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Abstract:

A phosphoglucomutase (β-phosphoglucomutase) specific for β-glucose 1-phosphate, which catalyzes the β-glucose 1-phosphate:glucose 6-phosphate interconversion, was 560-fold purified from Lactobacillus brevis strain L6. The isoelectric point of β-phosphoglucomutase was 3.8 and it had an apparent molecular weight of 29,000 estimated by gel chromatography. The enzyme required a divalent cation (Mn2+ > Mg2+ > Ni2+ > Co2+) and β-glucose 1,6-bisphosphate for activity. The equilibrium constant Ke for the reaction β-d-glucose 1-phosphate γ d-glucose 6-phosphate at 30 °C and pH 6.7 is 18.5. β-phosphoglucomutase had a pH optimum between 6.3 and 6.8 and appeared to be quite specific: α-glucose 1-phosphate, α- or β-galactose 1-phosphate and α- or β-N-acetylglucosamine 1-phosphate did not substitute for β-glucose 1-phosphate. Double reciprocal plots of the data from initial velocity studies at five β-glucose 1-phosphate concentrations (10 to 100 μm) and four β-glucose 1,6-bisphosphate concentrations (0.125 to 1.0 μm) showed that the apparent Michaelis constants for β-glucose 1-phosphate and β-glucose 1,6-bisphosphate were related to the concentrations of β-glucose 1,6-bisphosphate and β-glucose 1-phosphate, respectively, in such a way as to suggest a pingpong mechanism. The same conclusion was obtained when substrate-velocity relationships were investigated at fixed ratio of both substrates: the Lineweaver-Burk plots showed linear lines and no parabolic ones. The "true" Km for β-glucose 1-phosphate and β-glucose 1,6-bisphosphate were found to be about 12 and 0.8 μm, respectively. © 1984.

Registro:

Documento: Artículo
Título:Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis
Autor:Marechal, L.R.; Oliver, G.; Veiga, L.A.; de Ruiz Holgado, A.A.P.
Filiación:Instituto de Investigaciones Bioquimicos Fundacion Campomar Vuelta de Obligado 2490, 1428 Buenos Aires, Argentina
Centro de Referenda para Lactobacilos (C.E.R.E.L.A.) San Miguel de Tucuman, Argentina
Departamento de Bioquimica, Universidade Federal de Parana, Curitiba, Parana, Brazil
Palabras clave:phosphoglucomutase; article; catalysis; chemistry; drug effect; enzyme activation; enzymology; isolation and purification; kinetics; Lactobacillus; metabolism; Catalysis; Chemistry; Enzyme Activation; Kinetics; Lactobacillus; Phosphoglucomutase; Support, Non-U.S. Gov't
Año:1984
Volumen:228
Número:2
Página de inicio:592
Página de fin:599
DOI: http://dx.doi.org/10.1016/0003-9861(84)90027-4
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CODEN:ABBIA
CAS:phosphoglucomutase, 9001-81-4; Phosphoglucomutase, EC 5.4.2.2
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v228_n2_p592_Marechal

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Citas:

---------- APA ----------
Marechal, L.R., Oliver, G., Veiga, L.A. & de Ruiz Holgado, A.A.P. (1984) . Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis. Archives of Biochemistry and Biophysics, 228(2), 592-599.
http://dx.doi.org/10.1016/0003-9861(84)90027-4
---------- CHICAGO ----------
Marechal, L.R., Oliver, G., Veiga, L.A., de Ruiz Holgado, A.A.P. "Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis" . Archives of Biochemistry and Biophysics 228, no. 2 (1984) : 592-599.
http://dx.doi.org/10.1016/0003-9861(84)90027-4
---------- MLA ----------
Marechal, L.R., Oliver, G., Veiga, L.A., de Ruiz Holgado, A.A.P. "Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis" . Archives of Biochemistry and Biophysics, vol. 228, no. 2, 1984, pp. 592-599.
http://dx.doi.org/10.1016/0003-9861(84)90027-4
---------- VANCOUVER ----------
Marechal, L.R., Oliver, G., Veiga, L.A., de Ruiz Holgado, A.A.P. Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis. Arch. Biochem. Biophys. 1984;228(2):592-599.
http://dx.doi.org/10.1016/0003-9861(84)90027-4