phosphoglucomutase

Glucose-1-phosphate is converted to glucose-6-phosphate by the enzyme phosphoglucomutase.

After being converted to G6P, the molecule can be turned into glucose-1-phosphate by phosphoglucomutase.

In order to be used for metabolism, it must be converted to glucose-6-phosphate by the enzyme phosphoglucomutase.

Nevertheless, studies have shown that its structure appears to be markedly similar to a related enzyme called phosphoglucomutase.

The glucose-1-phosphate generated in step 3 of the Leloir pathway may be isomerized to glucose-6-phosphate by phosphoglucomutase.

The cleaved molecule is in the form of glucose-1-phosphate, which can be converted into G6P by phosphoglucomutase.

Additionally, phosphoglucomutase converts the D-glucose 1-phosphate to -glucose 6-phosphate.

G-1-P is then converted into G-6-P by enzyme phosphoglucomutase.

To be utilized in cellular catabolism it must first be converted to glucose 6-phosphate by the enzyme phosphoglucomutase.

Pgm encodes the enzyme phosphoglucomutase, which inter-converts glucose 1-phosphate and glucose 6-phosphate.

Determining Frequencies The third test looked at phosphoglucomutase, or PGM, which has 10 different forms.

"Enzymatic assay of inorganic phosphate with use of sucrose phosphorylase and phosphoglucomutase."

Each phosphoglucomutase monomer can be divided into four sequence domains, I-IV, based on the enzyme's default spatial configuration (see image at right).

In this case, phosphoglucomutase catalyzes the conversion of glucose 6-phosphate (which is easily generated from glucose by the action of hexokinase) to glucose 1-phosphate.

Studies have also shown that ovipositing is nonrandom and females lay eggs with varying PGM(phosphoglucomutase) genotypes in different environments in order to optimize offspring success.

The enzyme assay measures the conversion of NADP +to NADPH rather than a direct measure of phosphoglucomutase itself.

While rabbit muscle phosphoglucomutase has served as the prototype for much of the elucidation of this enzyme's structure, newer bacterium-derived crystal structures exhibit many of the same defining characteristics.

The names of isomerases are formed as "substrate isomerase" (for example, enoyl CoA isomerase), or as "substrate type of isomerase" (for example, phosphoglucomutase).

Glycogen is cleaved from the nonreducing ends of the chain by the enzyme glycogen phosphorylase to produce monomers of glucose-1-phosphate, which is then converted to glucose 6-phosphate by phosphoglucomutase.

This glucose 1-phosphate molecule is not itself a useful metabolic intermediate, but phosphoglucomutase catalyzes the conversion of this glucose 1-phosphate to glucose 6-phosphate (see below for the mechanism of this reaction).

High galactose-1-phosphate levels have been shown to interfere with phosphoglucomutase, glycogen phosphorylase, UDP-glycopyrophosphorylase, and inositol monophosphatase activity in bacterial models and in vitro, yet in vivo mechanisms toxicity have yet to be confirmed.

He was grouping a sample of the victim's blood and the blood from the dried stain by the ABO blood group system, and using electrophoresis to identify the haptoglobins and PGM, the enzyme phosphoglucomutase.

In 1958, funded by the British Council, he joined the Biochemistry Department at the University of Cambridge to work for a PhD under Malcolm Dixon on the mechanism of metal activation of the enzyme phosphoglucomutase.

Substrate-velocity relationships and induced transport tests have revealed that the dephosphorylated enzyme then facilitates the transfer of a phosphoryl group from the glucose-1,6-bisphosphate intermediate to the enzyme, regenerating phosphorylated phosphoglucomutase and yielding glucose 6-phosphate (in the forward direction).