The catalytic mechanisms and substrate specificities of decarboxylating dehydrogenases are under investigation. The structure of a closed, NAD- bound form of the decarboxylating dehydrogenase isopropylmalate dehydrogenase (IMDH) has been determined at 2.5 angstroms resolution by molecular replacement. This structure provides a basis for determining the origins of diverging substrate specificities among the decarboxylating dehydrogenases. Crystals have been obtained of a mutant IMDH whose substrate specificity has been altered to resemble that of isocitrate dehydrogenase (IDH). Crystals of pig heart isocitrate dehydrogenase have also been obtained.
| Yadav, Umesh C S; Srivastava, Satish K; Ramana, Kota V (2012) Prevention of VEGF-induced growth and tube formation in human retinal endothelial cells by aldose reductase inhibition. J Diabetes Complications 26:369-77 |
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