An amino acid sequence in the active centre of phosphoglucomutase

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Abstract
Phosphoglucomutase labelled with p32 was prepared by 2 methods involving reaction of the enzyme with labelled substrates. The P32 phosphoglucomutase was subjected to partial hydrolysis with trypsin and with acid and the [P32] peptides were purified by ionophoresis. The interrelationships of the peptides in the acid hydrolysate were determined by subjecting them to further partial acid hydrolysis and to the Edman degradation procedure. The individual residues in these peptides were identified from the ionophoretic and chromatographic mobilities of the peptides, by specific reactions and from the amino acid composition of highly purified peptides.. It was concluded that the amino acid sequence around the serine phosphate (SerP) residue was threonine alanine Ser. P hrstidine aspartic acid.