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1dfh

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[[Image:1dfh.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_1dfh| PDB=1dfh | SCENE= }}
{{STRUCTURE_1dfh| PDB=1dfh | SCENE= }}
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'''X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE'''
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===X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE===
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==Overview==
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Enoyl reductase (ENR), an enzyme involved in fatty acid biosynthesis, is the target for antibacterial diazaborines and the front-line antituberculosis drug isoniazid. Analysis of the structures of complexes of Escherichia coli ENR with nicotinamide adenine dinucleotide and either thienodiazaborine or benzodiazaborine revealed the formation of a covalent bond between the 2' hydroxyl of the nicotinamide ribose and a boron atom in the drugs to generate a tight, noncovalently bound bisubstrate analog. This analysis has implications for the structure-based design of inhibitors of ENR, and similarities to other oxidoreductases suggest that mimicking this molecular linkage may have generic applications in other areas of medicinal chemistry.
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The line below this paragraph, {{ABSTRACT_PUBMED_8953047}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 8953047 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8953047}}
==About this Structure==
==About this Structure==
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[[Category: Lipid biosynthesis]]
[[Category: Lipid biosynthesis]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:47:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:59:58 2008''

Revision as of 19:59, 30 June 2008

Image:1dfh.png

Template:STRUCTURE 1dfh

X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE

Template:ABSTRACT PUBMED 8953047

About this Structure

1DFH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A mechanism of drug action revealed by structural studies of enoyl reductase., Baldock C, Rafferty JB, Sedelnikova SE, Baker PJ, Stuitje AR, Slabas AR, Hawkes TR, Rice DW, Science. 1996 Dec 20;274(5295):2107-10. PMID:8953047

Page seeded by OCA on Mon Jun 30 22:59:58 2008

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