메뉴 건너뛰기




Volumn 185, Issue 8, 2003, Pages 2418-2431

Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE; BUTYRIC ACID DERIVATIVE; GENE PRODUCT; ISOLEUCINE; KETOMETHIOBUTYRATE; LEUCINE; METHIONINE; PHENYLALANINE; PROTEIN ASPB; PROTEIN PATA; PROTEIN YKRV; PROTEIN YUGH; PROTEIN YWFG; TYROSINE; UNCLASSIFIED DRUG; VALINE;

EID: 0037384217     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.8.2418-2431.2003     Document Type: Article
Times cited : (57)

References (55)
  • 2
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C., and J. Spizizen. 1961. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81:741-746.
    • (1961) J. Bacteriol. , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 3
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LIC-PCR)
    • Aslanidis, C., and P. J. de Jong. 1990. Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res. 18:6069-6074.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6069-6074
    • Aslanidis, C.1    De Jong, P.J.2
  • 5
    • 0019420298 scopus 로고
    • Methionine synthesis from 5′-methylthioadenosine in rat liver
    • Backlund, P. S., Jr., and R. A. Smith. 1981. Methionine synthesis from 5′-methylthioadenosine in rat liver. J. Biol. Chem. 256:1533-1535.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1533-1535
    • Backlund P.S., Jr.1    Smith, R.A.2
  • 6
    • 0029680253 scopus 로고    scopus 로고
    • Aspartate aminotransferase from an alkalophilic Bacillus contains an additional 20-amino acid extension at its functionally important N-terminus
    • Battchikova, N., M. Koivulehto, A. Denesyuk, L. Ptitsyn, Y. Boretsky, J. Hellman, and T. Korpela. 1996. Aspartate aminotransferase from an alkalophilic Bacillus contains an additional 20-amino acid extension at its functionally important N-terminus. J. Biochem. (Tokyo) 120:425-432.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 425-432
    • Battchikova, N.1    Koivulehto, M.2    Denesyuk, A.3    Ptitsyn, L.4    Boretsky, Y.5    Hellman, J.6    Korpela, T.7
  • 7
    • 0033836277 scopus 로고    scopus 로고
    • Antimalarial activities of aminooxy compounds
    • Berger, B. J. 2000. Antimalarial activities of aminooxy compounds. Antimicrob. Agents Chemother. 44:2540-2542.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2540-2542
    • Berger, B.J.1
  • 8
    • 0032468851 scopus 로고    scopus 로고
    • Methionine formation from alpha-ketomethiobutyrate in the trypanosomatid Crithidia fasciculata
    • Berger, B. J., W. W. Dai, and J. Wilson. 1998. Methionine formation from alpha-ketomethiobutyrate in the trypanosomatid Crithidia fasciculata. FEMS Microbiol. Lett. 165:305-312.
    • (1998) FEMS Microbiol. Lett. , vol.165 , pp. 305-312
    • Berger, B.J.1    Dai, W.W.2    Wilson, J.3
  • 9
    • 0034932250 scopus 로고    scopus 로고
    • Methionine regeneration and aspartate aminotransferase in parasitic protozoa
    • Berger, L. C., J. Wilson, P. Wood, and B. J. Berger. 2001. Methionine regeneration and aspartate aminotransferase in parasitic protozoa. J. Bacteriol. 183:4421-4434.
    • (2001) J. Bacteriol. , vol.183 , pp. 4421-4434
    • Berger, L.C.1    Wilson, J.2    Wood, P.3    Berger, B.J.4
  • 10
    • 0034468974 scopus 로고    scopus 로고
    • Diversity of L-methionine catabolism pathways in cheese-ripening bacteria
    • Bonnarme, P., L. Psoni, and H. E. Spinnler. 2000. Diversity of L-methionine catabolism pathways in cheese-ripening bacteria. Appl. Environ. Microbiol. 66:5514-5517.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 5514-5517
    • Bonnarme, P.1    Psoni, L.2    Spinnler, H.E.3
  • 11
    • 0017076160 scopus 로고
    • Derivation and properties of Michaelis-Menten type and Hill type equations for reference ligands
    • Chou, T. C. 1976. Derivation and properties of Michaelis-Menten type and Hill type equations for reference ligands. J. Theor. Biol. 59:253-276.
    • (1976) J. Theor. Biol. , vol.59 , pp. 253-276
    • Chou, T.C.1
  • 12
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden, A. 1974. A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem. J. 137:143-144.
    • (1974) Biochem. J. , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 13
    • 0024818761 scopus 로고
    • Cloning and sequencing of the gene coding for aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus
    • Cubellis, M. V., C. Rozzo, G. Nitti, M. I. Arnone, G. Marino, and G. Sannia. 1989. Cloning and sequencing of the gene coding for aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus. Eur. J. Biochem. 186:375-381.
    • (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
  • 14
    • 0032579183 scopus 로고    scopus 로고
    • Characterization of a branched-chain amino-acid aminotransferase from Schizosaccharomyces pombe
    • Eden, A., and N. Benvenisty. 1998. Characterization of a branched-chain amino-acid aminotransferase from Schizosaccharomyces pombe. Yeast 14: 189-194.
    • (1998) Yeast , vol.14 , pp. 189-194
    • Eden, A.1    Benvenisty, N.2
  • 15
    • 0000888840 scopus 로고    scopus 로고
    • Purification and cloning of the mitochondrial branched-chain amino acid aminotransferase from sheep placenta
    • Faure, M., F. Glomot, R. Bledsoe, S. Hutson, and I. Papet. 1999. Purification and cloning of the mitochondrial branched-chain amino acid aminotransferase from sheep placenta. Eur. J. Biochem. 259:104-111.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 104-111
    • Faure, M.1    Glomot, F.2    Bledsoe, R.3    Hutson, S.4    Papet, I.5
  • 16
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny inference package (version 3.2)
    • Felsenstein, J. 1989. PHYLIP - phylogeny inference package (version 3.2). Cladistics 5:164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 17
    • 0021187425 scopus 로고
    • Characterization of a defect in the pathway for converting 5′-deoxy-5′-methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinoma
    • Ghoda, L. Y., T. M. Savarese, D. L. Dexter, R. E. Parks, Jr., P. C. Trackman, and R. H. Abeles. 1984. Characterization of a defect in the pathway for converting 5′-deoxy-5′-methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinoma. J. Biol. Chem. 259:6715-6719.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6715-6719
    • Ghoda, L.Y.1    Savarese, T.M.2    Dexter, D.L.3    Parks R.E., Jr.4    Trackman, P.C.5    Abeles, R.H.6
  • 18
    • 0025099504 scopus 로고
    • Selective killing of Klebsiella pneumoniae by 5-trifluoromethylthioribose, Chemotherapeutic exploitation of the enzyme 5-methylthioribose kinase
    • Gianotti, A. J., P. A. Tower, J. H. Sheley, P. A. Conte, C. Spiro, A. J. Ferro, J. H. Fitchen, and M. K. Riscoe. 1990. Selective killing of Klebsiella pneumoniae by 5-trifluoromethylthioribose. Chemotherapeutic exploitation of the enzyme 5-methylthioribose kinase. J. Biol. Chem. 265:831-837.
    • (1990) J. Biol. Chem. , vol.265 , pp. 831-837
    • Gianotti, A.J.1    Tower, P.A.2    Sheley, J.H.3    Conte, P.A.4    Spiro, C.5    Ferro, A.J.6    Fitchen, J.H.7    Riscoe, M.K.8
  • 19
    • 0031735563 scopus 로고    scopus 로고
    • The S box regulon: A new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria
    • Grundy, F. J., and T. M. Henkin. 1998. The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria. Mol. Microbiol. 30:737-749.
    • (1998) Mol. Microbiol. , vol.30 , pp. 737-749
    • Grundy, F.J.1    Henkin, T.M.2
  • 20
    • 0002051540 scopus 로고    scopus 로고
    • Bioedit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall, T. A. 1999. Bioedit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41:95-98.
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 21
    • 0027408857 scopus 로고
    • Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme
    • Hall, T. R., R. Wallin, G. D. Reinhart, and S. M. Hutson. 1993. Branched chain aminotransferase isoenzymes. Purification and characterization of the rat brain isoenzyme. J. Biol. Chem. 268:3092-3098.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3092-3098
    • Hall, T.R.1    Wallin, R.2    Reinhart, G.D.3    Hutson, S.M.4
  • 22
    • 0033028593 scopus 로고    scopus 로고
    • Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae
    • Heilbronn, J., J. Wilson, and B. J. Berger. 1999. Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae. J. Bacteriol. 181:1739-1747.
    • (1999) J. Bacteriol. , vol.181 , pp. 1739-1747
    • Heilbronn, J.1    Wilson, J.2    Berger, B.J.3
  • 24
    • 0035233080 scopus 로고    scopus 로고
    • Structure and function of branched chain aminotransferases
    • Hutson, S. 2001. Structure and function of branched chain aminotransferases. Prog. Nucleic Acid Res. Mol. Biol. 70:175-206.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.70 , pp. 175-206
    • Hutson, S.1
  • 25
    • 0029584470 scopus 로고
    • Cloning and expression of the mammalian cytosolic branched chain aminotransferase isoenzyme
    • Hutson, S. M., R. K. Bledsoe, T. R. Hall, and P. A. Dawson. 1995. Cloning and expression of the mammalian cytosolic branched chain aminotransferase isoenzyme. J. Biol. Chem. 270:30344-30352.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30344-30352
    • Hutson, S.M.1    Bledsoe, R.K.2    Hall, T.R.3    Dawson, P.A.4
  • 26
    • 0031884617 scopus 로고    scopus 로고
    • Characterisation of Saccharomyces cerevisiae AR08 and AR09 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily
    • Iraqui, I., S. Vissers, M. Cartiaux, and A. Urrestarazu. 1998. Characterisation of Saccharomyces cerevisiae AR08 and AR09 genes encoding aromatic aminotransferases I and II reveals a new aminotransferase subfamily. Mol. Gen. Genet. 257:238-248.
    • (1998) Mol. Gen. Genet. , vol.257 , pp. 238-248
    • Iraqui, I.1    Vissers, S.2    Cartiaux, M.3    Urrestarazu, A.4
  • 27
    • 0032444219 scopus 로고    scopus 로고
    • Structure, evolution and action of vitamin B6-dependent enzymes
    • Jansonius, J. N. 1998. Structure, evolution and action of vitamin B6-dependent enzymes. Curr. Opin. Struct. Biol. 8:759-769.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 759-769
    • Jansonius, J.N.1
  • 28
    • 0029919942 scopus 로고    scopus 로고
    • Evolutionary recruitment of biochemically specialized subdivisions of family I within the protein superfamily of aminotransferases
    • Jensen, R. A., and W. Gu. 1996. Evolutionary recruitment of biochemically specialized subdivisions of family I within the protein superfamily of aminotransferases. J. Bacteriol. 178:2161-2171.
    • (1996) J. Bacteriol. , vol.178 , pp. 2161-2171
    • Jensen, R.A.1    Gu, W.2
  • 30
    • 0021909278 scopus 로고
    • Branched-chain amino acid aminotransferase of Escherichia coli: Nucleotide sequence of the ilvE gene and the deduced amino acid sequence
    • Kuramitsu, S., T. Ogawa, H. Ogawa, and H. Kagamiyama. 1985. Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence. J. Biochem. (Tokyo) 97:993-999.
    • (1985) J. Biochem. (Tokyo) , vol.97 , pp. 993-999
    • Kuramitsu, S.1    Ogawa, T.2    Ogawa, H.3    Kagamiyama, H.4
  • 31
    • 0022412459 scopus 로고
    • The metabolism of 5′-methylthioadenosine and 5-methylthioribose 1-phosphate in Saccharomyces cerevisiae
    • Marchitto, K. S., and A. J. Ferro. 1985. The metabolism of 5′-methylthioadenosine and 5-methylthioribose 1-phosphate in Saccharomyces cerevisiae. J. Gen. Microbiol. 131:2153-2164.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 2153-2164
    • Marchitto, K.S.1    Ferro, A.J.2
  • 32
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton, L. J., and A. E. Pegg. 1995. Polyamines as targets for therapeutic intervention. Annu. Rev. Pharmacol. Toxicol. 35:55-91.
    • (1995) Annu. Rev. Pharmacol. Toxicol. , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 33
    • 0017897799 scopus 로고
    • Aminotransferases for aromatic amino acids and aspartate in Bacillus subtilis
    • Mavrides, C., and M. Comerton. 1978. Aminotransferases for aromatic amino acids and aspartate in Bacillus subtilis. Biochim. Biophys. Acta 524: 60-67.
    • (1978) Biochim. Biophys. Acta , vol.524 , pp. 60-67
    • Mavrides, C.1    Comerton, M.2
  • 34
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta, P. K., T. I. Hale, and P. Christen. 1993. Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem. 214:549-561.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 35
    • 0029117531 scopus 로고
    • Culture conditions that influence accumulation of zwittermicin A by Bacillus cereus UW85
    • Milner, J. L., S. J. Raffel, B. J. Lethbridge, and J. Handelsman. 1995. Culture conditions that influence accumulation of zwittermicin A by Bacillus cereus UW85. Appl. Microbiol. Biotechnol. 43:685-691.
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 685-691
    • Milner, J.L.1    Raffel, S.J.2    Lethbridge, B.J.3    Handelsman, J.4
  • 38
    • 0036202171 scopus 로고    scopus 로고
    • Prediction of gene function in methylthioadenosine recycling from regulatory signals
    • Murphy, B. A., F. J. Grundy, and T. M. Henkin. 2002. Prediction of gene function in methylthioadenosine recycling from regulatory signals. J. Bacteriol. 184:2314-2318.
    • (2002) J. Bacteriol. , vol.184 , pp. 2314-2318
    • Murphy, B.A.1    Grundy, F.J.2    Henkin, T.M.3
  • 39
    • 0031590443 scopus 로고    scopus 로고
    • Cloning and sequencing of aspartate aminotransferase from Thermus aquaticus YT1
    • O'Farrell, P. A., G. Sannia, J. M. Walker, and S. Doonan. 1997. Cloning and sequencing of aspartate aminotransferase from Thermus aquaticus YT1. Biochem. Biophys. Res. Commun. 239:810-815.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 810-815
    • O'Farrell, P.A.1    Sannia, G.2    Walker, J.M.3    Doonan, S.4
  • 40
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page, R. D. 1996. TreeView: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12:357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 42
    • 0023791057 scopus 로고
    • Analogs of 5-methylthioribose, a novel class of antiprotozoal agents
    • Riscoe, M. K., A. J. Ferro, and J. H. Fitchen. 1988. Analogs of 5-methylthioribose, a novel class of antiprotozoal agents. Antimicrob. Agents Chemother. 32:1904-1906.
    • (1988) Antimicrob. Agents Chemother. , vol.32 , pp. 1904-1906
    • Riscoe, M.K.1    Ferro, A.J.2    Fitchen, J.H.3
  • 43
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and M. Nei. 1987. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 44
    • 0034076449 scopus 로고    scopus 로고
    • S-adenosylmethionine decarboxylase of Bacillus subtilis is closely related to archaebacterial counterparts
    • Sekowska, A., J. Y. Coppee, J. P. Le Caer, I. Martin-Verstraete, and A. Danchin. 2000. S-adenosylmethionine decarboxylase of Bacillus subtilis is closely related to archaebacterial counterparts. Mol. Microbiol. 36:1135-1147.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1135-1147
    • Sekowska, A.1    Coppee, J.Y.2    Le Caer, J.P.3    Martin-Verstraete, I.4    Danchin, A.5
  • 45
    • 0033615370 scopus 로고    scopus 로고
    • Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis
    • Sekowska, A., and A. Danchin. 1999. Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis. DNA Res. 6:255-264.
    • (1999) DNA Res. , vol.6 , pp. 255-264
    • Sekowska, A.1    Danchin, A.2
  • 46
    • 19044362589 scopus 로고    scopus 로고
    • The methionine salvage pathway in Bacillus subtilis
    • Sekowska, A., and A. Danchin. 2002. The methionine salvage pathway in Bacillus subtilis. BMC Microbiol. 2:8.
    • (2002) BMC Microbiol. , vol.2 , pp. 8
    • Sekowska, A.1    Danchin, A.2
  • 47
    • 19044394765 scopus 로고    scopus 로고
    • MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis
    • Sekowska, A., L. Mulard, S. Krogh, J. K. Tse, and A. Danchin. 2001. MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis. BMC Microbiol. 1:15.
    • (2001) BMC Microbiol. , vol.1 , pp. 15
    • Sekowska, A.1    Mulard, L.2    Krogh, S.3    Tse, J.K.4    Danchin, A.5
  • 48
    • 0028854698 scopus 로고
    • Cloning and expression of human tyrosine aminotransferase cDNA
    • Seralini, G. E., V. Luu-The, and F. Labrie. 1995. Cloning and expression of human tyrosine aminotransferase cDNA. Biochim. Biophys. Acta 1260:97-101.
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 97-101
    • Seralini, G.E.1    Luu-The, V.2    Labrie, F.3
  • 50
    • 0025264166 scopus 로고
    • Purification and characterization of thermostable aspartate aminotransferase from a thermophilic Bacillus species
    • Sung, M. H., K. Tanizawa, H. Tanaka, S. Kuramitsu, H. Kagamiyama, and K. Soda. 1990. Purification and characterization of thermostable aspartate aminotransferase from a thermophilic Bacillus species. J. Bacteriol. 172: 1345-1351.
    • (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
  • 51
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 52
    • 0001467537 scopus 로고
    • Recycling of 5′-methylthioadenosine-ribose carbon atoms into methionine in tomato tissue in relation to ethylene production
    • Wang, S. Y., D. O. Adams, and M. Lieberman. 1982. Recycling of 5′-methylthioadenosine-ribose carbon atoms into methionine in tomato tissue in relation to ethylene production. Plant Physiol. 70:117-121.
    • (1982) Plant Physiol. , vol.70 , pp. 117-121
    • Wang, S.Y.1    Adams, D.O.2    Lieberman, M.3
  • 53
    • 9344235427 scopus 로고    scopus 로고
    • Cloning and characterization of the metE gene encoding S-adenosylmethionine synthetase from Bacillus subtilis
    • Yocum, R. R., J. B. Perkins, C. L. Howitt, and J. Pero. 1996. Cloning and characterization of the metE gene encoding S-adenosylmethionine synthetase from Bacillus subtilis. J. Bacteriol. 178:4604-4610.
    • (1996) J. Bacteriol. , vol.178 , pp. 4604-4610
    • Yocum, R.R.1    Perkins, J.B.2    Howitt, C.L.3    Pero, J.4
  • 54
    • 0016703533 scopus 로고
    • D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties
    • Yonaha, K., H. Misono, T. Yamamoto, and K. Soda. 1975. D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties. J. Biol. Chem. 250:6983-6989.
    • (1975) J. Biol. Chem. , vol.250 , pp. 6983-6989
    • Yonaha, K.1    Misono, H.2    Yamamoto, T.3    Soda, K.4
  • 55
    • 0033981077 scopus 로고    scopus 로고
    • Characterization and role of the branched-chain aminotransferase (BcaT) isolated from Lactococcus lactis subsp. cremoris NCDO 763
    • Yvon, M., E. Chambellon, A. Bolotin, and F. Roudot-Algaron. 2000. Characterization and role of the branched-chain aminotransferase (BcaT) isolated from Lactococcus lactis subsp. cremoris NCDO 763. Appl. Environ. Microbiol. 66:571-577.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 571-577
    • Yvon, M.1    Chambellon, E.2    Bolotin, A.3    Roudot-Algaron, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.