Current Issues of Pharmacy and Medical Sciences

α-Phosphoglucomutase from Escherichia coli ATCC 25922 – pilot studies

Annales UMCS, Sectio DDD, Pharmacia, Vol. XXIV, N 4, 13

KATARZYNA PARADOWSKA, ANNA SURDY, GRAŻYNA GINALSKA

Chair and Department of Biochemistry and Biotechnology, Medical University in Lublin, Poland

Abstract

The α-phosphoglucomutase (α-PGM, EC 5.4.2.2) is an enzyme participating in the metabolism of the sugar and carrying the reversible isomerization of α-D-glucose-1-phosphate to a-D-glucose-6-phosphate.

Some properties of α-PGM from E. coli ATCC 25922 were studied. The Km constant for α-D-glucose-1-phosphate was 25 x 10-5 M/L. The enzyme had optimum activity in TRIS/HCl buffer, pH 8.0. Its activity was stimulated by addition of α-D-glucose-1,6-bisphosphate, Mg(II) cations and several thiols. The α-phosphoglucomutase had molecular weight 65 kDa and consisted of one polypeptide chain. Our results indicated the significant sensitivity of enzymatic activity by non- and organic mercuric compounds. The lack of the activity inhibition of characterized enzyme by chelators as 2,4’-bipyridyl, EDTA and TRIS indicated that the α-PGM is not a metallprotein. The similarities and differences between properties of a-phosphoglucomutases isolated from E. coli ATCC 25922 and other E. coli strains such as ATCC 26 and ATCC 35218 were discovered.

Our pilot studies have an important implication in better understanding of virulence of enteric bacteria (E.  coli).

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Keywords

α-phosphoglucomutase, Escherichia coli ATCC 25922, biofilm

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