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: Haemophilus influenzae, 3-isopropylmalate dehydrogenase, recombinant enzyme, leucine biosynthesis, antibacterial target, product inhibition
Protein & Peptide Letters
Title: Expression, Purification and Characterisation of Haemophilus influenzae 3-Isopropylmalate Dehydrogenase (LeuB)
Volume: 14 Issue: 8
Author(s): Sara Martignon, Franca Rossi and Menico Rizzi
Affiliation:
Keywords: Haemophilus influenzae, 3-isopropylmalate dehydrogenase, recombinant enzyme, leucine biosynthesis, antibacterial target, product inhibition
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.
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Cite this article as:
Sara Martignon , Franca Rossi and Menico Rizzi , Expression, Purification and Characterisation of Haemophilus influenzae 3-Isopropylmalate Dehydrogenase (LeuB), Protein & Peptide Letters 2007; 14 (8) . https://dx.doi.org/10.2174/092986607781483606
DOI https://dx.doi.org/10.2174/092986607781483606 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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