NDLI: Human Brain 6-Phosphogluconate Dehydrogenase: Purification and Kinetic Properties

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Human Brain 6-Phosphogluconate Dehydrogenase: Purification and Kinetic Properties

Content Provider	Scilit
Author	Weisz, Karen S. Schofield, Philip J. Edwards, Michael R.
Copyright Year	1985
Description	Journal: Journal of Neurochemistry 6-Phosphogluconate dehydrogenase has been purified from human brain to a specific activity of 22.8 U/mg protein. The molecular weight was 90,000. At low ionic strengths enzyme activity increased, due to an increase in Vmax and a decrease in Km for 6-phosphogluconate, and activity subsequently decreased as the ionic strength was increased (above 0.12). Both 6-phosphogluconate and NADP+ provided good protection against thermal inactivation, with 6-phosphogluconate also providing considerable protection against loss of activity caused by p-chloromercuribenzoate and iodoacetamide. Initial velocity studies indicated the enzyme mechanism was sequential. NADPH was a competitive inhibitor with respect to NADP+, and the Ki values for this inhibition were dependent on the concentration of 6-phosphogluconate. Product inhibition by NADPH was noncompetitive when 6-phosphogluconate was the variable substrate, whereas inhibition by the products CO2 and ribulose 5-phosphogluconate and NADP+ were varied. In totality these data suggest that binding of substrates to the enzyme is random. CO2 and ribulose 5-phosphate are released from the enzyme in random order with NADPH as the last product released.
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1471-4159.1985.tb05443.x/pdf
Ending Page	517
Page Count	8
Starting Page	510
e-ISSN	14714159
DOI	10.1111/j.1471-4159.1985.tb05443.x
Journal	Journal of Neurochemistry
Issue Number	2
Volume Number	44
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1985-02-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Neurochemistry Biochemistry and Molecular Biology 6‐phosphogluconate Dehydrogenase Human Brain Pentose Phosphate Pathway
Content Type	Text
Resource Type	Article

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