Unknown

Dataset Information

0

Production and crystallization of ?-phosphoglucomutase from Lactococcus lactis.


ABSTRACT: ?-Phosphoglucomutase (?-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and ?-glucose 1-phosphate. The gene encoding ?-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized crystals diffracted to 1.5 Å resolution at a synchrotron source.

SUBMITTER: Nogly P 

PROVIDER: S-EPMC3433211 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Production and crystallization of α-phosphoglucomutase from Lactococcus lactis.

Nogly Przemyslaw P   Castro Rute R   de Rosa Matteo M   Neves Ana Rute AR   Santos Helena H   Archer Margarida M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20120831 Pt 9


α-Phosphoglucomutase (α-PGM) is an enzyme that is essential for the growth of Lactococcus lactis. The enzyme links bacterial anabolism with sugar utilization through glycolysis by catalyzing the reversible interconversion of glucose 6-phosphate and α-glucose 1-phosphate. The gene encoding α-PGM was cloned and overexpressed in L. lactis. The purified protein was functionally active and was crystallized with ammonium sulfate as a precipitant using vapour-diffusion and seeding techniques. Optimized  ...[more]

Similar Datasets

| S-EPMC7093718 | biostudies-literature
| S-EPMC3164122 | biostudies-literature
| S-EPMC2708441 | biostudies-literature
| S-EPMC2515284 | biostudies-literature
| S-EPMC7825684 | biostudies-literature
| S-EPMC161528 | biostudies-literature
| S-EPMC7815928 | biostudies-literature
| S-EPMC8368392 | biostudies-literature
| S-EPMC522069 | biostudies-literature