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Expression, Purification and Characterisation of Haemophilus influenzae 3-Isopropylmalate Dehydrogenase (LeuB)

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Abstract:

3-isopropylmalate dehydrogenase (3IPMDH) is the third enzyme in leucine biosynthesis and a promising target for the development of broad-spectrum antibacterial agents. We report here the expression, purification and biochemical characterisation of Haemophilus influenzae 3-isopropylmalate dehydrogenase. The observed enzyme inhibition by the reaction product NADH could represent a regulatory mechanism for 3IPMDH.





Keywords: 3-isopropylmalate dehydrogenase; Haemophilus influenzae; antibacterial target; leucine biosynthesis; product inhibition; recombinant enzyme

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986607781483606

Publication date: August 1, 2007

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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