Inhibitor binding studies on enoyl-reductase reveal conformational changes related to substrate recognition.

A. Roujeinikova; S. Sedelnikova; G.J. de Boer; A.R. Stuitje; A.R. Slabas; J.B. Rafferty; D.W. Rice

doi:10.1074/jbc.274.43.30811

Inhibitor binding studies on enoyl-reductase reveal conformational changes related to substrate recognition.

A. Roujeinikova
, S. Sedelnikova
, G.J. de Boer
, A.R. Stuitje
, A.R. Slabas
, J.B. Rafferty
, D.W. Rice

Research output: Contribution to Journal › Article › Academic › peer-review

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Abstract

Enoyl acyl carrier protein reductase (ENR) is involved in fatty acid biosynthesis. In Escherichia coli this enzyme is the target for the experimental family of antibacterial agents, the diazaborines, and for triclosan, a broad spectrum antimicrobial agent. Biochemical studies have suggested that the mechanism of diazaborine inhibition is dependent on NAD

Original language	English
Pages (from-to)	30811-30817
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	274
DOIs	https://doi.org/10.1074/jbc.274.43.30811
Publication status	Published - 1999

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title = "Inhibitor binding studies on enoyl-reductase reveal conformational changes related to substrate recognition.",

abstract = "Enoyl acyl carrier protein reductase (ENR) is involved in fatty acid biosynthesis. In Escherichia coli this enzyme is the target for the experimental family of antibacterial agents, the diazaborines, and for triclosan, a broad spectrum antimicrobial agent. Biochemical studies have suggested that the mechanism of diazaborine inhibition is dependent on NAD",

author = "A. Roujeinikova and S. Sedelnikova and \{de Boer\}, G.J. and A.R. Stuitje and A.R. Slabas and J.B. Rafferty and D.W. Rice",

year = "1999",

doi = "10.1074/jbc.274.43.30811",

language = "English",

volume = "274",

pages = "30811--30817",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

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T1 - Inhibitor binding studies on enoyl-reductase reveal conformational changes related to substrate recognition.

AU - Roujeinikova, A.

AU - Sedelnikova, S.

AU - de Boer, G.J.

AU - Stuitje, A.R.

AU - Slabas, A.R.

AU - Rafferty, J.B.

AU - Rice, D.W.

PY - 1999

Y1 - 1999

N2 - Enoyl acyl carrier protein reductase (ENR) is involved in fatty acid biosynthesis. In Escherichia coli this enzyme is the target for the experimental family of antibacterial agents, the diazaborines, and for triclosan, a broad spectrum antimicrobial agent. Biochemical studies have suggested that the mechanism of diazaborine inhibition is dependent on NAD

AB - Enoyl acyl carrier protein reductase (ENR) is involved in fatty acid biosynthesis. In Escherichia coli this enzyme is the target for the experimental family of antibacterial agents, the diazaborines, and for triclosan, a broad spectrum antimicrobial agent. Biochemical studies have suggested that the mechanism of diazaborine inhibition is dependent on NAD

U2 - 10.1074/jbc.274.43.30811

DO - 10.1074/jbc.274.43.30811

M3 - Article

SN - 0021-9258

VL - 274

SP - 30811

EP - 30817

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

ER -

Inhibitor binding studies on enoyl-reductase reveal conformational changes related to substrate recognition.

Abstract

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