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Phosphoglucomutase isolation

Phosphoglucomutase was isolated by the Coris and crystallized by Najjar. Its mechanism of action was suggested from experiments by Leloir in 1951 using [32P]. The enzyme is a phosphoprotein. Leloir showed that the phosphate group was transferred from the enzyme to G-1-P in the course of the reaction to give G-1,6 diP, which then donated the phosphate from its 1-position back to the enzyme, releasing G-6-P ... [Pg.58]

The phosphoglucomutase enzyme catalyzes reaction 79. Reaction 78, which involves an inversion (Walden inversion) at C4 of the hexose, was shown to require a heat-stable cofactor. s This coenzyme for the galactowaldenase system was isolated and its structure determined. The coenzyme is uridinidiphosphoglucose (UDPGlucose). [Pg.388]

A recent search for this enzyme and coenzyme have revealed that phosphoglucomutase itself may be the phosphoribomutase, since the crystalline enzyme appears to be active on both substrates in a constant ratio maintained through intermediate stages in the purification. In the presence of trace amounts of glucose-1,6-diphosphate, ribose-1,5-diphosphate appears to be generated, and a compound which is probably this latter substance has been isolated from the reaction mixture. [Pg.215]

Overexpression of selected enzymes involved in galactose biosynthesis, either independently or collectively as an entire metabolic pathway, may be a route to increased levels of galactosylation in CHO cells. These include the UDP-glucose-4-epimerase [36], the phosphoglucomutase [43], and the UDP-glucose pyrophosphor-ylase [44] and the UDP-galactose transferase [45]. All of the genes for these enzymes have been isolated from either mammalian or microbial sources. [Pg.2142]


See other pages where Phosphoglucomutase isolation is mentioned: [Pg.401]    [Pg.190]    [Pg.114]    [Pg.117]    [Pg.57]    [Pg.152]    [Pg.43]    [Pg.61]    [Pg.79]    [Pg.185]    [Pg.479]   
See also in sourсe #XX -- [ Pg.408 ]

See also in sourсe #XX -- [ Pg.408 ]




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Phosphoglucomutases

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