Expression, purification and characterisation of Haemophilus influenzae 3-isopropylmalate dehydrogenase (LeuB)

Sara Martignon; Franca Rossi; Menico Rizzi

doi:10.2174/092986607781483606

Expression, purification and characterisation of Haemophilus influenzae 3-isopropylmalate dehydrogenase (LeuB)

Protein Pept Lett. 2007;14(8):822-7. doi: 10.2174/092986607781483606.

Authors

Sara Martignon¹, Franca Rossi, Menico Rizzi

Affiliation

¹ DiSCAFF, University of Piemonte Orientale Amedeo Avogadro, Via Bovio 6, 28100, Novara, Italy.

PMID: 17979826
DOI: 10.2174/092986607781483606

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

3-Isopropylmalate Dehydrogenase / biosynthesis*
3-Isopropylmalate Dehydrogenase / isolation & purification
3-Isopropylmalate Dehydrogenase / metabolism
Cations, Divalent / pharmacology
Cations, Monovalent / pharmacology
Cloning, Molecular
Escherichia coli / metabolism
Haemophilus influenzae / enzymology*
Hydrogen-Ion Concentration
Kinetics
Temperature

Substances

Cations, Divalent
Cations, Monovalent
3-Isopropylmalate Dehydrogenase