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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Stimulation of glyceraldehyde-3-phosphate dehydrogenase by oxyhemoglobin.

Glyceraldehyde-3-phosphate dehydrogenase ( GAPDH) is a key glycolytic enzyme regulated by many diverse mechanisms. In this study we present evidence that GAPDH activity is stimulated in the presence of oxyhemoglobin (2.3-fold, P < 0.005). No stimulation was seen by myoglobin, and only slight stimulation (1.2-fold, not significant) by methemoglobin was observed. Such stimulation may have physiological significance as 1,3-bis-phosphoglycerate, the product of GAPDH, isomerises to 2,3-bis-phosphoglycerate, an allosteric effector that decreases the oxygen affinity of hemoglobin, thus providing a feedback loop. The results suggest that when assaying GAPDH activity in biological samples, hemoglobin content should be taken into account.[1]

References

  1. Stimulation of glyceraldehyde-3-phosphate dehydrogenase by oxyhemoglobin. Brookes, P.S., Land, J.M., Clark, J.B., Heales, S.J. FEBS Lett. (1997) [Pubmed]
 
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