Further evidence for an essential histidyl residue at the active site of pig liver 5-aminolevulinic acid dehydratase

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Photoxidation with methylene blue and rose bengal and chemical modification by diethylpyrocarbonate of pig liver 5-aminolevulinic acid dehydratase produced strong inactivation of the enzyme which was concentration dependent. Loss of enzyme activity by both photoxidation and ethoxyformylation was pH...

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Autor principal: Fukuda, H.
Otros Autores: Dopera De Kracoff, Y.E, Inigo, L.E, Paredes, S.R, Ferramola De Sancovich, A.M, Sancovich, H.A, Batlle, A.M.C
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Informa Healthcare 1990
Acceso en línea:Registro en Scopus
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Aporte de:Registro referencial: Solicitar el recurso aquí
Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-0025326164 
024 7 |2 cas  |a Enzyme Inhibitors; Histidine, 71-00-1; Macromolecular Systems; Methylene Blue, 61-73-4; Porphobilinogen Synthase, EC 4.2.1.24; Rose Bengal, 11121-48-5 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a JEIMA 
100 1 |a Fukuda, H. 
245 1 0 |a Further evidence for an essential histidyl residue at the active site of pig liver 5-aminolevulinic acid dehydratase 
260 |b Informa Healthcare  |c 1990 
270 1 0 |m Fukuda, H.; Department of Biochemistry, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pabellhn II 1428, Nuñez, Buenos Aires, Argentina 
506 |2 openaire  |e Política editorial 
504 |a Jordan, P.M., Seehra, J.S., (1980) Chem. Comm., p. 240 
504 |a Jordan, P.M., Seehra, J.S., (1980) FEBS Letters, 114, p. 283 
504 |a Jordan, P.M., Gibbs, P.N.B., (1985) Biochem. J., 277, p. 1015 
504 |a Gibbs, P.N.B., Jordan, P.M., (1986) Biochem. J., 236, p. 447 
504 |a Barnard, G.F., Itoh, R., Hohberger, L.H., Shemin, D., (1977) J. Biol. Chem., 252, p. 8965 
504 |a del Batlle, A.M.C., Stella, A.M., (1978) Int. J. Biochem., 9, p. 861 
504 |a Tsukamoto, I., Yoshinaga, T., Sano, S., (1975) Biochem. Biophys. Res. Commun., 61, p. 294 
504 |a Weil, L., James, S., Buchert, A.R., (1953) Arch. Biochem. Biophys., 46, p. 266 
504 |a Weil, L., Seibles, T.S., (1955) Arch. Biochem. Biophys., S4, p. 368 
504 |a Oster, G., Bellin, J.S., Kimball, R.W., Schrader, M.E., (1959) J. Am. Chem. Soc., 81, p. 5095 
504 |a Ovadi, J., Libor, S., Elödi, P., (1967) Acta Biochim. Biophys. Acad. Sci. Hung., 2, p. 455 
504 |a Mullard, A., Hegyi, G., Horányi, M., (1969) Biochim. Biophys. Acta., 181, p. 184 
504 |a Melchior, W.B., Jr., Fahrney, D., (1970) Biochemistry, 9, p. 251 
504 |a Fukuda, H., Paredes, S.R., Batlle, A.M., Del, C., (1988) Comp. Biochem. Physiol., 91B, p. 285 
504 |a Ray, W.J., Jr., (1967) Meth. Enzymol., 11, p. 490 
504 |a Hoffee, P., Lai, C.Y., Pugh, E.L., Horecker, B.L., (1967) Proc. Natn. Acad. Sci. US.A., 57, p. 107 
504 |a Miles, E.W., (1977) Meth. Enzymol., 41, p. 412 
504 |a Sopena de Kracoff, Y.E., Kartofel, B.M., Ferramola de Sancovich, A.M., Sancovich, H.A., (1989) Anales Asoc. Quim. Arg., 77, p. 185 
504 |a Bellin, J.S., Yankus, C.A., (1967) Arch. Biochem. Biophys., 123, p. 18 
504 |a Westhead, E.W., (1965) Biochemistry, 4, p. 2139 
504 |a McCracken, S.R., Meigen, E.A., (1981) J. Biol. Chem., 256, p. 3945 
504 |a Seehra, J.S., Jordan, P.M., (1981) Eur. J. Biochem., 113, p. 435 
504 |a Abdulwajid, A.W., Wu, F.Y.H., (1986) Biochemistry, 25, p. 8167 
520 3 |a Photoxidation with methylene blue and rose bengal and chemical modification by diethylpyrocarbonate of pig liver 5-aminolevulinic acid dehydratase produced strong inactivation of the enzyme which was concentration dependent. Loss of enzyme activity by both photoxidation and ethoxyformylation was pH and time-dependent and protected by the presence of the substate and competitive inhibitors. The rate of inactivation was directly related to the state of protonation of histidyl groups, the unprotonated from being modified at a much faster rate than the protonated form. Plots of the pseudo-first order rate constants for 5-aminolevulinic acid dehydratase inactivation against pH resulted in typical titration curves showing inflection points at about pH 6.4 for methylene blue and rose bengal and 6.8 for diethylpyrocarbonate providing further and unequivocal evidence for the existence of critical histidyl groups at the active centre of the enzyme. © 1990 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.  |l eng 
536 |a Detalles de la financiación: National Council for Scientific Research 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: Alcira M. del C. Batlle, Horacio Sancovich and Ana M. Ferrarnola de Sancovich holds the post of Scientific Researcher at the Argentina National Research Council (CONICET); Haydee Fukuda and Sergio Paredes thank CONICET for fellowships. 
536 |a Detalles de la financiación: This work was supported by grants from CONICET and the Univeristy of Buenos Aires and is part of the Doctoral Thesis of Haydee Fukuda and Yolanda Sopena de Kracoff submitted to the University of Buenos Aires for their PhD degree. We thank Mrs. L. Lescano for expert technical assistance. 
593 |a Department of Biochemistry, Facultad de Ciencias Exactas y Naturales, Ciudad Universitaria, Pabellhn II 1428, Nuñez, Buenos Aires, Argentina 
690 1 0 |a 5-AMINOLEVULINIC ACID DEHYDRATASE 
690 1 0 |a DIETHYLPYROCARBONATE 
690 1 0 |a HISTIDYL RESIDUES 
690 1 0 |a METHYLENE BLUE 
690 1 0 |a ROSE BENGAL 
690 1 0 |a DIETHYL PYROCARBONATE 
690 1 0 |a HISTIDINE 
690 1 0 |a METHYLENE BLUE 
690 1 0 |a PORPHOBILINOGEN SYNTHASE 
690 1 0 |a ROSE BENGAL 
690 1 0 |a ANIMAL CELL 
690 1 0 |a ARTICLE 
690 1 0 |a ENZYME ACTIVE SITE 
690 1 0 |a ENZYME MODIFICATION 
690 1 0 |a NONHUMAN 
690 1 0 |a PHOTOOXIDATION 
690 1 0 |a SWINE 
690 1 0 |a ANIMAL 
690 1 0 |a BINDING SITES 
690 1 0 |a ENZYME INHIBITORS 
690 1 0 |a HISTIDINE 
690 1 0 |a HYDROGEN-ION CONCENTRATION 
690 1 0 |a KINETICS 
690 1 0 |a LIVER 
690 1 0 |a MACROMOLECULAR SYSTEMS 
690 1 0 |a METHYLENE BLUE 
690 1 0 |a PHOTOCHEMISTRY 
690 1 0 |a PORPHOBILINOGEN SYNTHASE 
690 1 0 |a ROSE BENGAL 
690 1 0 |a SUPPORT, NON-U.S. GOV'T 
690 1 0 |a SWINE 
690 1 0 |a ANIMALIA 
690 1 0 |a SUS SCROFA 
700 1 |a Dopera De Kracoff, Y.E. 
700 1 |a Inigo, L.E. 
700 1 |a Paredes, S.R. 
700 1 |a Ferramola De Sancovich, A.M. 
700 1 |a Sancovich, H.A. 
700 1 |a Batlle, A.M.C. 
773 0 |d Informa Healthcare, 1990  |g v. 3  |h pp. 295-302  |k n. 4  |p J. Enzyme Inhib. Med. Chem.  |x 14756366  |w (AR-BaUEN)CENRE-5562  |t Journal of Enzyme Inhibition and Medicinal Chemistry 
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856 4 0 |u https://doi.org/10.3109/14756369009030378  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_14756366_v3_n4_p295_Fukuda  |y Handle 
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999 |c 61537 

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