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Aspergillus terreus NADP-glutamate dehydrogenase is kinetically distinct from the allosteric enzyme of other Aspergilli

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Title Aspergillus terreus NADP-glutamate dehydrogenase is kinetically distinct from the allosteric enzyme of other Aspergilli
 
Creator CHOUDHURY, R
PUNEKAR, NS
 
Subject aconitic acid decarboxylase
fungi
purification
gene
inhibition
metabolism
allostery
aspergillus terreus
nadp-glutamate dehydrogenase
2-oxoglutarate saturation
 
Description NADP-Glutamate dehydrogenase (NADP-GDH) located at the interface of carbon and nitrogen metabolism has the potential to dictate fungal carbon flux. NADP-GDH from Aspergillus terreus, itaconate producer and an opportunistic pathogen, was purified to homogeneity using novel reactive dye-affinity resins. The pure enzyme was extensively characterized for its biochemical and kinetic properties and compared with its well studied Aspergillus niger counterpart. The A. terreus NADP-GDH was more stable and showed non-competitive ammonium inhibition with respect to glutamate It exhibited hyperbolic 2-oxoglutarate saturation albeit with a weak substrate inhibition. This is in contrast to the allosteric nature of the enzyme from other Aspergilli. Differential susceptibility to chymotrypsin is also consistent with the absence of substrate cooperativity and conformational changes associated with A. terreus NADP-GDH. The non-allosteric nature of A. terreus NADP-GDH provides a unique opportunity to assess the contribution of allostery in metabolic regulation. (C) 2009 The British Mycological Society.
 
Publisher ELSEVIER SCI LTD
 
Date 2011-07-21T21:03:28Z
2011-12-26T12:52:10Z
2011-12-27T05:39:12Z
2011-07-21T21:03:28Z
2011-12-26T12:52:10Z
2011-12-27T05:39:12Z
2009
 
Type Article
 
Identifier MYCOLOGICAL RESEARCH, 113(), 1121-1126
0953-7562
http://dx.doi.org/10.1016/j.mycres.2009.07.009
http://dspace.library.iitb.ac.in/xmlui/handle/10054/5993
http://hdl.handle.net/10054/5993
 
Language en