메뉴 건너뛰기




Volumn 119, Issue 4, 1996, Pages 690-696

A novel phenylserine dehydratase from Pseudomonas pickettii PS22: Purification, characterization, and sequence of its phosphopyridoxyl peptide

Author keywords

Phenylserine deaminase; Phenylserine dehydratase; Phosphopyridoxyl peptide; Pseudomonas pickettii; Pyridoxal 8' phosphate

Indexed keywords

4 CHLOROMERCURIBENZOIC ACID; BACTERIAL ENZYME; ENZYME INHIBITOR; HYDROLYASE; HYDROXYLAMINE; MERCUROUS CHLORIDE; MONOMER; PHENYLHYDRAZINE; PHENYLSERINE; PYRIDOXAL 5 PHOSPHATE; SERINE; THREONINE;

EID: 0029944859     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021297     Document Type: Article
Times cited : (6)

References (37)
  • 1
    • 0345146688 scopus 로고
    • Enzymatic cleavage and synthesis of L-threo-β-phenylserine and L-erythro-β-phenylserine
    • Bruns, F.H. and Fiedler, L. (1958) Enzymatic cleavage and synthesis of L-threo-β-phenylserine and L-erythro-β-phenylserine. Nature 181, 1533-1534
    • (1958) Nature , vol.181 , pp. 1533-1534
    • Bruns, F.H.1    Fiedler, L.2
  • 2
    • 0020005825 scopus 로고
    • Serine hydroxymethyltransferase
    • Schirch, L. (1982) Serine hydroxymethyltransferase. Adv. Enzymol. 53, 83-112
    • (1982) Adv. Enzymol. , vol.53 , pp. 83-112
    • Schirch, L.1
  • 3
    • 15844413566 scopus 로고
    • The enzymatic conversion of L-threo- and L-erythro-β-phenylserine to D- and L-mandelic acid
    • Fones, W.S. (1952) The enzymatic conversion of L-threo- and L-erythro-β-phenylserine to D- and L-mandelic acid. Arch. Biochem. Biophys. 36, 486-487
    • (1952) Arch. Biochem. Biophys. , vol.36 , pp. 486-487
    • Fones, W.S.1
  • 5
    • 85007753987 scopus 로고
    • Occurrence of an inducible phenylserine dehydratase in Pseudomonas pickettii PS22 isolated from soil
    • Misono, H., Okuda, H., Shin, K., Nagata, S., and Nagasaki, S. (1995) Occurrence of an inducible phenylserine dehydratase in Pseudomonas pickettii PS22 isolated from soil. Biosci. Biotechnol. Biochem. 59, 339-340
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 339-340
    • Misono, H.1    Okuda, H.2    Shin, K.3    Nagata, S.4    Nagasaki, S.5
  • 6
    • 0003828322 scopus 로고
    • Illustrative synthesis of erythro-phenylserine
    • (Greenstein, J.P. and Winitz, M., eds.) John Wiley and Sons, New York
    • Greenstein, J.P. and Winitz, M. (1961) Illustrative synthesis of erythro-phenylserine in Chemistry of the Amino Acids (Greenstein, J.P. and Winitz, M., eds.) Vol. 3, p. 2603, John Wiley and Sons, New York
    • (1961) Chemistry of the Amino Acids , vol.3 , pp. 2603
    • Greenstein, J.P.1    Winitz, M.2
  • 7
    • 0343717461 scopus 로고
    • The specific binding of pyridoxal 5′-phosphate to bovine plasma albumin
    • Dempsey, W.B. and Christensen, H.N. (1962) The specific binding of pyridoxal 5′-phosphate to bovine plasma albumin. J. Biol. Chem. 237, 1113-1120
    • (1962) J. Biol. Chem. , vol.237 , pp. 1113-1120
    • Dempsey, W.B.1    Christensen, H.N.2
  • 9
    • 78651153791 scopus 로고
    • Disc electrophoresis II. Method and application to human serum proteins
    • Davis, B.J. (1964) Disc electrophoresis II. Method and application to human serum proteins. Ann. N.Y. Acad. Sci. 121, 404-427
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 10
    • 0014963121 scopus 로고
    • Threonine deaminase: A novel activity stain on polyacrylamide gels
    • Feldberg, R.S. and Datta, P. (1970) Threonine deaminase: A novel activity stain on polyacrylamide gels. Science 170, 1414-1416
    • (1970) Science , vol.170 , pp. 1414-1416
    • Feldberg, R.S.1    Datta, P.2
  • 11
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K. and Osborn, M. (1969) The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406-4412
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 12
    • 0001515809 scopus 로고
    • The enzymatic oxidation of pyridoxine and pyridoxamine phosphates
    • Wada, H. and Snell, E.E. (1961) The enzymatic oxidation of pyridoxine and pyridoxamine phosphates. J. Biol. Chem. 236, 2089-2095
    • (1961) J. Biol. Chem. , vol.236 , pp. 2089-2095
    • Wada, H.1    Snell, E.E.2
  • 13
    • 0011723681 scopus 로고
    • The reaction of pyridoxal 5-phosphate with cyanide and its analytical use
    • Bonavita, V. (1960) The reaction of pyridoxal 5-phosphate with cyanide and its analytical use. Arch. Biochem. Biophys. 88, 366-372
    • (1960) Arch. Biochem. Biophys. , vol.88 , pp. 366-372
    • Bonavita, V.1
  • 14
    • 0014501272 scopus 로고
    • Inhibition by pyridoxal-phosphate of glyceraldehyde-3-phosphate dehydrogenase
    • Ronchi, S., Zapponi, M.C., and Ferri, G. (1969) Inhibition by pyridoxal-phosphate of glyceraldehyde-3-phosphate dehydrogenase. Eur. J. Biochem. 8, 325 331
    • (1969) Eur. J. Biochem. , vol.8 , pp. 325-331
    • Ronchi, S.1    Zapponi, M.C.2    Ferri, G.3
  • 16
    • 0000505226 scopus 로고
    • A crystalline enzyme that cleaves homoserine and cystathionine
    • Matsuo, Y. and Greenberg, D.M. (1959) A crystalline enzyme that cleaves homoserine and cystathionine. J. Biol. Chem. 234, 507-515
    • (1959) J. Biol. Chem. , vol.234 , pp. 507-515
    • Matsuo, Y.1    Greenberg, D.M.2
  • 17
    • 0014010352 scopus 로고
    • Crystalline D-serine dehydrase
    • Labow, R. and Robinson, W.G. (1966) Crystalline D-serine dehydrase. J. Biol. Chem. 241, 1239-1243
    • (1966) J. Biol. Chem. , vol.241 , pp. 1239-1243
    • Labow, R.1    Robinson, W.G.2
  • 18
    • 0027674952 scopus 로고
    • Cofactor identification of threonine-serine dehydratase from sheep liver
    • Tong, H. and Davis, L. (1993) Cofactor identification of threonine-serine dehydratase from sheep liver. Protein Express. Purif. 4, 438-444
    • (1993) Protein Express. Purif. , vol.4 , pp. 438-444
    • Tong, H.1    Davis, L.2
  • 21
    • 0015541850 scopus 로고
    • Threonine deaminases
    • Umbarger, H.E. (1973) Threonine deaminases. Adv. Enzymol. 37, 349-395
    • (1973) Adv. Enzymol. , vol.37 , pp. 349-395
    • Umbarger, H.E.1
  • 22
    • 0027247728 scopus 로고
    • Bacterial L-serine dehydratases: A new family of enzymes containing iron-sulfur clusters
    • Grabowski, R., Hofmeister, A.E.M., and Buckel, W. (1993) Bacterial L-serine dehydratases: A new family of enzymes containing iron-sulfur clusters. TIBS 18, 297-300
    • (1993) TIBS , vol.18 , pp. 297-300
    • Grabowski, R.1    Hofmeister, A.E.M.2    Buckel, W.3
  • 23
    • 0023773362 scopus 로고
    • Isolation and nucleotide sequence of the cDN a for rat liver serine dehydratase mRNA and structures of the 5′ and 3′ flanking regions of the serine dehydratase gene
    • Ogawa, H., Miller, D.A., Dunn, T., Su, Y., Burcham, J.M., Peraino, C., Fujioka, M., Babcock, K., and Pitot, H.C. (1988) Isolation and nucleotide sequence of the cDN A for rat liver serine dehydratase mRNA and structures of the 5′ and 3′ flanking regions of the serine dehydratase gene. Proc. Natl. Acad. Sci. USA 85, 5809-5813
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5809-5813
    • Ogawa, H.1    Miller, D.A.2    Dunn, T.3    Su, Y.4    Burcham, J.M.5    Peraino, C.6    Fujioka, M.7    Babcock, K.8    Pitot, H.C.9
  • 24
    • 0024459160 scopus 로고
    • Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources
    • Ogawa, H., Gomi, T., Konishi, K., Date, T., Nakashima, H., Nose, K., Matsuda, Y., Peraino, C., Pitot, H.C., and Fujioka, M. (1989) Human liver serine dehydratase. cDNA cloning and sequence homology with hydroxyamino acid dehydratases from other sources. J. Biol. Chem. 264, 15818-15823
    • (1989) J. Biol. Chem. , vol.264 , pp. 15818-15823
    • Ogawa, H.1    Gomi, T.2    Konishi, K.3    Date, T.4    Nakashima, H.5    Nose, K.6    Matsuda, Y.7    Peraino, C.8    Pitot, H.C.9    Fujioka, M.10
  • 25
    • 0023627141 scopus 로고
    • The complete nucleotide sequence of the ilvGMEOA cluster of Escherichia coli K-12
    • Cox, J.L., Cox, B.J., Fidanza, V., and Calhoun, D.H. (1987) The complete nucleotide sequence of the ilvGMEOA cluster of Escherichia coli K-12. Gene 56, 185-198
    • (1987) Gene , vol.56 , pp. 185-198
    • Cox, J.L.1    Cox, B.J.2    Fidanza, V.3    Calhoun, D.H.4
  • 26
    • 1242335574 scopus 로고
    • Covalent structure of biodegradative threonine dehydratase of Escherichia coli: Homology with other dehydratases
    • Datta, P., Goss, T.J., Omnaas, J.R., and Patil, E.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, E.V.4
  • 27
    • 0022379490 scopus 로고
    • Molecular cloning and expression of the biodegradative threonine dehydratase gene (tdc) of Escherichia coli K12
    • Goss, T.J. and Datta, P. (1985) Molecular cloning and expression of the biodegradative threonine dehydratase gene (tdc) of Escherichia coli K12. Mol. Gen. Genet. 201, 308-314
    • (1985) Mol. Gen. Genet. , vol.201 , pp. 308-314
    • Goss, T.J.1    Datta, P.2
  • 28
    • 0026841345 scopus 로고
    • Cloning and overproduction of biodegradative threonine deaminase from Escherichia coli W strain
    • Hirose, K., Fujita, M., Takeuchi, M., Yumoto, N., Tokushige, M., and Kawata, Y. (1992) Cloning and overproduction of biodegradative threonine deaminase from Escherichia coli W strain. Biotechnol. Appl. Biochem. 15, 134-141
    • (1992) Biotechnol. Appl. Biochem. , vol.15 , pp. 134-141
    • Hirose, K.1    Fujita, M.2    Takeuchi, M.3    Yumoto, N.4    Tokushige, M.5    Kawata, Y.6
  • 30
    • 0026621920 scopus 로고
    • Functional and structural analyses of threonine dehydratase from Corynebacterium glutamicum
    • Möckel, B., Eggeling, L., and Sahm, H. (1992) Functional and structural analyses of threonine dehydratase from Corynebacterium glutamicum. J. Bacteriol. 174, 8065-8072
    • (1992) J. Bacteriol. , vol.174 , pp. 8065-8072
    • Möckel, B.1    Eggeling, L.2    Sahm, H.3
  • 31
    • 0023900262 scopus 로고
    • Analysis of the functional domains of biosynthetic threonine deaminase by comparison of the amino acid sequences of three wild-type alleles to the amino acid sequence of biodegradative threonine deaminase
    • Taillon, B.E., Little, R., and Lawther, R.P. (1988) Analysis of the functional domains of biosynthetic threonine deaminase by comparison of the amino acid sequences of three wild-type alleles to the amino acid sequence of biodegradative threonine deaminase. Gene 63, 245-252
    • (1988) Gene , vol.63 , pp. 245-252
    • Taillon, B.E.1    Little, R.2    Lawther, R.P.3
  • 32
    • 0019815968 scopus 로고
    • Sequence of Escherichia coli D-serine dehydratase. Location of the pyridoxal-phosphate binding site
    • Schiltz, E. and Schmitt, W. (1981) Sequence of Escherichia coli D-serine dehydratase. Location of the pyridoxal-phosphate binding site. FEBS Lett. 134, 57-62
    • (1981) FEBS Lett. , vol.134 , pp. 57-62
    • Schiltz, E.1    Schmitt, W.2
  • 33
    • 84990684069 scopus 로고
    • Identification and primary structure of an active site peptide of Escherichia coli biodegradative threonine dehydratase
    • Pettigrew, D.W. and Wagner, R.M. (1986) Identification and primary structure of an active site peptide of Escherichia coli biodegradative threonine dehydratase. Biochem. Arch. 2, 215-221
    • (1986) Biochem. Arch. , vol.2 , pp. 215-221
    • Pettigrew, D.W.1    Wagner, R.M.2
  • 34
    • 0024968433 scopus 로고
    • The peptide sequences near the bound pyridoxal phosphate are conserved in serine dehydratase from rat liver, and threonine dehydratases from yeast and Escherichia coli
    • Ogawa, H., Konishi, K., and Fujioka, M. (1989) The peptide sequences near the bound pyridoxal phosphate are conserved in serine dehydratase from rat liver, and threonine dehydratases from yeast and Escherichia coli. Biochim. Biophys. Acta 996, 139-141
    • (1989) Biochim. Biophys. Acta , vol.996 , pp. 139-141
    • Ogawa, H.1    Konishi, K.2    Fujioka, M.3
  • 35
    • 0026695339 scopus 로고
    • Serine and threonine catabolism in Saccharomyces cerevisiae: The CHA1 polypeptide is homologous with other serine and threonine dehydratases
    • Bornæs, C., Petersen, J.G.L., and Holmberg, S. (1992) Serine and threonine catabolism in Saccharomyces cerevisiae: The CHA1 polypeptide is homologous with other serine and threonine dehydratases. Genetics 131, 531-539
    • (1992) Genetics , vol.131 , pp. 531-539
    • Bornæs, C.1    Petersen, J.G.L.2    Holmberg, S.3
  • 36
    • 0023771138 scopus 로고
    • D-Serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants
    • Marceau, M., McFall, E., Lewis, S.D., and Shafer, J.A. (1988) D-Serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants. J. Biol. Chem. 263, 16926-16933
    • (1988) J. Biol. Chem. , vol.263 , pp. 16926-16933
    • Marceau, M.1    McFall, E.2    Lewis, S.D.3    Shafer, J.A.4
  • 37
    • 0028044574 scopus 로고
    • Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Regio-specific α, β, and γ families
    • Alexander, F.W., Sandmeier, E., Mehta, P.K., and Christen, P. (1994) Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Regio-specific α, β, and γ families. Eur. J. Biochem. 219, 953-960
    • (1994) Eur. J. Biochem. , vol.219 , pp. 953-960
    • Alexander, F.W.1    Sandmeier, E.2    Mehta, P.K.3    Christen, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.