • High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta
    • Benning M.M., Shim H., Raushel F.M., Holden H.M. High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta. Biochemistry. 40:2001;2712-2722.
    • (2001) Biochemistry , vol.40 , pp. 2712-2722
    • Benning, M.M.1    Shim, H.2    Raushel, F.M.3    Holden, H.M.4
  • 30
    • 0036136174 scopus 로고    scopus 로고
    • Utilization of L-ascorbate by Escherichia coli K-12: Assignments of functions to products of the yjf-sga and yia-sgb operons
    • Yew W.S., Gerlt J.A. Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons. J. Bacteriol. 184:2002;302-306.
    • (2002) J. Bacteriol. , vol.184 , pp. 302-306
    • Yew, W.S.1    Gerlt, J.A.2
  • 31
    • 0033588155 scopus 로고    scopus 로고
    • Activity of yeast orotidine-5′-phosphate decarboxylase in the absence of metals
    • Miller B.G., Smiley J.A., Short S.A., Wolfenden R. Activity of yeast orotidine-5′-phosphate decarboxylase in the absence of metals. J. Biol. Chem. 274:1999;23841-23843.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23841-23843
    • Miller, B.G.1    Smiley, J.A.2    Short, S.A.3    Wolfenden, R.4
  • 32
    • 0017086956 scopus 로고
    • Purification and properties of 3-hexulosephosphate synthase from Methylomonas M 15
    • Sahm H., Schutte H., Kula M.R. Purification and properties of 3-hexulosephosphate synthase from Methylomonas M 15. Eur. J. Biochem. 66:1976;591-596.
    • (1976) Eur. J. Biochem. , vol.66 , pp. 591-596
    • Sahm, H.1    Schutte, H.2    Kula, M.R.3
  • 33
    • 0034681950 scopus 로고    scopus 로고
    • Structural basis for the catalytic mechanism of a proficient enzyme: Orotidine 5′-monophosphate decarboxylase
    • Harris P., Navarro Poulsen J.C., Jensen K.F., Larsen S. Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5′-monophosphate decarboxylase. Biochemistry. 39:2000;4217-4224.
    • (2000) Biochemistry , vol.39 , pp. 4217-4224
    • Harris, P.1    Navarro Poulsen, J.C.2    Jensen, K.F.3    Larsen, S.4
  • 34
  • 35
    • 0034102419 scopus 로고    scopus 로고
    • Electrostatic stress in catalysis: Structure and mechanism of the enzyme orotidine monophosphate decarboxylase
    • Wu N., Mo Y., Gao J., Pai E.F. Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase. Proc. Natl. Acad. Sci. U.S.A. 97:2000;2017-2022.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2017-2022
    • Wu, N.1    Mo, Y.2    Gao, J.3    Pai, E.F.4
  • 36
    • 0034104285 scopus 로고    scopus 로고
    • Anatomy of a proficient enzyme: The structure of orotidine 5′- monophosphate decarboxylase in the presence and absence of a potential transition state analog
    • Miller B.G., Hassell A.M., Wolfenden R., Milburn M.V., Short S.A. Anatomy of a proficient enzyme: the structure of orotidine 5′- monophosphate decarboxylase in the presence and absence of a potential transition state analog. Proc. Natl. Acad. Sci. U.S.A. 97:2000;2011-2016.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2011-2016
    • Miller, B.G.1    Hassell, A.M.2    Wolfenden, R.3    Milburn, M.V.4    Short, S.A.5
  • 37
    • 0032160488 scopus 로고    scopus 로고
    • D-Ribulose-5-phosphate 3-epimerase: Cloning and heterologous expression of the spinach gene, and purification and characterization of the recombinant enzyme
    • Chen Y.R., Hartman F.C., Lu T.Y., Larimer F.W. D-Ribulose-5-phosphate 3-epimerase: cloning and heterologous expression of the spinach gene, and purification and characterization of the recombinant enzyme. Plant Physiol. 118:1998;199-207.
    • (1998) Plant Physiol. , vol.118 , pp. 199-207
    • Chen, Y.R.1    Hartman, F.C.2    Lu, T.Y.3    Larimer, F.W.4
  • 38
    • 0033537899 scopus 로고    scopus 로고
    • Structure and mechanism of the amphibolic enzyme D-ribulose-5-phosphate 3-epimerase from potato chloroplasts
    • Kopp J., Kopriva S., Suss K.H., Schulz G.E. Structure and mechanism of the amphibolic enzyme D-ribulose-5-phosphate 3-epimerase from potato chloroplasts. J. Mol. Biol. 287:1999;761-771.
    • (1999) J. Mol. Biol. , vol.287 , pp. 761-771
    • Kopp, J.1    Kopriva, S.2    Suss, K.H.3    Schulz, G.E.4
  • 40
    • 0034636974 scopus 로고    scopus 로고
    • Structure of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: Comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis
    • Wagner T., Shumilin I.A., Bauerle R., Kretsinger R.H. Structure of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli: comparison of the Mn(2+)*2-phosphoglycolate and the Pb(2+)*2-phosphoenolpyruvate complexes and implications for catalysis. J. Mol. Biol. 301:2000;389-399.
    • (2000) J. Mol. Biol. , vol.301 , pp. 389-399
    • Wagner, T.1    Shumilin, I.A.2    Bauerle, R.3    Kretsinger, R.H.4
  • 41
    • 0034737424 scopus 로고    scopus 로고
    • Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthase
    • Radaev S., Dastidar P., Patel M., Woodard R.W., Gatti D.L. Structure and mechanism of 3-deoxy-D-manno-octulosonate 8-phosphate synthase. J. Biol. Chem. 275:2000;9476-9484.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9476-9484
    • Radaev, S.1    Dastidar, P.2    Patel, M.3    Woodard, R.W.4    Gatti, D.L.5
  • 43
    • 0034628501 scopus 로고    scopus 로고
    • Directed evolution of new catalytic activity using the α/β-barrel scaffold
    • Altamirano M.M., Blackburn J.M., Aguayo C., Fersht A.R. Directed evolution of new catalytic activity using the α/β-barrel scaffold. Nature. 403:2000;617-622.
    • (2000) Nature , vol.403 , pp. 617-622
    • Altamirano, M.M.1    Blackburn, J.M.2    Aguayo, C.3    Fersht, A.R.4
  • 44
    • 0037161739 scopus 로고    scopus 로고
    • Retraction. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold
    • Altamirano M.M., Blackburn J.M., Aguayo C., Fersht A.R. Retraction. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold. Nature. 417:2002;468.
    • (2002) Nature , vol.417 , pp. 468
    • Altamirano, M.M.1    Blackburn, J.M.2    Aguayo, C.3    Fersht, A.R.4
  • 45
    • 0034730195 scopus 로고    scopus 로고
    • Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways
    • Jurgens C., Strom A., Wegener D., Hettwer S., Wilmanns M., Sterner R. Directed evolution of a (beta alpha)8-barrel enzyme to catalyze related reactions in two different metabolic pathways. Proc. Natl. Acad. Sci. U.S.A. 97:2000;9925-9930. • A single mutation at the end of the fifth β-strand in HisA alters the substrate specificity so that this enzyme that catalyzes the Amadori reaction in histidine biosynthesis can catalyse the analogous Amadori reaction catalyzed by PRAI in tryptophan biosynthesis.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9925-9930
    • Jurgens, C.1    Strom, A.2    Wegener, D.3    Hettwer, S.4    Wilmanns, M.5    Sterner, R.6
  • 46
    • 0035814818 scopus 로고    scopus 로고
    • Structural determinants of the substrate and stereochemical specificity of phosphotriesterase
    • Chen-Goodspeed M., Sogorb M.A., Wu F., Hong S.B., Raushel F.M. Structural determinants of the substrate and stereochemical specificity of phosphotriesterase. Biochemistry. 40:2001;1325-1331.
    • (2001) Biochemistry , vol.40 , pp. 1325-1331
    • Chen-Goodspeed, M.1    Sogorb, M.A.2    Wu, F.3    Hong, S.B.4    Raushel, F.M.5
  • 47
    • 0035814812 scopus 로고    scopus 로고
    • Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues
    • Chen-Goodspeed M., Sogorb M.A., Wu F., Raushel F.M. Enhancement, relaxation, and reversal of the stereoselectivity for phosphotriesterase by rational evolution of active site residues. Biochemistry. 40:2001;1332-1339. • The substrate binding pockets for PTE were manipulated in a rational manner to alter the stereoselectivity. With only 4-5 amino acid changes within the active site, the stereoselectivity of the wild-type enzyme can be manipulated a factor of one-million-fold.
    • (2001) Biochemistry , vol.40 , pp. 1332-1339
    • Chen-Goodspeed, M.1    Sogorb, M.A.2    Wu, F.3    Raushel, F.M.4
  • 48
    • 0036208056 scopus 로고    scopus 로고
    • Bacterial cell surface display of organophosphorus hydrolase for selective screening of improved hydrolysis of organophosphate nerve agents
    • Cho C.M., Mulchandani A., Chen W. Bacterial cell surface display of organophosphorus hydrolase for selective screening of improved hydrolysis of organophosphate nerve agents. Appl. Environ. Microbiol. 68:2002;2026-2030.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2026-2030
    • Cho, C.M.1    Mulchandani, A.2    Chen, W.3
  • 49
    • 0034833072 scopus 로고    scopus 로고
    • Novel enzyme activities and functional plasticity revealed by recombining highly homologous enzymes
    • Raillard S., Krebber A., Chen Y., Ness J.E., Bermudez E., Trinidad R., Fullem R., Davis C., Welch M., Seffernick J.et al. Novel enzyme activities and functional plasticity revealed by recombining highly homologous enzymes. Chem. Biol. 8:2001;891-898. • The paper is an outstanding example for the creation of novel enzyme activities through gene shuffling methodology and characterization of substrate profiles with a small compound library.
    • (2001) Chem. Biol. , vol.8 , pp. 891-898
    • Raillard, S.1    Krebber, A.2    Chen, Y.3    Ness, J.E.4    Bermudez, E.5    Trinidad, R.6    Fullem, R.7    Davis, C.8    Welch, M.9    Seffernick, J.10
  • 50
    • 0034059496 scopus 로고    scopus 로고
    • Inverting enantioselectivity by directed evolution of hydantoinase for improved production of L-methionine
    • May O., Nguyen P.T., Arnold F.H. Inverting enantioselectivity by directed evolution of hydantoinase for improved production of L-methionine. Nat. Biotechnol. 18:2000;317-320.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 317-320
    • May, O.1    Nguyen, P.T.2    Arnold, F.H.3
  • 51
    • 0033768504 scopus 로고    scopus 로고
    • Directed evolution of D-2-keto-3-deoxy-6-phosphogluconate aldolase to new variants for the efficient synthesis of D- and L-sugars
    • Fong S., Machajewski T.D., Mak C.C., Wong C. Directed evolution of D-2-keto-3-deoxy-6-phosphogluconate aldolase to new variants for the efficient synthesis of D- and L-sugars. Chem. Biol. 7:2000;873-883.
    • (2000) Chem. Biol. , vol.7 , pp. 873-883
    • Fong, S.1    Machajewski, T.D.2    Mak, C.C.3    Wong, C.4
  • 52
    • 0035148643 scopus 로고    scopus 로고
    • Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli
    • Wymer N., Buchanan L.V., Henderson D., Mehta N., Botting C.H., Pocivavsek L., Fierke C.A., Toone E.J., Naismith J.H. Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli. Structure. 9:2001;1-9. • The position of the active site lysine residue in the class I KGPD aldolase was moved from the sixth to the seventh β-strand to give a mutant with enhanced substrate specificity.
    • (2001) Structure , vol.9 , pp. 1-9
    • Wymer, N.1    Buchanan, L.V.2    Henderson, D.3    Mehta, N.4    Botting, C.H.5    Pocivavsek, L.6    Fierke, C.A.7    Toone, E.J.8    Naismith, J.H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.