Rat harderian gland porphobilinogen deaminase: Characterization studies and regulatory action of protoporphyrin IX

Properties of purified porphobilinogen deaminase (PBG-D; EC 4.3.1.8) from rat harderian gland are here presented. The enzyme behaves as a monomer of M(r) 38 ± 2 kDa and is optimally active at pH 8.0-8.2. Its activation energy, determined by an Arrhenius plot, is 76.1 kJ/mol. Initial velocity studies...

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Autor principal: Cardalda, C.A
Otros Autores: Juknat, A.A, Princ, F.G, Batlle, A.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Academic Press Inc. 1997
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-0031282308 
024 7 |2 cas  |a 5,5' dithiobis(2 nitrobenzoic acid), 69-78-3; cysteine, 4371-52-2, 52-89-1, 52-90-4; n ethylmaleimide, 128-53-0; porphobilinogen deaminase, 9036-47-9, 9074-91-3; protoporphyrin, 553-12-8; uroporphyrin, 18273-06-8, 26316-36-9, 553-18-4, 607-14-7 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a ABBIA 
100 1 |a Cardalda, C.A. 
245 1 0 |a Rat harderian gland porphobilinogen deaminase: Characterization studies and regulatory action of protoporphyrin IX 
260 |b Academic Press Inc.  |c 1997 
270 1 0 |m Batlle, A.Viamonte 1881, 10 Piso, 1656 Buenos Aires, Argentina; email: cipyp@alad.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a Properties of purified porphobilinogen deaminase (PBG-D; EC 4.3.1.8) from rat harderian gland are here presented. The enzyme behaves as a monomer of M(r) 38 ± 2 kDa and is optimally active at pH 8.0-8.2. Its activation energy, determined by an Arrhenius plot, is 76.1 kJ/mol. Initial velocity studies showed a linear progress curve for uroporphyringen I formation and a hyperbolic dependence of the initial rate on substrate concentration, indicating the existence of a sequential displacement mechanism. Apparent kinetic constants, K(m) and V(m), calculated at 37°C and pH 8.0 were 1.1 μM and 170 pmol/min mg, respectively. The pH dependence of the apparent kinetic parameters revealed the ionization of residues with pK(A)/(ES) and pK(B)/(ES) of 7.4 ± 0.1 and 8.6 ± 0.1, respectively, and a pK(E) value of 8.0 ± 0.1. Incubation of PBG-D with 5.0 mM N-ethylmaleimide and 5.0 mM 5,5'- dithiobis(2-nitrobenzoic acid) at pH 8.0 led to inhibitions of 70 and 50%, respectively. The effect of pH, as well as the effect of thiol reagents, on enzyme activity strongly suggests the involvement of cysteine residue(s) in the mechanism of uroporphyrinogen I biosynthesis, in both the catalytic reaction and the substrate binding. Rat harderian gland PBG-D activity decreased with increasing concentrations of protoporphyrin IX, reaching a 40% inhibition at the in vivo concentration of the porphyrin and 7 μM PBG. Even at saturating concentrations of substrate, inhibition by protoporphyrin was not completely reversed. So, accumulated porphyrin may act as an regulator of PBG-D activity in rat harderian gland.  |l eng 
593 |a Ctro. de Invest. Sobre Porfirinas Y., Departamento de Quimica Biologica, Univ. de Buenos Aires Cd. Univ., 1428 Buenos Aires, Argentina 
690 1 0 |a CYSTEINE RESIDUE(S) 
690 1 0 |a PORPHOBILINOGEN DEAMINASE 
690 1 0 |a PORPHOBILINOGEN DEAMINASE REGULATION 
690 1 0 |a PROTOPORPHYRIN IX 
690 1 0 |a RAT HARDERIAN GLAND 
690 1 0 |a 5,5' DITHIOBIS(2 NITROBENZOIC ACID) 
690 1 0 |a CYSTEINE 
690 1 0 |a N ETHYLMALEIMIDE 
690 1 0 |a PORPHOBILINOGEN DEAMINASE 
690 1 0 |a PROTOPORPHYRIN 
690 1 0 |a UROPORPHYRIN 
690 1 0 |a ANIMAL TISSUE 
690 1 0 |a ARTICLE 
690 1 0 |a CATALYSIS 
690 1 0 |a ENZYME ACTIVITY 
690 1 0 |a ENZYME ANALYSIS 
690 1 0 |a ENZYME KINETICS 
690 1 0 |a ENZYME PURIFICATION 
690 1 0 |a ENZYME SUBSTRATE 
690 1 0 |a HARDER GLAND 
690 1 0 |a MALE 
690 1 0 |a MOLECULAR WEIGHT 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a RAT 
700 1 |a Juknat, A.A. 
700 1 |a Princ, F.G. 
700 1 |a Batlle, A. 
773 0 |d Academic Press Inc., 1997  |g v. 347  |h pp. 69-77  |k n. 1  |p ARCH. BIOCHEM. BIOPHYS.  |x 00039861  |w (AR-BaUEN)CENRE-1377  |t Archives of Biochemistry and Biophysics 
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