@article { ISI:000319992200002,
	title = {Biochemical correlate of dimorphism in a zygomycete benjaminiella poitrasii: characterization of purified NAD-dependent glutamate dehydrogenase, a target for antifungal agents},
	journal = {Antonie Van Leeuwenhoek International Journal of General and Molecular Microbiology},
	volume = {104},
	number = {1},
	year = {2013},
	month = {JUL},
	pages = {25-36},
	publisher = {SPRINGER},
	address = {VAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDS},
	abstract = {<p>The fungal organisms, especially pathogens, change their vegetative (Y, unicellular yeast and H, hypha) morphology reversibly for survival and proliferation in the host environment. NAD-dependent glutamate dehydrogenase (NAD-GDH, EC 1.4.1.2) from a non-pathogenic dimorphic zygomycete Benjaminiella poitrasii was previously reported to be an important biochemical correlate of the transition process. The enzyme was purified to homogeneity and characterized. It is a 371 kDa native molecular weight protein made up of four identical subunits. Kinetic studies showed that unlike other NAD-GDHs, it may act as an anabolic enzyme and has more affinity towards 2-oxoglutarate than l-glutamate. Chemical modifications revealed the involvement of single histidine and lysine residues in the catalytic activity of the enzyme. The phosphorylation and dephosphorylation study showed that the NAD-GDH is present in active phosphorylated form in hyphal cells of B. poitrasii. Two of the 1,2,3 triazole linked beta-lactam-bile acid conjugates synthesized in the laboratory (B18, B20) were found to be potent inhibitors of purified NAD-GDH which also significantly affected Y-H transition in B. poitrasii. Furthermore, the compound B20 inhibited germ tube formation during Y-H transition in Candida albicans strains and Yarrowia lipolytica. The possible use of NAD-GDH as a target for antifungal agents is discussed.</p>},
	keywords = {Antifungal agent, Benjaminiella poitrasii, Biochemical correlate of dimorphism, Candida albicans, NAD-GDH activity regulation, Yarrowia lipolytica, Yeast-hypha reversible transition},
	issn = {0003-6072},
	doi = {10.1007/s10482-013-9921-5},
	author = {Joshi, C. V. and Pathan, E. K. and Punekar, N. S. and Tupe, S. G. and Kapadnis, B. P. and Deshpande, Mukund V.}
}
