02552nas a2200289   4500008004100000022001400041245018000055210006900235260007400304300001000378490000800388520141500396653002101811653002801832653004001860653002101900653003201921653002401953653003801977100001802015700001902033700002002052700001702072700002102089700002602110856012602136       2013                        eng d  a0003-607200aBiochemical correlate of dimorphism in a zygomycete benjaminiella poitrasii: characterization of purified NAD-dependent glutamate dehydrogenase, a target for antifungal agents0 aBiochemical correlate of dimorphism in a zygomycete benjaminiell  aVAN GODEWIJCKSTRAAT 30, 3311 GZ DORDRECHT, NETHERLANDSbSPRINGERcJUL  a25-360 v1043 a<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>10aAntifungal agent10aBenjaminiella poitrasii10aBiochemical correlate of dimorphism10aCandida albicans10aNAD-GDH activity regulation10aYarrowia lipolytica10aYeast-hypha reversible transition1 aJoshi, C., V.1 aPathan, E., K.1 aPunekar, N., S.1 aTupe, S., G.1 aKapadnis, B., P.1 aDeshpande, Mukund, V.  uhttps://library.ncl.res.in/content/biochemical-correlate-dimorphism-zygomycete-benjaminiella-poitrasii-characterization-0