메뉴 건너뛰기




Volumn 28, Issue 5, 1996, Pages 543-549

A novel cystathionine β-synthase from Panagrellus redivivus (Nematoda)

Author keywords

Activated L serine sulphydrase activity; Cystathionine synthase; Nematodes; Panagrellus redivivus; S (2 hydroxethyl) cysteine; Thioether

Indexed keywords

MAMMALIA; NEMATODA; PANAGRELLUS REDIVIVUS;

EID: 0029889430     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/1357-2725(95)00165-4     Document Type: Article
Times cited : (3)

References (18)
  • 1
    • 0039580419 scopus 로고
    • Synthesis, characterization and reactions of 2′-, 3′-and 5′-(2-bromoethyl)-AMP: Potential affinity labels for nucleotide binding sites in enzymes
    • Bednar R. A. and Colman R. F. (1982) Synthesis, characterization and reactions of 2′-, 3′-and 5′-(2-bromoethyl)-AMP: potential affinity labels for nucleotide binding sites in enzymes. J. Protein Chem. 1. 203-224.
    • (1982) J. Protein Chem. , vol.1 , pp. 203-224
    • Bednar, R.A.1    Colman, R.F.2
  • 2
    • 0021306830 scopus 로고
    • The β-replacement specific pyridoxal phosphate dependent lyases
    • Braunstein A. E. and Goryachenkova E. V. (1984) The β-replacement specific pyridoxal phosphate dependent lyases. Adv. Enzymol. 56, 1-89.
    • (1984) Adv. Enzymol. , vol.56 , pp. 1-89
    • Braunstein, A.E.1    Goryachenkova, E.V.2
  • 3
    • 0015235272 scopus 로고
    • Specificity and some other properties of liver serine sulphydrase: Evidence for its identity with cystathionine β-synthase
    • Braunstein A. E., Goryachenkova E. V., Tolosa E. A., Willhardt I. H. and Yefremova L. L. (1971) Specificity and some other properties of liver serine sulphydrase: evidence for its identity with cystathionine β-synthase. Biochim. Biophys. Acta 242, 247-260.
    • (1971) Biochim. Biophys. Acta , vol.242 , pp. 247-260
    • Braunstein, A.E.1    Goryachenkova, E.V.2    Tolosa, E.A.3    Willhardt, I.H.4    Yefremova, L.L.5
  • 4
    • 0008886404 scopus 로고
    • Graphical determination of the dissociation constants for two substrate enzyme systems
    • Florini J. R. and Vestling C. S. (1957) Graphical determination of the dissociation constants for two substrate enzyme systems. Biochim. Biophys. Acta 25, 575-578.
    • (1957) Biochim. Biophys. Acta , vol.25 , pp. 575-578
    • Florini, J.R.1    Vestling, C.S.2
  • 5
    • 0014951927 scopus 로고
    • Studies on cystathionine synthase of rat liver: Properties of the highly purified enzyme
    • Kashiwamata S. and Greenberg D. M. (1970) Studies on cystathionine synthase of rat liver: properties of the highly purified enzyme. Biochim. Biophys. Acta 212, 488-500.
    • (1970) Biochim. Biophys. Acta , vol.212 , pp. 488-500
    • Kashiwamata, S.1    Greenberg, D.M.2
  • 6
    • 0040171834 scopus 로고
    • Clinical amino acid screening by thin-layer chromatography
    • Lee B. Y. and Thurmon T. F. (1993) Clinical amino acid screening by thin-layer chromatography. LC-GC Int. 5, 40-42.
    • (1993) LC-GC Int. , vol.5 , pp. 40-42
    • Lee, B.Y.1    Thurmon, T.F.2
  • 7
    • 0015934089 scopus 로고
    • An aspergillus nidulans mutant lacking cystathionine β-synthase: Identify of L-serine sulphydrase with cystathionine β -synthase and its distinctness from O-acetyl-L-serine sulphydrase
    • Pieniazek N. J., Stepien P. P. and Paszewski A. (1973) An Aspergillus nidulans mutant lacking cystathionine β-synthase: identify of L-serine sulphydrase with cystathionine β -synthase and its distinctness from O-acetyl-L-serine sulphydrase. Biochim. Biophys. Acta 297, 37-47.
    • (1973) Biochim. Biophys. Acta , vol.297 , pp. 37-47
    • Pieniazek, N.J.1    Stepien, P.P.2    Paszewski, A.3
  • 8
    • 0017390556 scopus 로고
    • A rapid sensitive and versatile assay for protein using Coomassie brilliant blue
    • Sedmak, J. J. and Grossberg, S. E. (1977) A rapid sensitive and versatile assay for protein using Coomassie brilliant blue. Analyt. Biochem. 79, 544-552.
    • (1977) Analyt. Biochem. , vol.79 , pp. 544-552
    • Sedmak, J.J.1    Grossberg, S.E.2
  • 9
    • 0038987656 scopus 로고
    • Purification and properties of cystathionine synthase in the silk worm, Bombyx mori
    • Shinbo H. (1982) Purification and properties of cystathionine synthase in the silk worm, Bombyx mori. Insect Biochem. 12, 571-577.
    • (1982) Insect Biochem. , vol.12 , pp. 571-577
    • Shinbo, H.1
  • 10
    • 0040171809 scopus 로고
    • Preparation and determination of sulphur amino acids and related compounds
    • Edited by Colowick S. P. and Kaplan N. O., Academic Press, New York
    • Stekol J. A. (1957) Preparation and determination of sulphur amino acids and related compounds. In Methods in Enzymology (Edited by Colowick S. P. and Kaplan N. O.), Vol. 3, pp. 578-600. Academic Press, New York.
    • (1957) Methods in Enzymology , vol.3 , pp. 578-600
    • Stekol, J.A.1
  • 11
    • 0000189737 scopus 로고
    • 6 and sulphur amino acid metabolism: Inborn errors, brain function, deficiency and mega vitamin therapy
    • Edited by Dolphin D., Poulson R. and Avramovic O., part B, Wiley, New York
    • 6, Pyridoxal Phosphate: Chemical, Biochemical and Medical Aspects (Edited by Dolphin D., Poulson R. and Avramovic O.), part B, pp. 507-572. Wiley, New York.
    • (1986) 6, Pyridoxal Phosphate: Chemical, Biochemical and Medical Aspects , pp. 507-572
    • Sturman, J.A.1
  • 12
    • 0021848513 scopus 로고
    • L-serine sulphydrase activity in trichomonads
    • Thong K.-W. and Coombs G. H. (1985) L-Serine sulphydrase activity in Trichomonads. IRCS Med. Sci. 13, 495-496.
    • (1985) IRCS Med. Sci. , vol.13 , pp. 495-496
    • Thong, K.-W.1    Coombs, G.H.2
  • 13
    • 0023190215 scopus 로고
    • Trichomonas species: Homocysteine desulphurase and serine sulphydrase activities
    • Thong K.-W. and Coombs G. H. (1987) Trichomonas species: homocysteine desulphurase and serine sulphydrase activities. Exp. Parasit. 63, 143-151.
    • (1987) Exp. Parasit. , vol.63 , pp. 143-151
    • Thong, K.-W.1    Coombs, G.H.2
  • 14
    • 0018583063 scopus 로고
    • Steady state kinetics of reactions catalysed by serine sulphydrase of Saccharomyces cerevisiae
    • Tolosa E. A., Willhardt I. E., Kozlov L. V. and Goryachenkova E. V. (1979) Steady state kinetics of reactions catalysed by serine sulphydrase of Saccharomyces cerevisiae. Biokhimiya 44, 356-360.
    • (1979) Biokhimiya , vol.44 , pp. 356-360
    • Tolosa, E.A.1    Willhardt, I.E.2    Kozlov, L.V.3    Goryachenkova, E.V.4
  • 15
    • 0025953091 scopus 로고
    • Cystathionine β-synthase and γ-cystathionase in helminths
    • Walker J. and Barrett J. (1991) Cystathionine β-synthase and γ-cystathionase in helminths. Parasit. Res. 77, 709-713.
    • (1991) Parasit. Res. , vol.77 , pp. 709-713
    • Walker, J.1    Barrett, J.2
  • 16
    • 0026828013 scopus 로고
    • Biochemical characterisation of the enzyme responsible for 'activated L-serine sulphydrase' activity in nematodes
    • Walker J. and Barrett J. (1992) Biochemical characterisation of the enzyme responsible for 'activated L-serine sulphydrase' activity in nematodes. Exp. Parasit. 74, 205-215.
    • (1992) Exp. Parasit. , vol.74 , pp. 205-215
    • Walker, J.1    Barrett, J.2
  • 17
    • 0027024501 scopus 로고
    • The identification of a variant form of cystathionine β-synthase in nematodes
    • Walker J., Barrett J. and Thong K.-W. (1992) The identification of a variant form of cystathionine β-synthase in nematodes. Exp. Parasit. 75, 415-424.
    • (1992) Exp. Parasit. , vol.75 , pp. 415-424
    • Walker, J.1    Barrett, J.2    Thong, K.-W.3
  • 18
    • 0005499841 scopus 로고
    • Statistical estimations in enzyme kinetics
    • Wilkinson G. N. (1961) Statistical estimations in enzyme kinetics. Biochem. J. 80, 324-332.
    • (1961) Biochem. J. , vol.80 , pp. 324-332
    • Wilkinson, G.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.