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)

Sara Martignon, Franca Rossi, Menico Rizzi

Dipartimento di Scienze del Farmaco

Risultato della ricerca: Contributo su rivista › Articolo in rivista › peer review

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.

Lingua originale	Inglese
pagine (da-a)	822-827
Numero di pagine	6
Rivista	Protein and Peptide Letters
Volume	14
Numero di pubblicazione	8
DOI	https://doi.org/10.2174/092986607781483606
Stato di pubblicazione	Pubblicato - ago 2007

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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.",

keywords = "3-isopropylmalate dehydrogenase, Antibacterial target, Haemophilus influenzae, Leucine biosynthesis, Product inhibition, Recombinant enzyme",

author = "Sara Martignon and Franca Rossi and Menico Rizzi",

year = "2007",

month = aug,

doi = "10.2174/092986607781483606",

language = "English",

volume = "14",

pages = "822--827",

journal = "Protein and Peptide Letters",

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T1 - Expression, purification and characterisation of Haemophilus influenzae 3-isopropylmalate dehydrogenase (LeuB)

AU - Martignon, Sara

AU - Rossi, Franca

AU - Rizzi, Menico

PY - 2007/8

Y1 - 2007/8

N2 - 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.

AB - 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.

KW - 3-isopropylmalate dehydrogenase

KW - Antibacterial target

KW - Haemophilus influenzae

KW - Leucine biosynthesis

KW - Product inhibition

KW - Recombinant enzyme

UR - https://www.scopus.com/pages/publications/34548685337

U2 - 10.2174/092986607781483606

DO - 10.2174/092986607781483606

M3 - Article

SN - 0929-8665

VL - 14

SP - 822

EP - 827

JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

IS - 8

ER -

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

Abstract

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