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Araujo, L.S.; Lombardo, M.E.; Rossetti, ]M.V.; Batlle, A.M.d.C. "Saccharomyces cerevisiae porphobilinogenase: Some physical and kinetic properties" (1989) Comparative Biochemistry and Physiology -- Part B: Biochemistry and. 92(2):297-301
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Abstract:

1. 1. Properties of porphobilinogenase (PBGase), the enzyme complex converting porphobilinogen (PBG) into uroporphyrinogens, were studied in a wild strain, D273-10B and a mutant, B231, of Saccharomyces cerevisiae 2. 2. A well-defined maximum of enzyme activity was observed for the mutant strain after 20 hr of growth; whilst the activity in the wild strain did not vary significantly during growth. 3. 3. Neither PBG consumption nor uroporphyrinogen formation were modified by the presence of air either in the wild or in the mutant strain. 4. 4. In both the wild and mutant strains uroporphyrinogen formation increased linearly with both protein concentration and incubation time. 5. 5. The addition of a mixture of sodium and magnesium salts to the assay system inhibited the enzyme activity of both strains by 50% without modifying the isomer composition. 6. 6. The same optimum pH (7.4) and mol. wt (50,000 ± 5000) was found for the enzyme from both strains. 7. 7. The enzyme from both the wild and mutant strains shows Michaelis-Menten kinetics when isolated from cells at either the exponential or the stationary phases of growth. Accumulation of porphyrins and δ-aminolevulinic acid occurring during the exponential phase in the mutant strain, did not modify the kinetics. © 1989.

Registro:

Documento: Artículo
Título:Saccharomyces cerevisiae porphobilinogenase: Some physical and kinetic properties
Autor:Araujo, L.S.; Lombardo, M.E.; Rossetti, ]M.V.; Batlle, A.M.d.C.
Filiación:Centro de Investigaciones sobre Porfirinas y Porfirias, CIPYP (CONICET-FCEN, UBA), Ciudad Universitaria, Pabellon II, 2do. Piso, 1428 Buenos Aires, Argentina
Palabras clave:ammonia lyase; Ammonia Lyases; magnesium; porphobilinogenase; sodium; article; enzymology; genetics; kinetics; metabolism; molecular weight; mutation; pH; Saccharomyces cerevisiae; Ammonia-Lyases; Hydrogen-Ion Concentration; Kinetics; Magnesium; Molecular Weight; Mutation; Saccharomyces cerevisiae; Sodium; Support, Non-U.S. Gov't
Año:1989
Volumen:92
Número:2
Página de inicio:297
Página de fin:301
DOI: http://dx.doi.org/10.1016/0305-0491(89)90281-2
Título revista:Comparative Biochemistry and Physiology -- Part B: Biochemistry and
ISSN:03050491
CAS:magnesium, 7439-95-4; porphobilinogenase, 9055-40-7; sodium, 7440-23-5; Ammonia-Lyases, EC 4.3.1.; Magnesium, 7439-95-4; porphobilinogenase, EC 5.-; Sodium, 7440-23-5
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03050491_v92_n2_p297_Araujo

Referencias:

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Citas:

---------- APA ----------
Araujo, L.S., Lombardo, M.E., Rossetti, ]M.V. & Batlle, A.M.d.C. (1989) . Saccharomyces cerevisiae porphobilinogenase: Some physical and kinetic properties. Comparative Biochemistry and Physiology -- Part B: Biochemistry and, 92(2), 297-301.
http://dx.doi.org/10.1016/0305-0491(89)90281-2
---------- CHICAGO ----------
Araujo, L.S., Lombardo, M.E., Rossetti, ]M.V., Batlle, A.M.d.C. "Saccharomyces cerevisiae porphobilinogenase: Some physical and kinetic properties" . Comparative Biochemistry and Physiology -- Part B: Biochemistry and 92, no. 2 (1989) : 297-301.
http://dx.doi.org/10.1016/0305-0491(89)90281-2
---------- MLA ----------
Araujo, L.S., Lombardo, M.E., Rossetti, ]M.V., Batlle, A.M.d.C. "Saccharomyces cerevisiae porphobilinogenase: Some physical and kinetic properties" . Comparative Biochemistry and Physiology -- Part B: Biochemistry and, vol. 92, no. 2, 1989, pp. 297-301.
http://dx.doi.org/10.1016/0305-0491(89)90281-2
---------- VANCOUVER ----------
Araujo, L.S., Lombardo, M.E., Rossetti, ]M.V., Batlle, A.M.d.C. Saccharomyces cerevisiae porphobilinogenase: Some physical and kinetic properties. 1989;92(2):297-301.
http://dx.doi.org/10.1016/0305-0491(89)90281-2