Navegar

Colección

Datos Estadísticas

Artículo

Sopena De Kracoff, Y.E.; de Sancovich, A.M.F.; Sancovich, H.A. "Evidence of an essential lysine in pig liver 5-aminolevulinic acid dehydratase" (1995) International Journal of Biochemistry and Cell Biology. 27(12):1331-1339
Estamos trabajando para incorporar este artículo al repositorio
Consulte el artículo en la página del editor
Consulte la política de Acceso Abierto del editor

Abstract:

5-Aminolevulinic acid dehydratase catalyses the self condensation between two molecules of 5-aminolevulinic acid, via a Schiff base, in which a lysine residue at its active site is proposed to be involved. The aim of the work was to further clarify the mechanism of this step in porphobilinogen biosynthesis. 5-Aminolevulinic acid dehydratase was purified 230-fold from pig liver, ε-Aminolysil residues were identified by treating the enzyme with pyridoxal 5-phosphate. Schiff bases formed between either the substrate or pyridoxal 5-phosphate and the enzyme were stabilized by NaBH4 reduction. Levulinate and pyruvate acted as competitive enzyme inhibitors. Pyridoxal 5-phosphate but not pyridoxamine 5-phosphate reversibly inhibited the enzyme activity, in a competitive fashion (Ki = 0.12 mM). After NaBH4 treatment this inhibition became irreversible. The amount of labelled substrate bound to the enzyme after NaBH4 reduction decreased in the presence of either pyridoxal 5-phosphate, levulinate or pyruvate. Enzyme elution profiles from Sephacryl S-300 showed that NaBH4 treatment (1) in absence of substrate, did not induce any change on the enzyme, eluting as a typical 5-aminolevulinic acid dehydratase single peak (Mw 280,000), which overlapped with that of the enzyme activity; and (2) in the presence of labelled 5-aminolevulinate, had an additional peak eluting with a Mw of 140,000, without enzyme activity. This peak coincides in shape and elution volume with the radioactive one. These data suggest that pyruvate regulates pig liver 5-aminolevulinic acid dehydratase activity in vivo and that during catalysis, a tetrameric structure forms the enzyme-substrate complex. The results support the involvement of a critical ε-aminolysil group at the active site of the enzyme. © 1995 Elsevier Science Ltd.

Registro:

Documento: Artículo
Título:Evidence of an essential lysine in pig liver 5-aminolevulinic acid dehydratase
Autor:Sopena De Kracoff, Y.E.; de Sancovich, A.M.F.; Sancovich, H.A.
Filiación:Departmento de Quimica Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellon II, Nunez, 1428 Buenos Aires, Argentina
Palabras clave:5-Aminolevulinic acid dehydratase; Active site residues inhibition; Glucose effect; Lysine residues; Pyridoxal 5-phosphate; porphobilinogen synthase; amino acid sequence; animal tissue; article; controlled study; enzyme active site; enzyme analysis; enzyme purification; liver; nonhuman; swine; Animal; Enzyme Inhibitors; Kinetics; Levulinic Acids; Liver; Lysine; Models, Molecular; Porphobilinogen; Porphobilinogen Synthase; Pyridoxal Phosphate; Pyridoxamine; Pyruvates; Pyruvic Acid; Support, Non-U.S. Gov't; Swine
Año:1995
Volumen:27
Número:12
Página de inicio:1331
Página de fin:1339
DOI: http://dx.doi.org/10.1016/1357-2725(95)00097-9
Título revista:International Journal of Biochemistry and Cell Biology
Título revista abreviado:Int. J. Biochem. Cell Biol.
ISSN:13572725
CODEN:IJBBF
CAS:porphobilinogen synthase, 9036-37-7; Enzyme Inhibitors; levulinic acid, 123-76-2; Levulinic Acids; Lysine, 56-87-1; Porphobilinogen Synthase, EC 4.2.1.24; Porphobilinogen, 487-90-1; Pyridoxal Phosphate, 54-47-7; pyridoxamine phosphate, 529-96-4; Pyridoxamine, 85-87-0; Pyruvates; Pyruvic Acid, 127-17-3
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13572725_v27_n12_p1331_SopenaDeKracoff

Referencias:

  • Barnard, Itoh, Hohberger, Shemin, Mechanism of porphobilinogen synthase (1977) Possible role of essential thiol groups, 252, pp. 8965-8974. , J. Biol. Chem
  • Batlle A.M. del, Stella, Delta aminolaevulinate dehydratase (1978) Its mechanism of action, 9, pp. 861-864. , Int. J. Biochem
  • Bleile, Jameson, Harrison, Inactivation of porcine heart cytoplasmic malate dehydrogenase by pyridoxal 5 phosphate (1976) J. Biol. Chem., 251, pp. 6304-6307
  • Chen, Engel, Modification of pig M4 lactate dehydrogenase by pyridoxal 5 phosphate (1975) Demonstration of an essential lysine residue, 149, pp. 107-113. , Biochem. J
  • Fasella, Pyridoxal phosphate (1967) A. Rev. Biochem., 36, pp. 185-210
  • Fukuda, Sopena de Kracoff, Iñigo, Paredes, Ferramola de Sancovich, Sancovich, Batlle A.M. del, Further evidence for an essential histidyl residue at the active site of pig liver 5-aminolevulinic acid dehydratase (1990) J. Enzyme Inhibition, 3, pp. 295-302
  • Gibbs, Jordan, Identification of lysine at the active site of human 5 aminolevulinate dehydratase (1986) Biochem. J., 236, pp. 447-451
  • Hart, Battersby, Purification and properties of uroporphyrinogen III synthase (cosynthetase) from Euglena gracilis (1985) Biochem. J., 232, pp. 151-160
  • Hayashi, Wada, Yoshimura, Esaki, Soda, Recent topics in pyridoxal 5-phosphate enzyme studies (1990) A. Rev. Biochem., 59, pp. 87-110
  • Jaffe, Abrams, Kaempfen, Harris, Jr, 5-Chlorolevulinate modification of porphobilinogen synthase identifies a potential role for the catalytic zinc (1992) Biochemistry, 31, pp. 2113-2123
  • Jordan, Gibbs, Mechanism of action of 5-aminolaevulinate dehydratase from human erythrocytes (1985) Biochem. J., 227, pp. 1015-1020
  • Jordan, Sheera, Mechanism of action of 5 aminolevulinic dehydratase stepwise order of addition of the two molecules of 5 aminolevulinic acid in the enzymatic synthesis of porphobilinogen (1980) Journal of the Chemical Society, Chemical Communications, pp. 240-242
  • Jordan, Sheera, 13C NMR as a probe for the study of enzyme-catalyzed reactions (1980) Mechanism of action of 5 aminolevulinic acid dehydratase, 114, pp. 283-286. , FEBS Lett
  • Lowry, Rosenbrough, Farr, Randall, Protein measurement with the Folin phenol reagent (1951) J. Biol. Chem., 193, pp. 265-275
  • Maralihalli, Bhagwat, Interaction of pyridoxal phosphate with the amino groups at the active site of 5 aminolevulinic acid dehydratase in maize (1985) J. Biosci., 7, pp. 359-364
  • Moore, Labbe, A quantitative assay for urinary porphobilinogen (1964) Clin. Chem., 10, pp. 1105-1111
  • Nandi, Shemin, δ Aminolevulinic acid dehydratase of Rhodopseudomonas spheroides (1968) J. Biol. Chem., 243, pp. 1236-1242
  • Shemin, δ Aminolevulinic acid dehydratase (1972) The Enzymes, 7, pp. 323-337. , P. Boyer, 3rd edn, Academic Press, Dresden-Leipzig
  • Shemin, 5-aminolevulinic acid dehydratase: structure, function and mechanism (1976) Phil. Trans. R. Soc. Lond. B, 273, pp. 109-115
  • Sopena de Kracoff, Kartofel, Ferramola de Sancovich, Sancovich, Pig liver 5-aminolevulinic dehydratase (1989) Purification, properties and aminoacid residues comprise within its active site, 77, pp. 185-195. , An. Asoc. Quim. Argent
  • Tschudy, Hess, Frykholm, Inhibition of δ-aminolevulinic acid dehydratase by 4,6dioxoheptanoic acid (1981) J. Biol. Chem., 256, pp. 9915-9923
  • Tsukamoto, Yoshinaga, Sano, Evidence for histidine as another functional group of δ aminolevulinic acid dehydratase from beef liver (1975) Biochem. biophys. Res. Commun., 67, pp. 294-300
  • Wimmer, Mo, Sawyers, Harrison, Biphasic inactivation of porcine heart mitochondrial malate dehydrogenase by pyridoxal 5 phosphate (1975) J. Biol. Chem., 250, pp. 710-715
  • Wu, Shemin, Richards, Williams, The quaternary structure of δ aminolevulinic acid dehydratase from bovine liver (1974) Proc. Nat. Acad. Sci. U.S.A., 69, pp. 2585-2588

Citas:

---------- APA ----------
Sopena De Kracoff, Y.E., de Sancovich, A.M.F. & Sancovich, H.A. (1995) . Evidence of an essential lysine in pig liver 5-aminolevulinic acid dehydratase. International Journal of Biochemistry and Cell Biology, 27(12), 1331-1339.
http://dx.doi.org/10.1016/1357-2725(95)00097-9
---------- CHICAGO ----------
Sopena De Kracoff, Y.E., de Sancovich, A.M.F., Sancovich, H.A. "Evidence of an essential lysine in pig liver 5-aminolevulinic acid dehydratase" . International Journal of Biochemistry and Cell Biology 27, no. 12 (1995) : 1331-1339.
http://dx.doi.org/10.1016/1357-2725(95)00097-9
---------- MLA ----------
Sopena De Kracoff, Y.E., de Sancovich, A.M.F., Sancovich, H.A. "Evidence of an essential lysine in pig liver 5-aminolevulinic acid dehydratase" . International Journal of Biochemistry and Cell Biology, vol. 27, no. 12, 1995, pp. 1331-1339.
http://dx.doi.org/10.1016/1357-2725(95)00097-9
---------- VANCOUVER ----------
Sopena De Kracoff, Y.E., de Sancovich, A.M.F., Sancovich, H.A. Evidence of an essential lysine in pig liver 5-aminolevulinic acid dehydratase. Int. J. Biochem. Cell Biol. 1995;27(12):1331-1339.
http://dx.doi.org/10.1016/1357-2725(95)00097-9