메뉴 건너뛰기




Volumn 40, Issue 4, 2007, Pages 569-577

Cloning, DNA shuffling and expression of serine hydroxymethyltransferase gene from Escherichia coli strain AB90054

Author keywords

Directed evolution; DNA shuffling; Protein engineering; Serine hydroxymethyltransferase

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; DNA; ENZYMES; ESCHERICHIA COLI; PROTEINS;

EID: 33847293684     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.05.018     Document Type: Article
Times cited : (22)

References (48)
  • 3
    • 0012996147 scopus 로고
    • The biochemistry of folic acid and related pteridines
    • Blakeley R.L. The biochemistry of folic acid and related pteridines. Front Biol 13 (1969) 189-218
    • (1969) Front Biol , vol.13 , pp. 189-218
    • Blakeley, R.L.1
  • 4
    • 0015935223 scopus 로고
    • Rat liver aminomalonate decarboxylase. Identity with cytoplasmic serine hydroxymethylase and allothreonine aldolase
    • Palekar A.G., Tate S.S., and Meister A. Rat liver aminomalonate decarboxylase. Identity with cytoplasmic serine hydroxymethylase and allothreonine aldolase. J Biol Chem 248 (1973) 1158-1167
    • (1973) J Biol Chem , vol.248 , pp. 1158-1167
    • Palekar, A.G.1    Tate, S.S.2    Meister, A.3
  • 5
    • 0019493184 scopus 로고
    • The role of serine hydroxymethyltransferase in cell proliferation: DNA synthesis from serine following mitogenic stimulation of lymphocytes
    • Eichler H.G., Hubbard R., and Snell K. The role of serine hydroxymethyltransferase in cell proliferation: DNA synthesis from serine following mitogenic stimulation of lymphocytes. Biosci Rep 1 (1981) 101-106
    • (1981) Biosci Rep , vol.1 , pp. 101-106
    • Eichler, H.G.1    Hubbard, R.2    Snell, K.3
  • 6
    • 0023829928 scopus 로고
    • Enzymic imbalance in serine metabolism in human colon carcinoma and rat sarcoma
    • Snell K., Natsumeda Y., Eble J.N., Glover J.L., and Weber G. Enzymic imbalance in serine metabolism in human colon carcinoma and rat sarcoma. Br J Cancer 57 (1988) 87-90
    • (1988) Br J Cancer , vol.57 , pp. 87-90
    • Snell, K.1    Natsumeda, Y.2    Eble, J.N.3    Glover, J.L.4    Weber, G.5
  • 7
    • 0023655502 scopus 로고
    • The modulation of serine metabolism in hepatoma 3924A during different phases of cellular proliferation in culture
    • Snell K., Natsumeda Y., and Weber G. The modulation of serine metabolism in hepatoma 3924A during different phases of cellular proliferation in culture. Biochem J 245 (1987) 609-612
    • (1987) Biochem J , vol.245 , pp. 609-612
    • Snell, K.1    Natsumeda, Y.2    Weber, G.3
  • 8
    • 0015239671 scopus 로고
    • Serine transhydroxymethylase. Affinity of the active site for substrates, substrate analogues, and anions
    • Schirch L., and Diller A. Serine transhydroxymethylase. Affinity of the active site for substrates, substrate analogues, and anions. J Biol Chem 246 (1971) 3961-3966
    • (1971) J Biol Chem , vol.246 , pp. 3961-3966
    • Schirch, L.1    Diller, A.2
  • 9
    • 0017760965 scopus 로고
    • Studies of the reactions of lamb liver serine hydroxymethyltransferase with l-phenylalanine: kinetic isotope effects upon quinonoid intermidiate formation
    • Ulevitch R.J., and Kallen R.G. Studies of the reactions of lamb liver serine hydroxymethyltransferase with l-phenylalanine: kinetic isotope effects upon quinonoid intermidiate formation. Biochemistry 16 (1977) 5342-5350
    • (1977) Biochemistry , vol.16 , pp. 5342-5350
    • Ulevitch, R.J.1    Kallen, R.G.2
  • 10
    • 0017073124 scopus 로고
    • Metabolism of glutamine and ammonia in rat liver: the effects of N-acetylglutamate and phosphate
    • Jones C.W., and Priest D.G. Metabolism of glutamine and ammonia in rat liver: the effects of N-acetylglutamate and phosphate. Arch Biochem Biophys 174 (1976) 305-311
    • (1976) Arch Biochem Biophys , vol.174 , pp. 305-311
    • Jones, C.W.1    Priest, D.G.2
  • 11
    • 0041763398 scopus 로고
    • Purification and regulatory properties of mung bean (Vigna radiata L.) serine hydroxymethyltransferase
    • Rao D.N., and Rao A.N. Purification and regulatory properties of mung bean (Vigna radiata L.) serine hydroxymethyltransferase. Plant Physiol 69 (1982) 11-18
    • (1982) Plant Physiol , vol.69 , pp. 11-18
    • Rao, D.N.1    Rao, A.N.2
  • 13
    • 0019512373 scopus 로고
    • Construction and expression of hybrid plasmids containing the Escherichia coli glyA gene
    • Stauffer G.V., Plamann M.D., and Stauffer L.T. Construction and expression of hybrid plasmids containing the Escherichia coli glyA gene. Gene 14 (1981) 63-72
    • (1981) Gene , vol.14 , pp. 63-72
    • Stauffer, G.V.1    Plamann, M.D.2    Stauffer, L.T.3
  • 14
    • 0021100754 scopus 로고
    • Complete nucleotide sequence of the Escherichia coli glyA gene
    • Plamann M., Stauffer L., Urbanowski M., and Stauffer G. Complete nucleotide sequence of the Escherichia coli glyA gene. Nucl Acids Res 11 (1983) 2065-2075
    • (1983) Nucl Acids Res , vol.11 , pp. 2065-2075
    • Plamann, M.1    Stauffer, L.2    Urbanowski, M.3    Stauffer, G.4
  • 15
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri A., Whitehorn E.A., Tate E., and Stemmer W.P. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat Biotechnol 14 (1996) 315-319
    • (1996) Nat Biotechnol , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 16
    • 0030722164 scopus 로고    scopus 로고
    • DNA shuffling and screening strategies for improving vaccine efficacy
    • Patten P.A., Howard R.J., and Stemmer W.P. DNA shuffling and screening strategies for improving vaccine efficacy. Curr Opin Biotechnol 8 (1997) 724-733
    • (1997) Curr Opin Biotechnol , vol.8 , pp. 724-733
    • Patten, P.A.1    Howard, R.J.2    Stemmer, W.P.3
  • 17
    • 0034059496 scopus 로고    scopus 로고
    • Inverting enantioselectivity by directed evolution of hydantoinase for improved production of l-methionine
    • May O., Nguyen P.T., and 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
  • 18
    • 0034518317 scopus 로고    scopus 로고
    • Directed evolution of methbolically engineered Escherichia coli for carotenoid production
    • Wang C., Oh M.K., and Liao J.C. Directed evolution of methbolically engineered Escherichia coli for carotenoid production. Biotechnol Prog 16 (2000) 922-926
    • (2000) Biotechnol Prog , vol.16 , pp. 922-926
    • Wang, C.1    Oh, M.K.2    Liao, J.C.3
  • 20
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung D.W., Chen E.Y., Goeddel D.V., et al. A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique 1 (1989) 11-15
    • (1989) Technique , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.Y.2    Goeddel, D.V.3
  • 22
    • 0028050350 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution
    • Stemmer W.P.C. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Nature 370 (1994) 389-391
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 23
    • 0030754926 scopus 로고    scopus 로고
    • Optimization of DNA shuffling for high fidelity recombination
    • Zhao H., and Arnold F.H. Optimization of DNA shuffling for high fidelity recombination. Nucl Acids Res 25 (1997) 1307-1308
    • (1997) Nucl Acids Res , vol.25 , pp. 1307-1308
    • Zhao, H.1    Arnold, F.H.2
  • 25
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash T. The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochem J 55 (1953) 416-421
    • (1953) Biochem J , vol.55 , pp. 416-421
    • Nash, T.1
  • 26
    • 0022773885 scopus 로고
    • Synthesis of l-tyrosine by a coupled reaction of serine hydroxymethyltransferase and β-tyrosinase
    • Lee T.K., and Hsiao H.Y. Synthesis of l-tyrosine by a coupled reaction of serine hydroxymethyltransferase and β-tyrosinase. Enzyme Microb Technol 9 (1986) 523-526
    • (1986) Enzyme Microb Technol , vol.9 , pp. 523-526
    • Lee, T.K.1    Hsiao, H.Y.2
  • 28
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: inter-based tools for automated comparative protein modeling
    • Peitsch M.C. ProMod and Swiss-Model: inter-based tools for automated comparative protein modeling. Biochem Soc Trans 24 (1996) 274-279
    • (1996) Biochem Soc Trans , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 29
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the swiss-PDBViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the swiss-PDBViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 31
    • 0033737481 scopus 로고    scopus 로고
    • Gene organization of a Plasmodium falciparum serine hydroxymenthyltransferase and its functional expression in Escherichia coli
    • Alfadhli S., and Rathod P.K. Gene organization of a Plasmodium falciparum serine hydroxymenthyltransferase and its functional expression in Escherichia coli. Mol Biochem Parasitol 110 (2000) 283-291
    • (2000) Mol Biochem Parasitol , vol.110 , pp. 283-291
    • Alfadhli, S.1    Rathod, P.K.2
  • 32
    • 0033152865 scopus 로고    scopus 로고
    • Protein evolution by molecular breeding
    • Minshull J., and Stemmer W.P. Protein evolution by molecular breeding. Curr Opin Chem Biol 3 (1999) 284-290
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 284-290
    • Minshull, J.1    Stemmer, W.P.2
  • 33
    • 23744475412 scopus 로고    scopus 로고
    • Recent advances in the bioremediation of persistent organic pollutants via biomolecular engineering
    • Ang E.L., Zhao H., and Obbard J.P. Recent advances in the bioremediation of persistent organic pollutants via biomolecular engineering. Enzyme Microb Technol 37 (2005) 487-496
    • (2005) Enzyme Microb Technol , vol.37 , pp. 487-496
    • Ang, E.L.1    Zhao, H.2    Obbard, J.P.3
  • 34
    • 0035009353 scopus 로고    scopus 로고
    • Directed evolution and the creation of enantioselective biocatalysts
    • Jaeger K.E., Eggert T., Eipper A., and Reetz M.T. Directed evolution and the creation of enantioselective biocatalysts. Appl Microbiol Biotechnol 55 (2001) 519-530
    • (2001) Appl Microbiol Biotechnol , vol.55 , pp. 519-530
    • Jaeger, K.E.1    Eggert, T.2    Eipper, A.3    Reetz, M.T.4
  • 35
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Hanes J., and Pluckthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc Natl Acad Sci 94 (1997) 4937-4942
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 4937-4942
    • Hanes, J.1    Pluckthun, A.2
  • 36
    • 0033584889 scopus 로고    scopus 로고
    • Selection for improved protein stability by phage display
    • Jung S., Honegger A., and Pluckthun A. Selection for improved protein stability by phage display. J Mol Biol 294 (1999) 163-180
    • (1999) J Mol Biol , vol.294 , pp. 163-180
    • Jung, S.1    Honegger, A.2    Pluckthun, A.3
  • 37
    • 0035941119 scopus 로고    scopus 로고
    • Directed evolution of α-aspartyl dipeptidase from salmonella typhimurium
    • Kong D.X., Liu M.Y., and Zhang J. Directed evolution of α-aspartyl dipeptidase from salmonella typhimurium. Biochem Biophys Res Commun 289 (2001) 137-142
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 137-142
    • Kong, D.X.1    Liu, M.Y.2    Zhang, J.3
  • 38
    • 5644249284 scopus 로고    scopus 로고
    • Directed evolution of a glycosynthase from agrobacterium sp. increases its catalytic activity dramatically and expands its substrate repertoire
    • Kim W.Y., Lee S.S., Warren J.A.R., and Withers G.S. Directed evolution of a glycosynthase from agrobacterium sp. increases its catalytic activity dramatically and expands its substrate repertoire. J Biol Chem 279 (2004) 42787-42793
    • (2004) J Biol Chem , vol.279 , pp. 42787-42793
    • Kim, W.Y.1    Lee, S.S.2    Warren, J.A.R.3    Withers, G.S.4
  • 39
    • 0035969999 scopus 로고    scopus 로고
    • Directed evolution of ampicillin-resistant activity from a functional unrelated DNA fragment: a laboratory model of molecular evolution
    • Yano T., and Kagamiyama H. Directed evolution of ampicillin-resistant activity from a functional unrelated DNA fragment: a laboratory model of molecular evolution. Proc Natl Acad Sci 98 (2001) 903-907
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 903-907
    • Yano, T.1    Kagamiyama, H.2
  • 40
    • 0022967088 scopus 로고
    • Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagines by site-directed mttagenesis
    • Hopkins S., and Schirch V. Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagines by site-directed mttagenesis. J Biol Chem 261 (1986) 3363-3369
    • (1986) J Biol Chem , vol.261 , pp. 3363-3369
    • Hopkins, S.1    Schirch, V.2
  • 41
    • 0031035739 scopus 로고    scopus 로고
    • Molecular cloning, characterization and regulation of the human mitochondrial serine hydroxymethyltransferase gene
    • Stover P., Chen L., Suh J.R., Stover D., and Shane B. Molecular cloning, characterization and regulation of the human mitochondrial serine hydroxymethyltransferase gene. J Biol Chem 272 (1997) 1842-1848
    • (1997) J Biol Chem , vol.272 , pp. 1842-1848
    • Stover, P.1    Chen, L.2    Suh, J.R.3    Stover, D.4    Shane, B.5
  • 42
    • 0032515921 scopus 로고    scopus 로고
    • Molecular cloning, characterization and alternate splicing of the human cytoplasmic serine hydroxymethyltransferase gene
    • Girgis S., Llya M., Nasrallah J.R.S., Oppenheim E., Zanetti K.A., Mastri M.G., et al. Molecular cloning, characterization and alternate splicing of the human cytoplasmic serine hydroxymethyltransferase gene. Gene 210 (1998) 315-324
    • (1998) Gene , vol.210 , pp. 315-324
    • Girgis, S.1    Llya, M.2    Nasrallah, J.R.S.3    Oppenheim, E.4    Zanetti, K.A.5    Mastri, M.G.6
  • 43
    • 0028084927 scopus 로고
    • The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases
    • Usha R., Savithri H.S., and Rao A.N. The primary structure of sheep liver cytosolic serine hydroxymethyltransferase and an analysis of the evolutionary relationships among serine hydroxymethyltransferases. Biochim Biophys Acta 1204 (1994) 75-83
    • (1994) Biochim Biophys Acta , vol.1204 , pp. 75-83
    • Usha, R.1    Savithri, H.S.2    Rao, A.N.3
  • 44
    • 0026788143 scopus 로고
    • Arginine residues involved in binding of tetrahydrofolate to sheep liver serine hydroxymethyltransferase
    • Usha R., Savithri H.S., and Rao A.N. Arginine residues involved in binding of tetrahydrofolate to sheep liver serine hydroxymethyltransferase. J Biol Chem 267 (1992) 9289-9293
    • (1992) J Biol Chem , vol.267 , pp. 9289-9293
    • Usha, R.1    Savithri, H.S.2    Rao, A.N.3
  • 45
    • 0032530853 scopus 로고    scopus 로고
    • The crystal structure of human cytosolic serine hydroxymethyltransferase
    • Renwick B.S., Snell K., and Baumann U. The crystal structure of human cytosolic serine hydroxymethyltransferase. Structure 6 (1998) 1105-1116
    • (1998) Structure , vol.6 , pp. 1105-1116
    • Renwick, B.S.1    Snell, K.2    Baumann, U.3
  • 46
    • 0030857353 scopus 로고    scopus 로고
    • Importance of the amino acid terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase
    • Jagath J.R., Sharma B., Bhaskar B., Datta A., Rao A.N., and Aavithri S.H. Importance of the amino acid terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase. Eur J Biochem 247 (1997) 372-379
    • (1997) Eur J Biochem , vol.247 , pp. 372-379
    • Jagath, J.R.1    Sharma, B.2    Bhaskar, B.3    Datta, A.4    Rao, A.N.5    Aavithri, S.H.6
  • 47
    • 0021881054 scopus 로고
    • Serine hydroxymethyltransferase from E. coli: purification and properties
    • Schirch L., Hopkins S., Villar E., and Angelaccio S. Serine hydroxymethyltransferase from E. coli: purification and properties. J Bacteriol 163 (1985) 1-7
    • (1985) J Bacteriol , vol.163 , pp. 1-7
    • Schirch, L.1    Hopkins, S.2    Villar, E.3    Angelaccio, S.4
  • 48
    • 0023149814 scopus 로고
    • Purification and characterization of a serine hydroxymethyltransferase from an obligate methylotroph, Hyphomicrobium methylovorum GM2
    • Silvia S.M., Shin-Ichiro T., Yoshikazu I., and Hideaki Y. Purification and characterization of a serine hydroxymethyltransferase from an obligate methylotroph, Hyphomicrobium methylovorum GM2. Eur J Biochem 162 (1987) 533-540
    • (1987) Eur J Biochem , vol.162 , pp. 533-540
    • Silvia, S.M.1    Shin-Ichiro, T.2    Yoshikazu, I.3    Hideaki, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.