1dfh: Difference between revisions

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[[Image:1dfh.~~jpg~~|left|200px]]

[[Image:1dfh.png|left|200px]]

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

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8953047}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8953047 is the PubMed ID number.

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==About this Structure==

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[[Category: Lipid biosynthesis]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:47:44 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:59:58 2008''

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-[[Image:1dfh.jpg|left|200px]]
+{{Seed}}
+[[Image:1dfh.png|left|200px]]
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 {{STRUCTURE_1dfh|  PDB=1dfh  |  SCENE=  }}
-'''X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE'''
+===X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8953047}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8953047 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8953047}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Lipid biosynthesis]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:47:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:59:58 2008''