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Abstract:

1. 1. The effect of diethylpyrocarbonate (DEP) (0.1-0.35 mM) on the purified pig liver aminolevulic acid dehydratase (ALA-D) containing 0.3 g-atoms Zn/subunit, under different pHs (6.0-7.5), temperature (0-18°C) and time (0-60 min) was studied 2. 2. Three histidyl residues/subunit were modified by DEP (0.2 mM, pH 6.8), but activity was completely lost after the first one had reacted, indicating the presence of one histidine residue essential for ALA-D catalysis. Reactivation by treatment with hydroxylamine (0.7 mM, pH 7.0) confirmed that only histidine and no other nucleophile amino acids were directly involved in DEP inhibition. 3. 3. Zn ions (0.5 mM) and the substrate ALA (5-10 mM) protected against DEP inactivation, protection was dependent on pH. 4. 4. Sn, Se, Hg, Cd, Mn, Co and Pb (0.01-0.1 mM) did not significantly protect ALA-D against inactivation. 5. 5. It is concluded that the substrate and Zn binding sites and the essential histidyl residues are in close proximity in the active center. It is proposed that in the catalytic synthesis of porphobilinogen from ALA, histidine groups have the specific role of transporting protons from the aqueous media to a hydrophobic active site. © 1988.

Registro:

Documento: Artículo
Título:Active site histidine in pig liver aminolevulic acid dehydratase modified by diethylpyrocarbonate and protected by Zn2+ Ions
Autor:Fukuda, H.; Paredes, S.R.; del C. Batlle, A.M.
Filiación:Centro de Investigaciones sobre Porfirinas y Porfirias-CIPYP (CONICET-FCEyNn, UBA), Ciudad Universitaria, Pabellon II, 2o Piso, 1428 Nuñez Buenos Aires, Argentina
Palabras clave:diethyl pyrocarbonate; histidine; metal; porphobilinogen synthase; zinc; animal; article; binding site; enzymology; in vitro study; liver; metabolism; pH; swine; Animal; Binding Sites; Diethyl Pyrocarbonate; Histidine; Hydrogen-Ion Concentration; In Vitro; Liver; Metals; Porphobilinogen Synthase; Support, Non-U.S. Gov't; Swine; Zinc
Año:1988
Volumen:91
Número:2
Página de inicio:285
Página de fin:291
DOI: http://dx.doi.org/10.1016/0305-0491(88)90144-7
Título revista:Comparative Biochemistry and Physiology -- Part B: Biochemistry and
ISSN:03050491
CAS:diethyl pyrocarbonate, 1609-47-8; histidine, 645-35-2, 7006-35-1, 71-00-1; porphobilinogen synthase, 9036-37-7; zinc, 7440-66-6; Diethyl Pyrocarbonate, 1609-47-8; Histidine, 71-00-1; Metals; Porphobilinogen Synthase, EC 4.2.1.24; Zinc, 7440-66-6
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v91_n2_p285_Fukuda

Referencias:

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Citas:

---------- APA ----------
Fukuda, H., Paredes, S.R. & del C. Batlle, A.M. (1988) . Active site histidine in pig liver aminolevulic acid dehydratase modified by diethylpyrocarbonate and protected by Zn2+ Ions. Comparative Biochemistry and Physiology -- Part B: Biochemistry and, 91(2), 285-291.
http://dx.doi.org/10.1016/0305-0491(88)90144-7
---------- CHICAGO ----------
Fukuda, H., Paredes, S.R., del C. Batlle, A.M. "Active site histidine in pig liver aminolevulic acid dehydratase modified by diethylpyrocarbonate and protected by Zn2+ Ions" . Comparative Biochemistry and Physiology -- Part B: Biochemistry and 91, no. 2 (1988) : 285-291.
http://dx.doi.org/10.1016/0305-0491(88)90144-7
---------- MLA ----------
Fukuda, H., Paredes, S.R., del C. Batlle, A.M. "Active site histidine in pig liver aminolevulic acid dehydratase modified by diethylpyrocarbonate and protected by Zn2+ Ions" . Comparative Biochemistry and Physiology -- Part B: Biochemistry and, vol. 91, no. 2, 1988, pp. 285-291.
http://dx.doi.org/10.1016/0305-0491(88)90144-7
---------- VANCOUVER ----------
Fukuda, H., Paredes, S.R., del C. Batlle, A.M. Active site histidine in pig liver aminolevulic acid dehydratase modified by diethylpyrocarbonate and protected by Zn2+ Ions. 1988;91(2):285-291.
http://dx.doi.org/10.1016/0305-0491(88)90144-7