PMID: 41237Oct 1, 1979

Evidence for a tyrosine residue at the active site of phosphoglucomutase and its interaction with vanadate

Proceedings of the National Academy of Sciences of the United States of America


The rate of transfer of [32P]phosphate from [32P]-labeled phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate:alpha-D-glucose-1-phosphate phosphotransferase, EC to glucose increases dramatically between pH 8.5 and 10.5 with a half maximal rate at pH 9.8. This suggests the participation of a residue containing an ionizable group with a pK close to 10. The inhibition of enzyme activity obtained with tyrosine-derivatizing reactions--iodination, nitration, acetylation, and diazo coupling--is strongly indicative of tyrosine participation. Thiol reagents, p-hydroxymercuribenzoate and ethyleneimine, were without effect. Vanadate and arsenate augmented the transfer reaction 200- and 2.5-fold, respectively, and lowered the pH optimum of the reaction.


Feb 28, 1983·Biochimica Et Biophysica Acta·D L Barsky, P A Hoffee
Aug 1, 1981·Environmental Health Perspectives·K W Jennette
Dec 1, 1991·Archives of Biochemistry and Biophysics·G L Mendz
Jul 30, 1981·Biochemical and Biophysical Research Communications·F ClimentJ Carreras
Oct 30, 1981·Biochemical and Biophysical Research Communications·G Carpenter
Mar 20, 1990·Biochemistry·M D PercivalM J Gresser

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