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Volumn 67, Issue 3, 2003, Pages 490-498

Characterization of aspartate aminotransferase from the cyanobacterium phormidiu lapideum

Author keywords

Aspartate aminotransferase; Cyanobacterium; Phormidium lapideum; Thermotolerant enzyme

Indexed keywords

2 OXOGLUTARIC ACID; AGENTS INTERACTING WITH TRANSMITTER, HORMONE OR DRUG RECEPTORS; ALPHA-KETOGLUTARIC ACID; AMINO ACID; ASPARTATE AMINOTRANSFERASE; ASPARTIC ACID; CYSTEINE; CYSTEINE SULFINIC ACID; DRUG DERIVATIVE;

EID: 0038459991     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.67.490     Document Type: Article
Times cited : (11)

References (40)
  • 1
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta, P. K., Hale, T. I., and Christen, P., Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem., 214, 549-561 (1993).
    • (1993) Eur. J. Biochem. , vol.214 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 2
    • 0029919942 scopus 로고    scopus 로고
    • Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases
    • Jensen, R. A., and Gu, W., Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases. J. Bacteriol., 178, 2161-2171 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 2161-2171
    • Jensen, R.A.1    Gu, W.2
  • 3
    • 0030025487 scopus 로고    scopus 로고
    • An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8
    • Okamoto, A., Kato, R., Masui, R., Yamagishi, A., Oshima, T., and Kuramitsu, S., An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. J. Biochem. (Tokyo), 119, 135-144 (1996).
    • (1996) J. Biochem. (Tokyo) , vol.119 , pp. 135-144
    • Okamoto, A.1    Kato, R.2    Masui, R.3    Yamagishi, A.4    Oshima, T.5    Kuramitsu, S.6
  • 4
    • 0025911849 scopus 로고
    • Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary X-ray characterization
    • Sung, M.-H., Tanizawa, K., Tanaka, H., Kuramitsu, S., Kagamiyama, H., Hirotsu, K., Okamoto, A., Higuchi, T., and Soda, K., Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary X-ray characterization. J. Biol. Chem., 266, 2567-2572 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 2567-2572
    • Sung, M.-H.1    Tanizawa, K.2    Tanaka, H.3    Kuramitsu, S.4    Kagamiyama, H.5    Hirotsu, K.6    Okamoto, A.7    Higuchi, T.8    Soda, K.9
  • 5
    • 0027219893 scopus 로고
    • Isolation and characterization of a gene coding for a novel aspartate aminotransferase from Rhizobium meliloti
    • Alfano, J. R., and Kahn, M. L., Isolation and characterization of a gene coding for a novel aspartate aminotransferase from Rhizobium meliloti. J. Bacteriol., 175, 4186-4196 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 4186-4196
    • Alfano, J.R.1    Kahn, M.L.2
  • 6
    • 0024818761 scopus 로고
    • Cloning and sequencing of the gene coding for aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolo-bus solfataricus
    • Cubellis, M. V., Rozzo, C., Nitti, G., Arnone, M. I., Marino, G., and Sannia, G., Cloning and sequencing of the gene coding for aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolo-bus solfataricus. Eur. J. Biochem., 186, 375-381 (1989).
    • (1989) Eur. J. Biochem. , vol.186 , pp. 375-381
    • Cubellis, M.V.1    Rozzo, C.2    Nitti, G.3    Arnone, M.I.4    Marino, G.5    Sannia, G.6
  • 7
    • 0028914569 scopus 로고
    • Pyridoxal phosphate-dependent enzymes
    • John, R. A., Pyridoxal phosphate-dependent enzymes. Biochim. Biophys. Acta, 1248, 81-96 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 81-96
    • John, R.A.1
  • 8
    • 0025264166 scopus 로고
    • Purification and characterization of thermostable aspartate aminotransferase from a thermophilic Bacillus species
    • Sung, M.-H., Tanizawa, K., Tanaka, H., Kuramitsu, S., Kagamiyama, H., and Soda, K., Purification and characterization of thermostable aspartate aminotransferase from a thermophilic Bacillus species. J. Bacteriol., 172, 1345-1351 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 1345-1351
    • Sung, M.-H.1    Tanizawa, K.2    Tanaka, H.3    Kuramitsu, S.4    Kagamiyama, H.5    Soda, K.6
  • 9
    • 0024279194 scopus 로고
    • Purification and characterization of aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
    • Marino, G., Nitti, G., Arnone, M. I., Sannia, G., Gambacorta, A., and Rosa, M. D., Purification and characterization of aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. J. Biol. Chem., 263, 12305-12309 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 12305-12309
    • Marino, G.1    Nitti, G.2    Arnone, M.I.3    Sannia, G.4    Gambacorta, A.5    Rosa, M.D.6
  • 10
    • 0026751404 scopus 로고
    • X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
    • McPhalen, C. A., Vincent, M. G., and Jansonius, J. N., X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J. Mol. Biol., 225, 495-517 (1992).
    • (1992) J. Mol. Biol. , vol.225 , pp. 495-517
    • Mc Phalen, C.A.1    Vincent, M.G.2    Jansonius, J.N.3
  • 11
    • 0028904402 scopus 로고
    • Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 Â resolution
    • Malashkevich, V. N., Strokopytov, B. V., Borisov, V. V., Dauter, Z., Wilson, K. S., and Torchinsky, Y. M., Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 Â resolution. J. Mol. Biol., 247, 111-124 (1995).
    • (1995) J. Mol. Biol. , vol.247 , pp. 111-124
    • Malashkevich, V.N.1    Strokopytov, B.V.2    Borisov, V.V.3    Dauter, Z.4    Wilson, K.S.5    Torchinsky, Y.M.6
  • 12
    • 0028174289 scopus 로고
    • Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms
    • Jager, J., Moser, M., Sauder, U., and Jansonius, J. N., Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms. J. Mol. Biol., 239, 285-305 (1994).
    • (1994) J. Mol. Biol. , vol.239 , pp. 285-305
    • Jager, J.1    Moser, M.2    Sauder, U.3    Jansonius, J.N.4
  • 13
    • 0028028030 scopus 로고
    • X-ray crystallographic study of pyridoxamine 5?-phosphate-type aspartate aminotransferases from Escherichia coli in three forms
    • Miyahara, I., Hirotsu, K., Hayashi, H., and Kagamiyama, H., X-ray crystallographic study of pyridoxamine 5?-phosphate-type aspartate aminotransferases from Escherichia coli in three forms. J. Biochem. (Tokyo), 116, 1001-1012 (1994).
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 1001-1012
    • Miyahara, I.1    Hirotsu, K.2    Hayashi, H.3    Kagamiyama, H.4
  • 14
    • 0030845064 scopus 로고    scopus 로고
    • Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate
    • Rhee, S., Silva, M. M., Hyde, C. C., Rogers, P. H., Metzler, C. M., Metzler, D. E., and Arnone, A., Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate. J. Biol. Chem., 272, 17293-17302 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 17293-17302
    • Rhee, S.1    Silva, M.M.2    Hyde, C.C.3    Rogers, P.H.4    Metzler, C.M.5    Metzler, D.E.6    Arnone, A.7
  • 16
    • 0002641297 scopus 로고
    • Cell Differentiation and Funcition
    • Papageorgiou, G. C., and Packer, L., Elesevier Biomedica, New York
    • Flores, E., Ramos, J. L., Herrero, A., and Guerrero, M. G., Cell Differentiation and Funcition. In “Photosynthetic prokaryotes”, eds. Papageorgiou, G. C., and Packer, L., Elesevier Biomedica, New York, pp. 363-384 (1983).
    • (1983) Photosynthetic Prokaryotes , pp. 363-384
    • Flores, E.1    Ramos, J.L.2    Herrero, A.3    Guerrero, M.G.4
  • 17
    • 0024208166 scopus 로고
    • Glutamine synthetase from a cyanobacterium, Phormidium lapideum: Purification, characterization, and comparison with other cyanobacterial enzymes
    • Sawa, Y., Ochiai, H., Yoshida, K., Tanizawa, K., Tanaka, H., and Soda, K., Glutamine synthetase from a cyanobacterium, Phormidium lapideum: purification, characterization, and comparison with other cyanobacterial enzymes. J. Biochem. (Tokyo), 104, 917-923 (1988).
    • (1988) J. Biochem. (Tokyo) , vol.104 , pp. 917-923
    • Sawa, Y.1    Ochiai, H.2    Yoshida, K.3    Tanizawa, K.4    Tanaka, H.5    Soda, K.6
  • 18
    • 0024618578 scopus 로고
    • Purification and properties of glutamine synthetase from the non-N2-fixing cyanobacterium Phor-midium laminosum
    • 2-fixing cyanobacterium Phor-midium laminosum. J. Bacteriol., 171, 1158-1165 (1989).
    • (1989) J. Bacteriol. , vol.171 , pp. 1158-1165
    • Blanco, F.1    Alana, A.2    Llama, M.J.3    Serra, J.L.4
  • 19
    • 0031051869 scopus 로고    scopus 로고
    • Purification and characterization of a new type of glutamine synthetase from cyanobacteria
    • Garcia-Dominguez, M., Reyes, J. C., and Florencio, F. J., Purification and characterization of a new type of glutamine synthetase from cyanobacteria. Eur. J. Biochem., 244, 258-264 (1997).
    • (1997) Eur. J. Biochem. , vol.244 , pp. 258-264
    • Garcia-Dominguez, M.1    Reyes, J.C.2    Florencio, F.J.3
  • 20
    • 0343517151 scopus 로고    scopus 로고
    • Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the cyanobacterium Synechocystis sp. PCC 6803: Expression and assembly in Escherichia coli
    • Navarro, F., Martin-Figueroa, E., Candau, P., and Florencio, F. J., Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the cyanobacterium Synechocystis sp. PCC 6803: expression and assembly in Escherichia coli. Arch. Biochem. Biophys., 379, 267-276 (2000).
    • (2000) Arch. Biochem. Biophys. , vol.379 , pp. 267-276
    • Navarro, F.1    Martin-Figueroa, E.2    Candau, P.3    Florencio, F.J.4
  • 21
    • 0027984543 scopus 로고
    • Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum
    • Sawa, Y., Tani, M., Murata, K., Shibata, H., and Ochiai, H., Purification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum. J. Biochem. (Tokyo), 116, 995-1000 (1994).
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 995-1000
    • Sawa, Y.1    Tani, M.2    Murata, K.3    Shibata, H.4    Ochiai, H.5
  • 22
    • 0003466067 scopus 로고
    • Transaminases
    • Dolphi, D., Poulson, R., and Avramovic, O., John Wiley, New York
    • Salerno, C., Giartosio, A., and Fasella, P., Transaminases. In “Vitamin B6 pyridoxal phosphate”, eds. Dolphi, D., Poulson, R., and Avramovic, O., John Wiley, New York, part B, pp. 117-167 (1986).
    • (1986) Vitamin B6 Pyridoxal Phosphate , pp. 117-167
    • Salerno, C.1    Giartosio, A.2    Fasella, P.3
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for 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
  • 24
    • 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
  • 25
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H., Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry, 6, 1948-1954 (1967).
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 26
    • 0018416496 scopus 로고
    • Ellman’s reagent: 5,5?-dithiobis (2-nitrobenzoic acid) a reexamination
    • Riddles, P. W., Blakeley, R. L., and Zerner, B., Ellman’s reagent: 5,5?-dithiobis (2-nitrobenzoic acid) a reexamination. Anal. Biochem., 94, 75-81 (1979).
    • (1979) Anal. Biochem. , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 27
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P., Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem., 262, 10035-10038 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 28
    • 0022272517 scopus 로고
    • Glutamate-aspartate transaminase from microorganisms
    • Yagi, T., Kagamiyama, H., Nozak, M., and Soda, K., Glutamate-aspartate transaminase from microorganisms. Methods Enzymol., 113, 83-89 (1985).
    • (1985) Methods Enzymol. , vol.113 , pp. 83-89
    • Yagi, T.1    Kagamiyama, H.2    Nozak, M.3    Soda, K.4
  • 29
    • 0027077735 scopus 로고
    • Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures
    • Tanaka, T., Yamamoto, S., Taniguchi, M., Hayashi, H., Kuramitsu, S., Kagamiyama, H., and Oi, S., Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures. J. Biochem. (Tokyo), 112, 811-815 (1992).
    • (1992) J. Biochem. (Tokyo) , vol.112 , pp. 811-815
    • Tanaka, T.1    Yamamoto, S.2    Taniguchi, M.3    Hayashi, H.4    Kuramitsu, S.5    Kagamiyama, H.6    Oi, S.7
  • 30
    • 0002568348 scopus 로고
    • The binding of pyridoxal 5-phosphate to aspartate aminotransferase of pig heart
    • Scardi, V., Scotto, P., Iaccarino, M., and Scarano, E., The binding of pyridoxal 5-phosphate to aspartate aminotransferase of pig heart. Biochem. J., 88, 172-175 (1963).
    • (1963) Biochem. J. , vol.88 , pp. 172-175
    • Scardi, V.1    Scotto, P.2    Iaccarino, M.3    Scarano, E.4
  • 31
    • 0001515809 scopus 로고
    • The enzymatic oxidation of pyridoxine and pyridoxamine phosphates
    • Wada, H., and Snell, E. E., The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J. Biol. Chem., 236, 2089-2095 (1961).
    • (1961) J. Biol. Chem. , vol.236 , pp. 2089-2095
    • Wada, H.1    Snell, E.E.2
  • 32
    • 0028344034 scopus 로고
    • Further thermal characterization of an aspartate aminotransferase from a halophilic organism
    • Muriana, F. J., Alvarez-Ossorio, M. C., and Relimpio, A. M., Further thermal characterization of an aspartate aminotransferase from a halophilic organism. Biochem. J., 298, 465-470 (1994).
    • (1994) Biochem. J. , vol.298 , pp. 465-470
    • Muriana, F.J.1    Alvarez-Ossorio, M.C.2    Relimpio, A.M.3
  • 33
    • 0025371891 scopus 로고
    • Purification and properties of L-aspar-tate aminotransferase of Chlamydomonas rein-hardtii
    • Lain-Guelbenzu, B., Munoz-Blanco, J., and Cardenas, J., Purification and properties of L-aspar-tate aminotransferase of Chlamydomonas rein-hardtii. Eur. J. Bochem., 188, 529-533 (1990).
    • (1990) Eur. J. Bochem. , vol.188 , pp. 529-533
    • Lain-Guelbenzu, B.1    Munoz-Blanco, J.2    Cardenas, J.3
  • 34
    • 0018802745 scopus 로고
    • Cysteine sulfonate transamination activity of aspartate aminotransferases
    • Yagi, T., Kagamiyama, H., and Nozaki, M., Cysteine sulfonate transamination activity of aspartate aminotransferases. Biochem. Biophys. Res. Commun., 90, 1447-1452 (1981).
    • (1981) Biochem. Biophys. Res. Commun. , vol.90 , pp. 1447-1452
    • Yagi, T.1    Kagamiyama, H.2    Nozaki, M.3
  • 35
    • 0000427037 scopus 로고
    • A kinetic and equilibrium analysis of the glutamic oxaloacetate transaminase mechanism
    • Velick, S. F., and Vavra, J., A kinetic and equilibrium analysis of the glutamic oxaloacetate transaminase mechanism. J. Biol. Chem., 237, 2109-2122 (1962).
    • (1962) J. Biol. Chem. , vol.237 , pp. 2109-2122
    • Velick, S.F.1    Vavra, J.2
  • 36
    • 4544296061 scopus 로고
    • The influence of inorganic nitrogen supply on amination and related reactions in the blue-green alga, Anabaena cylindrica Lemm
    • Batt, T., and Brown, D. H., The influence of inorganic nitrogen supply on amination and related reactions in the blue-green alga, Anabaena cylindrica Lemm. Planta, 116, 27-37 (1974).
    • (1974) Planta , vol.116 , pp. 27-37
    • Batt, T.1    Brown, D.H.2
  • 37
    • 0017113897 scopus 로고
    • Alanine dehydrogenase of the N2-fixing blue-green alga, Anabaena cylindrica
    • 2-fixing blue-green alga, Anabaena cylindrica. Arch. Microbiol., 107, 115-124 (1976).
    • (1976) Arch. Microbiol. , vol.107 , pp. 115-124
    • Rowell, P.1    Stewart, W.D.P.2
  • 38
    • 0021880512 scopus 로고
    • Inhibition of nitrate utilization by amino acids in intact Anacystis nidulans cells
    • Romero, J. M., Flores, E., and Guerrero, M. G., Inhibition of nitrate utilization by amino acids in intact Anacystis nidulans cells. Arch. Mircrobiol., 142, 1-5 (1985).
    • (1985) Arch. Mircrobiol. , vol.142 , pp. 1-5
    • Romero, J.M.1    Flores, E.2    Guerrero, M.G.3
  • 39
    • 0017324410 scopus 로고
    • Phototrophic prokaryotes: The cyanobacteria
    • Stanier, R. Y., and Cohen-Bazire, G., Phototrophic prokaryotes: the cyanobacteria. Annu. Rev. Microbiol., 31, 225-274 (1977).
    • (1977) Annu. Rev. Microbiol. , vol.31 , pp. 225-274
    • Stanier, R.Y.1    Cohen-Bazire, G.2


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