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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1984
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v228_n2_p592_Marechal http://hdl.handle.net/20.500.12110/paper_00039861_v228_n2_p592_Marechal |
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paper:paper_00039861_v228_n2_p592_Marechal2023-06-08T14:25:00Z Partial purification and some properties of β-phosphoglucomutase from Lactobacillus brevis 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. 1984 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v228_n2_p592_Marechal http://hdl.handle.net/20.500.12110/paper_00039861_v228_n2_p592_Marechal |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
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 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. |
| 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 |
| publishDate |
1984 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v228_n2_p592_Marechal http://hdl.handle.net/20.500.12110/paper_00039861_v228_n2_p592_Marechal |
| _version_ |
1768542246729154560 |