Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

Author(s): Sara Martignon, Franca Rossi and Menico Rizzi

Volume 14, Issue 8, 2007

Page: [822 - 827] Pages: 6

DOI: 10.2174/092986607781483606

Price: $65

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


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy