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Volumn 62, Issue 12, 1998, Pages 2357-2363

Alanine dehydrogenase from enterobacter aerogenes: Purification, characterization, and primary structure

Author keywords

Alanine dehydrogenase; Enterobacter aerogenes; Kinetic mechanism; Nucleotide sequence; Primary structure

Indexed keywords

ALANINE DEHYDROGENASE; BACTERIAL DNA; LYSYL ENDOPEPTIDASE; OXIDOREDUCTASE; PRIMER DNA; SERINE PROTEINASE;

EID: 0032241271     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.2357     Document Type: Article
Times cited : (20)

References (29)
  • 1
    • 0027371155 scopus 로고
    • Alanine dehydrogenase (Aid) is required for normal sporulation in Bacillus subtilis
    • Siranosian, K. J., Ireton, K., and Grossman, A. D., Alanine dehydrogenase (aid) is required for normal sporulation in Bacillus subtilis. J. Bacteriol., 175, 6789-6795 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 6789-6795
    • Siranosian, K.J.1    Ireton, K.2    Grossman, A.D.3
  • 2
    • 0016223894 scopus 로고
    • Regulation of alanine dehydrogenase in Bacillus lichniformis
    • McCowen, S. M. and Phibbs, P. V. Jr., Regulation of alanine dehydrogenase in Bacillus lichniformis. J. Bacteriol., 118, 590-597 (1974).
    • (1974) J. Bacteriol. , vol.118 , pp. 590-597
    • McCowen, S.M.1    Phibbs, P.V.2
  • 3
    • 0015535639 scopus 로고
    • Ammonia assimilation in blue-green algae
    • Neilson, A. H. and Doudoroff, M., Ammonia assimilation in blue-green algae. Arch. Microbiol., 89, 15-22 (1983).
    • (1983) Arch. Microbiol. , vol.89 , pp. 15-22
    • Neilson, A.H.1    Doudoroff, M.2
  • 4
    • 0024688380 scopus 로고
    • Purification and properties of L-alanine dehydrogenase of the phototrophic bacterium Rhodobacter capsulatus E1F1
    • Caballero, F. J., Cardenas, J., and Castillo, F., Purification and properties of L-alanine dehydrogenase of the phototrophic bacterium Rhodobacter capsulatus E1F1. J. Bacteriol., 171, 3205-3210 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 3205-3210
    • Caballero, F.J.1    Cardenas, J.2    Castillo, F.3
  • 5
    • 0018974217 scopus 로고
    • Alanine dehydrogenase of the β-lactam antibiotic producer Streptomyces clavuligerus
    • Aharonowitz, Y. and Friedrich, C. G., Alanine dehydrogenase of the β-lactam antibiotic producer Streptomyces clavuligerus. Arch. Microbiol., 125, 137-142 (1980).
    • (1980) Arch. Microbiol. , vol.125 , pp. 137-142
    • Aharonowitz, Y.1    Friedrich, C.G.2
  • 6
    • 0018702816 scopus 로고
    • Purification and properties of alanine dehydrogenase from Bacillus sphaericus
    • Ohshima, T. and Soda, K., Purification and properties of alanine dehydrogenase from Bacillus sphaericus. Eur. J. Biochem., 100, 29-39 (1979).
    • (1979) Eur. J. Biochem. , vol.100 , pp. 29-39
    • Ohshima, T.1    Soda, K.2
  • 7
    • 85004282009 scopus 로고
    • Crystallization and properties of alanine dehydrogenase from Streptomyces phaeochromogenes
    • Itoh, N. and Morikawa, R., Crystallization and properties of alanine dehydrogenase from Streptomyces phaeochromogenes. Agric. Biol. Chem., 47, 2511-2519 (1983).
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 2511-2519
    • Itoh, N.1    Morikawa, R.2
  • 8
    • 50849151000 scopus 로고
    • Enzymatic properties of alanine dehydrogenase of Bacillus subtilis
    • Yoshida, A. and Freese, E., Enzymatic properties of alanine dehydrogenase of Bacillus subtilis. Biochim. Biophys. Acta, 96, 248-262 (1970).
    • (1970) Biochim. Biophys. Acta , vol.96 , pp. 248-262
    • Yoshida, A.1    Freese, E.2
  • 11
    • 0027984543 scopus 로고
    • Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum
    • Sawa, Y., Tani, M., Murata, K., Shibata, H., and Ochiai, FI., Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum. J. Biochem., 116, 995-1000 (1994).
    • (1994) J. Biochem. , vol.116 , pp. 995-1000
    • Sawa, Y.1    Tani, M.2    Murata, K.3    Shibata, H.4    Ochiai, F.I.5
  • 13
    • 0000912120 scopus 로고
    • Purification and partial characterization of alanine dehydrogenase from Streptomyces aureofa-ciens
    • Vancurova, I., Vancura, A., Vole, J., Neuzil, J., Flieger, M., Basarova, G., and Behai, V., Purification and partial characterization of alanine dehydrogenase from Streptomyces aureofa-ciens. Arch. Microbiol., 150, 438-440 (1988).
    • (1988) Arch. Microbiol. , vol.150 , pp. 438-440
    • Vancurova, I.1    Vancura, A.2    Vole, J.3    Neuzil, J.4    Flieger, M.5    Basarova, G.6    Behai, V.7
  • 14
    • 0024987320 scopus 로고
    • Thermostable alanine dehydrogenase from thermophilic Bacillus sphaericus DSM 462
    • Ohshima, T., Sakane, M., Yamazaki, T., and Soda, K., Thermostable alanine dehydrogenase from thermophilic Bacillus sphaericus DSM 462. Eur. J. Biochem., 191, 715-720 (1990).
    • (1990) Eur. J. Biochem. , vol.191 , pp. 715-720
    • Ohshima, T.1    Sakane, M.2    Yamazaki, T.3    Soda, K.4
  • 15
    • 0027180051 scopus 로고
    • Alanine dehydrogenase from soy bean nodule bacteroides: Purification and properties
    • Smith, M. T. and Emerich, S. W., Alanine dehydrogenase from soy bean nodule bacteroides: Purification and properties. Arch. Biochem. Biophys., 304, 379-385 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 379-385
    • Smith, M.T.1    Emerich, S.W.2
  • 16
    • 85009617175 scopus 로고
    • Thermostable amino acid dehydrogenases: Applications and gene cloning
    • Ohshima T. and Soda K., Thermostable amino acid dehydrogenases: Applications and gene cloning. TIBTECH, 1, 210-214 (1989).
    • (1989) TIBTECH , vol.1 , pp. 210-214
    • Ohshima, T.1    Soda, K.2
  • 17
    • 0025022003 scopus 로고
    • Alanine dehydrogenases from two Bacillus species with distinct thermostability: Molecular cloning, DNA and protein sequence determination, and structural comparison with other NAD(P)+-dependent dehydrogenases
    • +-dependent dehydrogenases. Biochemistry, 29, 1009-1015 (1990).
    • (1990) Biochemistry , vol.29 , pp. 1009-1015
    • Kuroda, S.1    Tanizawa, K.2    Sakamoto, Y.3    Tanaka, H.4    Soda, K.5
  • 19
    • 0026769810 scopus 로고
    • Structure and function of a 40,000-molecular-weight protein antigen of Mycobacterium tuberculosis
    • Andersen, A. B., Andersen, P., and Ljungqvist, L., Structure and function of a 40,000-molecular-weight protein antigen of Mycobacterium tuberculosis. Infect. Immun., 60, 2317-2323 (1992).
    • (1992) Infect. Immun. , vol.60 , pp. 2317-2323
    • Ersen, A.B.1    Ersen, P.2    Ljungqvist, L.3
  • 20
  • 21
    • 0019293885 scopus 로고
    • An absolute method for protein determination based on difference in absorbance at 235 and 280 nm
    • Whitaker J. R. and Granum P. E., An absolute method for protein determination based on difference in absorbance at 235 and 280 nm. Anal. Biochem., 109, 156-159 (1980).
    • (1980) Anal. Biochem. , vol.109 , pp. 156-159
    • Whitaker, J.R.1    Granum, P.E.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito, M. and Miura, K., Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochem. Biophys. Acta, 72, 619-629 (1963).
    • (1963) Biochem. Biophys. Acta , vol.72 , pp. 619-629
    • Saito, M.1    Miura, K.2
  • 25
    • 0027026252 scopus 로고
    • Selective amplification of cDNA sequence from total RNA by cassette-ligation mediated polymerase chain reaction (PCR): Application to sequencing 6.5 kb genome segment of hantavirus strain B-l
    • Isegawa, I., Sheng, J., Sokawa, Y., Yamanishi, K., Nakagomi, O., and Ueda, S., Selective amplification of cDNA sequence from total RNA by cassette-ligation mediated polymerase chain reaction (PCR): application to sequencing 6.5 kb genome segment of hantavirus strain B-l. Mol. Cell. Probes, 6, 467-475 (1992).
    • (1992) Mol. Cell. Probes , vol.6 , pp. 467-475
    • Isegawa, I.1    Sheng, J.2    Sokawa, Y.3    Yamanishi, K.4    Nakagomi, O.5    Ueda, S.6
  • 26
    • 0013612812 scopus 로고
    • Steady state kinetics
    • Boyer, P. D., 3rd ed, Academic Press, New York
    • Cleland, W. W., Steady state kinetics. In “The Enzyme”, ed. Boyer, P. D., 3rd ed., Vol. 2, Academic Press, New York, pp. 1-65 (1970).
    • (1970) The Enzyme , vol.2 , pp. 1-65
    • Cleland, W.W.1
  • 27
    • 0023655184 scopus 로고
    • An NAD+-dependent alanine dehydrogenase from a methylotrophic bacterium
    • +-dependent alanine dehydrogenase from a methylotrophic bacterium. Biochem. J., 244, 565-570 (1987).
    • (1987) Biochem. J. , vol.244 , pp. 565-570
    • Bellion, E.1    Tan, F.2
  • 28
    • 0019869869 scopus 로고
    • Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase
    • Grimshaw, C. E. and Cleland, W. W., Kinetic mechanism of Bacillus subtilis L-alanine dehydrogenase. Biochemistry, 20, 5600-5655 (1981).
    • (1981) Biochemistry , vol.20 , pp. 5600-5655
    • Grimshaw, C.E.1    Cleland, W.W.2


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