title: Expression, purification and characterisation of Haemophilus influenzae 3-isopropylmalate dehydrogenase (LeuB).
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.
authors.affiliation: DiSCAFF, University of Piemonte Orientale Amedeo Avogadro, Via Bovio 6, 28100, Novara, Italy.
authors.forename: Sara
authors.initials: S
authors.lastname: Martignon
authors.forename: Franca
authors.initials: F
authors.lastname: Rossi
authors.forename: Menico
authors.initials: M
authors.lastname: Rizzi
mesh_terms: D050539:3-Isopropylmalate Dehydrogenase / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D002413:Cations, Divalent / Q000494:pharmacology; D002414:Cations, Monovalent / Q000494:pharmacology; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000378:metabolism; D006193:Haemophilus influenzae / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013696:Temperature
chemical_list: D002413:Cations, Divalent; D002414:Cations, Monovalent; D050539:3-Isopropylmalate Dehydrogenase