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Volumn 70, Issue 9, 2006, Pages 2230-2235

Alteration of coenzyme specificity of lactate dehydrogenase from Thermus thermophilus by introducing the loop region of NADP(H)-dependent malate dehydrogenase

Author keywords

Coenzyme specificity; Lactate dehydrogenase; Thermus thermophilus

Indexed keywords

COENZYME SPECIFICITY; LACTATE DEHYDROGENASE; MUTANT ENZYMES; THERMUS THERMOPHILUS;

EID: 33749004786     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60170     Document Type: Article
Times cited : (13)

References (21)
  • 1
    • 0023057044 scopus 로고
    • Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity
    • Nishiyama, M., Matsubara, N., Yamamoto, K., Iijima, S., Uozumi, T., and Beppu, T., Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity. J. Biol. Chem., 261, 14178-14183 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 14178-14183
    • Nishiyama, M.1    Matsubara, N.2    Yamamoto, K.3    Iijima, S.4    Uozumi, T.5    Beppu, T.6
  • 2
    • 0018966272 scopus 로고
    • Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile Thermus flavus AT-62
    • Iijima, S., Saiki, T., and Beppu, T., Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile Thermus flavus AT-62. Biochim. Biophys. Acta, 613, 1-9 (1980).
    • (1980) Biochim. Biophys. Acta , vol.613 , pp. 1-9
    • Iijima, S.1    Saiki, T.2    Beppu, T.3
  • 3
    • 0027156651 scopus 로고
    • Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • Kelly, C. A., Nishiyama, M., Ohnishi, Y., Beppu, T., and Birktoft, J. J., Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. Biochemistry, 32, 3913-3922 (1993).
    • (1993) Biochemistry , vol.32 , pp. 3913-3922
    • Kelly, C.A.1    Nishiyama, M.2    Ohnishi, Y.3    Beppu, T.4    Birktoft, J.J.5
  • 4
    • 0031887256 scopus 로고    scopus 로고
    • Designing the hydrophobic core of Thermus flavus malate dehydrogenase based on side-chain packing
    • Kono, H., Nishiyama, M., Tanokura, M., and Doi, J., Designing the hydrophobic core of Thermus flavus malate dehydrogenase based on side-chain packing. Protein Eng., 11, 47-52 (1998).
    • (1998) Protein Eng. , vol.11 , pp. 47-52
    • Kono, H.1    Nishiyama, M.2    Tanokura, M.3    Doi, J.4
  • 5
    • 0027415645 scopus 로고
    • Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis
    • Nishiyama, M., Birktoft, J. J., and Beppu, T., Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis. J. Biol. Chem., 268, 4656-4660 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 4656-4660
    • Nishiyama, M.1    Birktoft, J.J.2    Beppu, T.3
  • 6
    • 22144480963 scopus 로고    scopus 로고
    • Crystal structure of NAD-dependent malate dehydrogenase complexed with NADP(H)
    • Tomita, T., Fushinobu, S., Kuzuyama, T., and Nishiyama, M., Crystal structure of NAD-dependent malate dehydrogenase complexed with NADP(H). Biochem. Biophys. Res. Commun., 334, 613-618 (2005).
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 613-618
    • Tomita, T.1    Fushinobu, S.2    Kuzuyama, T.3    Nishiyama, M.4
  • 7
    • 0030893657 scopus 로고    scopus 로고
    • NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding
    • Carugo, O., and Argos, P., NADP-dependent enzymes. I: conserved stereochemistry of cofactor binding. Proteins, 28, 10-28 (1997).
    • (1997) Proteins , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 8
    • 0142071842 scopus 로고    scopus 로고
    • Complete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase
    • Rosell, A., Valencia, E., Ochoa, W. F., Fita, I., Pares, X., and Farres, J., Complete reversal of coenzyme specificity by concerted mutation of three consecutive residues in alcohol dehydrogenase. J. Biol. Chem., 278, 40573-40580 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 40573-40580
    • Rosell, A.1    Valencia, E.2    Ochoa, W.F.3    Fita, I.4    Pares, X.5    Farres, J.6
  • 9
    • 0025191073 scopus 로고
    • A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme
    • Feeney, R., Clarke, A. R., and Holbrook, J. J., A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme. Biochem. Biophys. Res. Commun., 166, 667-672 (1990).
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 667-672
    • Feeney, R.1    Clarke, A.R.2    Holbrook, J.J.3
  • 10
    • 0032744506 scopus 로고    scopus 로고
    • Redesign of the coenzyme specificity in L-lactate dehydrogenase from Bacillus stearothermophilus using site-directed mutagenesis and media engineering
    • Holmberg, N., Ryde, U., and Bulow, L., Redesign of the coenzyme specificity in L-lactate dehydrogenase from Bacillus stearothermophilus using site-directed mutagenesis and media engineering. Protein Eng., 12, 851-856 (1999).
    • (1999) Protein Eng. , vol.12 , pp. 851-856
    • Holmberg, N.1    Ryde, U.2    Bulow, L.3
  • 11
    • 23944434781 scopus 로고    scopus 로고
    • A modified consensus approach to mutagenesis inverts the cofactor specificity of Bacillus stearothermophilus lactate dehydrogenase
    • Flores, H., and Ellington, A. D., A modified consensus approach to mutagenesis inverts the cofactor specificity of Bacillus stearothermophilus lactate dehydrogenase. Protein Eng. Des. Sel., 18, 369-377 (2005).
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 369-377
    • Flores, H.1    Ellington, A.D.2
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W., Statistical analysis of enzyme kinetic data. Methods Enzymol., 78, 103-138 (1979).
    • (1979) Methods Enzymol. , vol.78 , pp. 103-138
    • Cleland, W.W.1
  • 15
    • 0021743361 scopus 로고
    • L-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium: Desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence
    • Taguchi, H., Matsuzawa, H., and Ohta, T., L-Lactate dehydrogenase from Thermus caldophilus GK24, an extremely thermophilic bacterium: desensitization to fructose 1,6-bisphosphate in the activated state by arginine-specific chemical modification and the N-terminal amino acid sequence. Eur. J. Biochem., 145, 283-290 (1984).
    • (1984) Eur. J. Biochem. , vol.145 , pp. 283-290
    • Taguchi, H.1    Matsuzawa, H.2    Ohta, T.3
  • 16
    • 0017577897 scopus 로고
    • Comparative studies of lactic acid dehydrogenases in lactic acid bacteria. I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei ssp. casei and Lactobacillus curvatus
    • Hensel, R., Mayr, U., Stetter, K. O., and Kandler, O., Comparative studies of lactic acid dehydrogenases in lactic acid bacteria. I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei ssp. casei and Lactobacillus curvatus. Arch. Microbiol., 112, 81-93 (1977).
    • (1977) Arch. Microbiol. , vol.112 , pp. 81-93
    • Hensel, R.1    Mayr, U.2    Stetter, K.O.3    Kandler, O.4
  • 17
    • 0026512524 scopus 로고
    • Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5Å resolution
    • Wigley, D. B., Gamblin, S. J., Turkenburg, J. P., Dodson, E. J., Piontek, K., Muirhead, H., and Holbrook, J. J., Structure of a ternary complex of an allosteric lactate dehydrogenase from Bacillus stearothermophilus at 2.5Å resolution. J. Mol. Biol., 223, 317-335 (1992).
    • (1992) J. Mol. Biol. , vol.223 , pp. 317-335
    • Wigley, D.B.1    Gamblin, S.J.2    Turkenburg, J.P.3    Dodson, E.J.4    Piontek, K.5    Muirhead, H.6    Holbrook, J.J.7
  • 18
    • 0000869471 scopus 로고
    • Fructose-1,6-diphosphate requirement of streptococcal lactic dehydrogenases
    • Wolin, M. J., Fructose-1,6-diphosphate requirement of streptococcal lactic dehydrogenases. Science, 146, 775-777 (1964).
    • (1964) Science , vol.146 , pp. 775-777
    • Wolin, M.J.1
  • 19
    • 0029151201 scopus 로고
    • CH/π interaction in the packing of the adenine ring in protein structures
    • Chakrabarti, P., and Samanta, U., CH/π interaction in the packing of the adenine ring in protein structures. J. Mol. Biol., 251, 9-14 (1995).
    • (1995) J. Mol. Biol. , vol.251 , pp. 9-14
    • Chakrabarti, P.1    Samanta, U.2
  • 20
    • 0033561407 scopus 로고    scopus 로고
    • Chloroplast NADP-malate dehydrogenase: Structural basis of light-dependent regulation of activity by thiol oxidation and reduction
    • Carr, P. D., Verger, D., Ashton, A. R., and Ollis, D. L., Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction. Structure, 7, 461-475 (1999).
    • (1999) Structure , vol.7 , pp. 461-475
    • Carr, P.D.1    Verger, D.2    Ashton, A.R.3    Ollis, D.L.4
  • 21
    • 77956940478 scopus 로고
    • Lactate dehydrogenase
    • ed. Boyer, E. D., Academic Press, New York
    • Holbrook, J. J., Liljas, A., Steindel, S. J., and Rossman, M. G., Lactate dehydrogenase. In "The Enzymes," ed. Boyer, E. D., Academic Press, New York, pp. 191-289 (1975).
    • (1975) The Enzymes , pp. 191-289
    • Holbrook, J.J.1    Liljas, A.2    Steindel, S.J.3    Rossman, M.G.4


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