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Encyclopedia > Phosphoglucomutase

Phosphoglucomutase (EC 5.4.2.2/5/6) is an enzyme that creates a glucose isomer by changing the site of the Phosphate ion.


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PGM1/YKL127W Summary (513 words)
Phosphoglucomutase (EC:5.4.2.2) catalyzes the interconversion of glucose-6-phosphate and glucose-1-phosphate and is important for carbohydrate metabolism in a variety of organisms, ranging from bacteria to humans (3, 4, 1, 5).
Phosphoglucomutase is also required for the synthesis of N-linked glycoproteins, extracellular glycans, and UDP-glucose (3, 4, 5, 6).
Phosphoglucomutase also indirectly effects calcium uptake and homeostasis because glucose-1-phosphate and glucose-6-phosphate effect cation uptake (7, 8, 4).
The Herbert Newby McCoy Award 1991 Winner (1093 words)
It is involved with the metabolism of glucose, where it functions to interconvert glucose 1-phosphate and glucose 6-phosphate so that regulation of those enzymes involved with the subsequent degradation of glucose 6-phosphate or the storage of glucose 1-phosphate can be used to control the relative importance of immediately-usable versus stored energy.
Thus, the enzyme is able to convert a molecule of glucose 1-phosphate to glucose 6-phosphate even in the presence of other sugar phosphates at a ratio of 1:50,000, without disturbing the surrounding population, and it accomplishes with 0.001 sec what would require hundreds of years in the absence of a catalyst.
Ray’s initial studies with phosphoglucomutase defined the reaction pathway of the enzyme and were the first to define the order of substrate-metal ion binding in a metal-ion activated enzymic reaction.
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