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Structural analysis of glyceraldehyde-3-phosphate dehydrogenase functional diversity
- Sirover, Michael A.
- The international journal of biochemistry & cell biology 2014 v.57 pp. 20-26
- amino acids, cell viability, energy, functional diversity, genes, glyceraldehyde-3-phosphate dehydrogenase, post-translational modification, proteins, structure-activity relationships
- Multifunctional proteins provide a new mechanism to expand exponentially cell information and capability beyond that indicated by conventional gene analyses. As such, examination of their structure–function relationships provides a means to define the mechanisms through which cells accomplish critical yet disparate activities required for cell viability and survival. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) may be considered the quintessential multidimensional protein which exhibits a variety of functions unrelated to its classical role in energy production. This review discusses new insights into the structure–function mechanisms through which defined GAPDH amino acid domains are utilized for its diverse activities, the importance of its post-translational modification, and, intriguingly, the logic inherent in the presence or the absence of specific signaling domains.