1dfi: Difference between revisions

Line 1:

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

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

<!--

Line 9:

Line 10:

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

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

~~==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.

-->

==About this Structure==

Line 27:

Line 31:

[[Category: Lipid biosynthesis]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:47:54 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:00:01 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1dfi.jpg|left|200px]]
+{{Seed}}
+[[Image:1dfi.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dfi|  PDB=1dfi  |  SCENE=  }}
-'''X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD'''
+===X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD===
-==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 27: / Line 31: @@
 [[Category: Lipid biosynthesis]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:47:54 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:00:01 2008''