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

The rate of transfer of [32P]phosphate from [32P]-labeled phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate:alpha-D-glucose-1-phosphate phosphotransferase, EC 2.7.5.1) 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...

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Bibliographic Details
Main Authors: Layne, P P, Najjar, V A
Format: Artigo
Language:Inglês
Published: 1979
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Research Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC413068/
https://ncbi.nlm.nih.gov/pubmed/41237
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