Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis
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 molec...
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todo:paper_00039861_v228_n2_p592_Marechal2023-10-03T13:56:58Z Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis Marechal, L.R. Oliver, G. Veiga, L.A. de Ruiz Holgado, A.A.P. 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 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00039861_v228_n2_p592_Marechal |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 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 |
| topic_facet |
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 |
| description |
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. |
| format |
JOUR |
| author |
Marechal, L.R. Oliver, G. Veiga, L.A. de Ruiz Holgado, A.A.P. |
| author_facet |
Marechal, L.R. Oliver, G. Veiga, L.A. de Ruiz Holgado, A.A.P. |
| author_sort |
Marechal, L.R. |
| title |
Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis |
| title_short |
Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis |
| title_full |
Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis |
| title_fullStr |
Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis |
| title_full_unstemmed |
Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis |
| title_sort |
partial purification and some properties of β-phosphoglucomutase from lactobacillus brevis |
| url |
http://hdl.handle.net/20.500.12110/paper_00039861_v228_n2_p592_Marechal |
| work_keys_str_mv |
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