a study of structure-activity relationship for diazaborine inhibition of Escherichia coli encoy- ACP reductase

C.W. Levy; C. Baldock; A.J. Wallace; S. Sedelnikova; R.C. Viner; J.M. Clough; A.R. Stuitje; A.R. Slabas; D.W. Rice; J.B. Rafferty

doi:10.1006/jmbi.2001.4643

a study of structure-activity relationship for diazaborine inhibition of Escherichia coli encoy- ACP reductase

C.W. Levy, C. Baldock, A.J. Wallace, S. Sedelnikova, R.C. Viner, J.M. Clough, A.R. Stuitje, A.R. Slabas, D.W. Rice, J.B. Rafferty

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

Abstract

Enoyl acyl carrier protein (ACP) reductase catalyses the last reductive step of fatty acid biosynthesis, reducing the enoyl group of a growing fatty acid chain attached to ACP to its acyl product using NAD(P)H as the cofactor. This enzyme is the target for the diazaborine class of anti-bacterial agents, the biocide triclosan, and one of the targets for the front-line anti-tuberculosis drug isoniazid. The structures of complexes of Escherichia coli enoyl-ACP reductase (ENR) from crystals grown in the presence of NAD

Original language	English
Pages (from-to)	171-180
Journal	Journal of Molecular Biology
Volume	309
Issue number	1
DOIs	https://doi.org/10.1006/jmbi.2001.4643
Publication status	Published - 2001

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10.1006/jmbi.2001.4643

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title = "a study of structure-activity relationship for diazaborine inhibition of Escherichia coli encoy- ACP reductase",

abstract = "Enoyl acyl carrier protein (ACP) reductase catalyses the last reductive step of fatty acid biosynthesis, reducing the enoyl group of a growing fatty acid chain attached to ACP to its acyl product using NAD(P)H as the cofactor. This enzyme is the target for the diazaborine class of anti-bacterial agents, the biocide triclosan, and one of the targets for the front-line anti-tuberculosis drug isoniazid. The structures of complexes of Escherichia coli enoyl-ACP reductase (ENR) from crystals grown in the presence of NAD",

author = "C.W. Levy and C. Baldock and A.J. Wallace and S. Sedelnikova and R.C. Viner and J.M. Clough and A.R. Stuitje and A.R. Slabas and D.W. Rice and J.B. Rafferty",

year = "2001",

doi = "10.1006/jmbi.2001.4643",

language = "English",

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journal = "Journal of Molecular Biology",

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T1 - a study of structure-activity relationship for diazaborine inhibition of Escherichia coli encoy- ACP reductase

AU - Levy, C.W.

AU - Baldock, C.

AU - Wallace, A.J.

AU - Sedelnikova, S.

AU - Viner, R.C.

AU - Clough, J.M.

AU - Stuitje, A.R.

AU - Slabas, A.R.

AU - Rice, D.W.

AU - Rafferty, J.B.

PY - 2001

Y1 - 2001

N2 - Enoyl acyl carrier protein (ACP) reductase catalyses the last reductive step of fatty acid biosynthesis, reducing the enoyl group of a growing fatty acid chain attached to ACP to its acyl product using NAD(P)H as the cofactor. This enzyme is the target for the diazaborine class of anti-bacterial agents, the biocide triclosan, and one of the targets for the front-line anti-tuberculosis drug isoniazid. The structures of complexes of Escherichia coli enoyl-ACP reductase (ENR) from crystals grown in the presence of NAD

AB - Enoyl acyl carrier protein (ACP) reductase catalyses the last reductive step of fatty acid biosynthesis, reducing the enoyl group of a growing fatty acid chain attached to ACP to its acyl product using NAD(P)H as the cofactor. This enzyme is the target for the diazaborine class of anti-bacterial agents, the biocide triclosan, and one of the targets for the front-line anti-tuberculosis drug isoniazid. The structures of complexes of Escherichia coli enoyl-ACP reductase (ENR) from crystals grown in the presence of NAD

U2 - 10.1006/jmbi.2001.4643

DO - 10.1006/jmbi.2001.4643

M3 - Article

SN - 0022-2836

VL - 309

SP - 171

EP - 180

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 1

ER -

a study of structure-activity relationship for diazaborine inhibition of Escherichia coli encoy- ACP reductase

Abstract

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