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Volumn 248, Issue 2, 1997, Pages 385-393

Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38

Author keywords

Arthrobacter; D threonine aldolase; Divalent cation; Pyridoxal 5' phosphate; Threonine

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE;

EID: 0030931107     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00385.x     Document Type: Article
Times cited : (49)

References (47)
  • 1
    • 0022819963 scopus 로고
    • Evolution of biosynthetic pathways: A common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase
    • Parsot, C. (1986) Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase, EMBO J. 5, 3013-3019.
    • (1986) EMBO J. , vol.5 , pp. 3013-3019
    • Parsot, C.1
  • 2
    • 0021101299 scopus 로고
    • Nucleotide sequence of thrC and of the transcription termination region of the threonine operon in Escherichia coli K12
    • Parsot, C., Cossart, P., Saint-Girons, I. & Cohen, G. N. (1983) Nucleotide sequence of thrC and of the transcription termination region of the threonine operon in Escherichia coli K12, Nucleic Acids Res. 11, 7331-7345.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 7331-7345
    • Parsot, C.1    Cossart, P.2    Saint-Girons, I.3    Cohen, G.N.4
  • 3
    • 0023627141 scopus 로고
    • The complete nucleotide sequence of the ilvGMEDA cluster of Escherichia coli K-12
    • Cox, J. L., Cox, B. J., Fidanza, V. & Calhoun, D. H. (1987) The complete nucleotide sequence of the ilvGMEDA cluster of Escherichia coli K-12, Gene (Amst.) 56. 185-198.
    • (1987) Gene (Amst.) , vol.56 , pp. 185-198
    • Cox, J.L.1    Cox, B.J.2    Fidanza, V.3    Calhoun, D.H.4
  • 4
    • 1242335574 scopus 로고
    • Covalent structure of biodegradative threonine dehydratase of Escherichia coli: Homology with other dehydratases
    • Datta, P., Goss, T. J., Omnaas, J. R. & Patil, R. V. (1987) Covalent structure of biodegradative threonine dehydratase of Escherichia coli: homology with other dehydratases, Proc. Natl Acad. Sci. USA 84, 393-397.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 393-397
    • Datta, P.1    Goss, T.J.2    Omnaas, J.R.3    Patil, R.V.4
  • 5
    • 0001123209 scopus 로고
    • Nucleotide sequence of the gene for threonine deaminase (ILVI) of Saccharomyces cerevisiae
    • Kielland-Brandt, M. C., Holmberg, S. & Peterson, J. G. L. (1984) Nucleotide sequence of the gene for threonine deaminase (ILVI) of Saccharomyces cerevisiae, Carlsberg Res. Commun. 49, 567-575.
    • (1984) Carlsberg Res. Commun. , vol.49 , pp. 567-575
    • Kielland-Brandt, M.C.1    Holmberg, S.2    Peterson, J.G.L.3
  • 6
    • 0015497795 scopus 로고
    • Inactivation of serine transhydroxymethylase and threonine aldolase activities
    • Akhtar, M. & El-Obeid, H. A. (1972) Inactivation of serine transhydroxymethylase and threonine aldolase activities, Biochim. Biophys. Acta 258, 791-799.
    • (1972) Biochim. Biophys. Acta , vol.258 , pp. 791-799
    • Akhtar, M.1    El-Obeid, H.A.2
  • 7
    • 0015829222 scopus 로고
    • Bacterial threonine aldolase and serine hydroxymethyltransferase enzymes
    • Bell, S. C. & Turner, J. M. (1973) Bacterial threonine aldolase and serine hydroxymethyltransferase enzymes, Biochem. Soc. Trans. 1, 678-681.
    • (1973) Biochem. Soc. Trans. , vol.1 , pp. 678-681
    • Bell, S.C.1    Turner, J.M.2
  • 8
    • 0014773496 scopus 로고
    • Purification and properties of threonine aldolase from Clostridium pasteurianum
    • Dainty, R. H (1970) Purification and properties of threonine aldolase from Clostridium pasteurianum, Biochem. J. 117, 585-592.
    • (1970) Biochem. J. , vol.117 , pp. 585-592
    • Dainty, R.H.1
  • 9
    • 0013525742 scopus 로고
    • Studies on the properties of threonine aldolases
    • Karasek, M. A. & Greenberg, D. M. (1957) Studies on the properties of threonine aldolases, J. Biol. Chem. 227, 191-205.
    • (1957) J. Biol. Chem. , vol.227 , pp. 191-205
    • Karasek, M.A.1    Greenberg, D.M.2
  • 10
    • 0017722979 scopus 로고
    • Bacterial catabolism of threonine. Threonine degradation initiated by L-threonine acetaldehyde-lyase (aldolase) in species of Pseudomonas
    • Bell, S. C. & Turner, J. M. (1977) Bacterial catabolism of threonine. Threonine degradation initiated by L-threonine acetaldehyde-lyase (aldolase) in species of Pseudomonas, Biochem. J. 166, 209-216.
    • (1977) Biochem. J. , vol.166 , pp. 209-216
    • Bell, S.C.1    Turner, J.M.2
  • 11
    • 0014881586 scopus 로고
    • Glycine formation via threonine and serine aldolase. Its interrelation with the pyruvate formate lyase pathway of one-carbon unit synthesis in Clostridium kluyveri
    • Jungermann, K. A., Schmidt, W., Kirchniawy, F. H. Rupprecht, E. H & Thauer, R. K. (1970) Glycine formation via threonine and serine aldolase. Its interrelation with the pyruvate formate lyase pathway of one-carbon unit synthesis in Clostridium kluyveri, Eur. J. Biochem. 16, 424-429.
    • (1970) Eur. J. Biochem. , vol.16 , pp. 424-429
    • Jungermann, K.A.1    Schmidt, W.2    Kirchniawy, F.H.3    Rupprecht, E.H.4    Thauer, R.K.5
  • 12
    • 0022341663 scopus 로고
    • Evidence for L-threonine cleavage and allothreonine formation by different enzymes from Clostridium pasteurianum: Threonine aldolase and serine hydroxymethyltransferase
    • Stöcklein, W. & Schmidt, H.-L. (1985) Evidence for L-threonine cleavage and allothreonine formation by different enzymes from Clostridium pasteurianum: threonine aldolase and serine hydroxymethyltransferase, Biochem. J. 232, 621-622.
    • (1985) Biochem. J. , vol.232 , pp. 621-622
    • Stöcklein, W.1    Schmidt, H.-L.2
  • 13
    • 0015132277 scopus 로고
    • L-Threonine acetaldehydelyase in a strain of Bacillus subtilis
    • Willetts, A. J. & Turner, J. M. (1971) L-Threonine acetaldehydelyase in a strain of Bacillus subtilis, Biochim. Biophys. Acta 252, 105-110.
    • (1971) Biochim. Biophys. Acta , vol.252 , pp. 105-110
    • Willetts, A.J.1    Turner, J.M.2
  • 14
    • 0015497816 scopus 로고
    • Threonine aldolase from Candida humicola. II. Purification, crystallization and properties
    • Kumagai, H., Nagate, T., Yoshida, H. & Yamada, H. (1972) Threonine aldolase from Candida humicola. II. Purification, crystallization and properties. Biochim. Biophys. Acta 258, 779-790.
    • (1972) Biochim. Biophys. Acta , vol.258 , pp. 779-790
    • Kumagai, H.1    Nagate, T.2    Yoshida, H.3    Yamada, H.4
  • 15
    • 0001115196 scopus 로고
    • Formation of threonine aldolase by bacteria and yeasts
    • Yamada, H., Kumagai, H., Nagate, T. & Yoshida, H. (1971) Formation of threonine aldolase by bacteria and yeasts, Agric. Biol. Chem. 35, 1340-1345.
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1340-1345
    • Yamada, H.1    Kumagai, H.2    Nagate, T.3    Yoshida, H.4
  • 16
    • 0014490868 scopus 로고
    • Threonine aldolase and allothreonine aldolase in rat liver
    • Riario-Sforza, G., Pagani, R. & Marinello, E. (1969) Threonine aldolase and allothreonine aldolase in rat liver, Eur. J. Biochem. 8, 88-92.
    • (1969) Eur. J. Biochem. , vol.8 , pp. 88-92
    • Riario-Sforza, G.1    Pagani, R.2    Marinello, E.3
  • 17
    • 0022537834 scopus 로고
    • L-Threonine aldolase is not a genuine enzyme in rat liver
    • Yeung, Y. G. (1986) L-Threonine aldolase is not a genuine enzyme in rat liver, Biochem. J. 237, 187-190.
    • (1986) Biochem. J. , vol.237 , pp. 187-190
    • Yeung, Y.G.1
  • 19
    • 0008616697 scopus 로고
    • The preparation of hydroxyphenylserines from benzyloxybenzaldehydes and glycine
    • Bolhofer, W. A. (1954) The preparation of hydroxyphenylserines from benzyloxybenzaldehydes and glycine, J. Am. Chem. Soc. 76, 1322-1326.
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 1322-1326
    • Bolhofer, W.A.1
  • 20
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash, T. (1953) The colorimetric estimation of formaldehyde by means of the Hantzsch reaction, Biochem. J. 55, 416-421.
    • (1953) Biochem. J. , vol.55 , pp. 416-421
    • Nash, T.1
  • 21
    • 0000894177 scopus 로고
    • A1
    • Sneath, P. H. A., Mair, N. S., Sharpe, M. H. & Holt, J. G., eds Williams & Wilkins, Baltiomore
    • A1, in Bergey's manual of systematic bacteriology (Sneath, P. H. A., Mair, N. S., Sharpe, M. H. & Holt, J. G., eds) vol. 2, pp. 1288-1301, Williams & Wilkins, Baltiomore.
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1288-1301
    • Keddie, R.M.1    Collins, M.D.2    Jones, D.3
  • 22
    • 0015243885 scopus 로고
    • Polypeptides of the tail fibres of bacteriophage T4
    • King, J. & Laemmli, U. K. (1971) Polypeptides of the tail fibres of bacteriophage T4. J. Mol. Biol. 62, 465-477.
    • (1971) J. Mol. Biol. , vol.62 , pp. 465-477
    • King, J.1    Laemmli, U.K.2
  • 23
    • 0010581394 scopus 로고
    • Automatic recording apparatus for use in the chromatography of amino acids
    • Spackman, D. H., Stein, W. H. & Moore, S. (1958) Automatic recording apparatus for use in the chromatography of amino acids, Anal. Chem. 30, 1190-1206.
    • (1958) Anal. Chem. , vol.30 , pp. 1190-1206
    • Spackman, D.H.1    Stein, W.H.2    Moore, S.3
  • 24
    • 0001524478 scopus 로고
    • On the determination of cystine as cysteic acid
    • Moore, S. (1963) On the determination of cystine as cysteic acid, J. Biol. Chem. 238, 235-237.
    • (1963) J. Biol. Chem. , vol.238 , pp. 235-237
    • Moore, S.1
  • 25
    • 0017226811 scopus 로고
    • Complete amino acid analysis of proteins from a single hydrolysate
    • Simpson, R. J., Neuberger, M. R. & Liu, T.-Y. (1976) Complete amino acid analysis of proteins from a single hydrolysate, J. Biol. Chem. 251, 1936-1940.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1936-1940
    • Simpson, R.J.1    Neuberger, M.R.2    Liu, T.-Y.3
  • 26
    • 0024365806 scopus 로고
    • Automated enantioseparation of amino acids by derivatization with o-phthalaldehyde and N-acetylated cysteines
    • Brückner, H., Wittner, R. & Godel, R (1989) Automated enantioseparation of amino acids by derivatization with o-phthalaldehyde and N-acetylated cysteines, J. Chromalogr. 476, 73-82.
    • (1989) J. Chromalogr. , vol.476 , pp. 73-82
    • Brückner, H.1    Wittner, R.2    Godel, R.3
  • 27
    • 0001271824 scopus 로고
    • Resolution of amino acid enantiomers by high-performance liquid chromatography using automated pre-column derivatization with a chiral reagent
    • Buck, R. H. & Krummen, K. (1984) Resolution of amino acid enantiomers by high-performance liquid chromatography using automated pre-column derivatization with a chiral reagent, J. Chromatogr. 315, 279-286.
    • (1984) J. Chromatogr. , vol.315 , pp. 279-286
    • Buck, R.H.1    Krummen, K.2
  • 28
    • 0023160460 scopus 로고
    • High-performance liquid chromatographic determination of enantiomeric amino acids and amino alcohols after derivatization with o-phthaldialdehyde and various chiral mercaptans: Application to peptide hydrolysates
    • Buck, R. H. & Krummen, K. (1987) High-performance liquid chromatographic determination of enantiomeric amino acids and amino alcohols after derivatization with o-phthaldialdehyde and various chiral mercaptans: application to peptide hydrolysates, J. Chromatogr. 387, 255-265.
    • (1987) J. Chromatogr. , vol.387 , pp. 255-265
    • Buck, R.H.1    Krummen, K.2
  • 29
    • 0022509023 scopus 로고
    • o-Phthalaldehyde-N-acetyl-L-cysteine as a chiral derivatization reagent for liquid chromatographic optical resolution of amino acid enantiomers and its application to conventional amino acid analysis
    • Nimura, N. & Kinoshita, T. (1986) o-Phthalaldehyde-N-acetyl-L-cysteine as a chiral derivatization reagent for liquid chromatographic optical resolution of amino acid enantiomers and its application to conventional amino acid analysis, J. Chromatogr. 352, 169-177.
    • (1986) J. Chromatogr. , vol.352 , pp. 169-177
    • Nimura, N.1    Kinoshita, T.2
  • 30
    • 0030872722 scopus 로고    scopus 로고
    • Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39
    • Kataoka, M., Wada, M., Nishi, K., Shimizu, S. & Yamada, H. (1997) Purification and characterization of L-allo-threonine aldolase from Aeromonas jandaei DK-39, FEMS Microbiol. Lett. 151, 245-248.
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 245-248
    • Kataoka, M.1    Wada, M.2    Nishi, K.3    Shimizu, S.4    Yamada, H.5
  • 31
    • 0013916457 scopus 로고
    • On the role of pyridoxal 5′-phosphate in phosphorylase. II. Resolution of rabbit muscle phosphorylase b
    • Shaltiel, S., Hedrick, J. L. & Fischer, E. H. (1966) On the role of pyridoxal 5′-phosphate in phosphorylase. II. Resolution of rabbit muscle phosphorylase b, Biochemistry 5, 2108-2116.
    • (1966) Biochemistry , vol.5 , pp. 2108-2116
    • Shaltiel, S.1    Hedrick, J.L.2    Fischer, E.H.3
  • 32
    • 0018160479 scopus 로고
    • Interaction of pyridoxal 5-phosphate with apo-serine hydroxymethyltransferase
    • Jones, C. W. & Priest, D. G. (1978) Interaction of pyridoxal 5-phosphate with apo-serine hydroxymethyltransferase, Biochim. Biophys. Acta 526, 369-374.
    • (1978) Biochim. Biophys. Acta , vol.526 , pp. 369-374
    • Jones, C.W.1    Priest, D.G.2
  • 33
    • 0038134349 scopus 로고
    • Purification and properties of erythro-β-hydroxyaspartate dehydratase from Micrococcus denitrificans
    • Gibbs, R. G. & Morris, J. G. (1965) Purification and properties of erythro-β-hydroxyaspartate dehydratase from Micrococcus denitrificans, Biochem. J. 97, 547-554.
    • (1965) Biochem. J. , vol.97 , pp. 547-554
    • Gibbs, R.G.1    Morris, J.G.2
  • 36
  • 38
    • 0014410177 scopus 로고
    • Serine transhydroxymethylase: Identification as the threonine and allothreonine aldolases
    • Schirch, L. V. & Gross, T. (1968) Serine transhydroxymethylase: identification as the threonine and allothreonine aldolases, J. Biol. Chem. 243, 5651-5655.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5651-5655
    • Schirch, L.V.1    Gross, T.2
  • 40
    • 0024297340 scopus 로고
    • Three-dimensional structure of the tryptophan synthase α2β2 multienzyme complex from Salmonella typhimurium
    • Hyde, C. C., Ahmed, S. A., Padlan, H. A., Miles, E. W. & Davies, D. R. (1988) Three-dimensional structure of the tryptophan synthase α2β2 multienzyme complex from Salmonella typhimurium, J. Biol. Chem. 263, 17857-17871.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17857-17871
    • Hyde, C.C.1    Ahmed, S.A.2    Padlan, H.A.3    Miles, E.W.4    Davies, D.R.5
  • 42
    • 0023656873 scopus 로고
    • X-ray crystallographic studies of the alanine-specific racemase from Bacillus stearothermophilus:overproduction, crystallization, and preliminary characterization
    • Neidhart, D. J., Disterfano, M. D., Tanizawa, K., Soda, K., Walsh, C. T. & Petsko, G. A. (1987) X-ray crystallographic studies of the alanine-specific racemase from Bacillus stearothermophilus:overproduction, crystallization, and preliminary characterization, J. Biol. Chem. 262, 15323-15326.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15323-15326
    • Neidhart, D.J.1    Disterfano, M.D.2    Tanizawa, K.3    Soda, K.4    Walsh, C.T.5    Petsko, G.A.6
  • 43
    • 0023644474 scopus 로고
    • The three-dimensional structure of acarbose bound to glycogen phosphorylase
    • Goldsmith, E. J., Fletterick, R. J. & Withers, S. G. (1987) The three-dimensional structure of acarbose bound to glycogen phosphorylase, J. Biol. Chem. 262, 1449-1455.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1449-1455
    • Goldsmith, E.J.1    Fletterick, R.J.2    Withers, S.G.3
  • 44
    • 0027182377 scopus 로고
    • Dialkylglycine decarboxylase structure: Bifunctional active site and alkali metal sites
    • Toney, M. D., Hohenester, E., Cowan, S. W. & Jansonius, J. N. (1993) Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites. Science 261, 756-759.
    • (1993) Science , vol.261 , pp. 756-759
    • Toney, M.D.1    Hohenester, E.2    Cowan, S.W.3    Jansonius, J.N.4
  • 45
    • 0028885266 scopus 로고
    • Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase
    • Toney, M. D., Hohenester, E., Keller, J. W. & Jansonius, J. N. (1995) Structural and mechanistic analysis of two refined crystal structures of the pyridoxal phosphate-dependent enzyme dialkylglycine decarboxylase, J. Mol. Biol. 245, 151-179.
    • (1995) J. Mol. Biol. , vol.245 , pp. 151-179
    • Toney, M.D.1    Hohenester, E.2    Keller, J.W.3    Jansonius, J.N.4
  • 46
    • 0029144437 scopus 로고
    • Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity
    • Sugio, S., Petsko, G. A., Manning, J. M. Soda, K. & Ringe, D. (1995) Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity, Biochemistry 34, 9661-9669.
    • (1995) Biochemistry , vol.34 , pp. 9661-9669
    • Sugio, S.1    Petsko, G.A.2    Manning, J.M.3    Soda, K.4    Ringe, D.5


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