1tve: Difference between revisions

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[[Image:1tve.~~gif~~|left|200px]]

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

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~~'''~~Homoserine Dehydrogenase in complex with 4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol~~'''~~

===Homoserine Dehydrogenase in complex with 4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol===

~~==Overview==~~

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~~A relatively unexploited potential target for antimicrobial agents is~~ the ~~biosynthesis of essential amino acids. Homoserine dehydrogenase, which reduces aspartate semi-aldehyde~~ to ~~homoserine in a NAD~~(P)~~H-dependent reaction~~, is ~~one such target that is required for~~ the ~~biosynthesis of Met, Thr, and Ile from Asp~~. ~~We report a small molecule screen of yeast homoserine dehydrogenase that has identified a new class of phenolic inhibitors of this class of enzyme. X~~-ray crystal structural analysis of one of the inhibitors in complex with homoserine dehydrogenase reveals that these molecules bind in the amino acid binding region of the active site and that the phenolic hydroxyl group interacts specifically with the backbone amide of Gly175. These results provide the first nonamino acid inhibitors of this class of enzyme and have the potential to be exploited as leads in antifungal compound design.

The line below this paragraph, {{ABSTRACT_PUBMED_15210149}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15210149 is the PubMed ID number.

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==About this Structure==

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[[Category: Antifungal]]

[[Category: Small molecule screening]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 10~~:24:55 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:08:31 2008''

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-[[Image:1tve.gif|left|200px]]
+{{Seed}}
+[[Image:1tve.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1tve|  PDB=1tve  |  SCENE=  }}
-'''Homoserine Dehydrogenase in complex with 4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol'''
+===Homoserine Dehydrogenase in complex with 4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol===
-==Overview==
+<!--
-A relatively unexploited potential target for antimicrobial agents is the biosynthesis of essential amino acids. Homoserine dehydrogenase, which reduces aspartate semi-aldehyde to homoserine in a NAD(P)H-dependent reaction, is one such target that is required for the biosynthesis of Met, Thr, and Ile from Asp. We report a small molecule screen of yeast homoserine dehydrogenase that has identified a new class of phenolic inhibitors of this class of enzyme. X-ray crystal structural analysis of one of the inhibitors in complex with homoserine dehydrogenase reveals that these molecules bind in the amino acid binding region of the active site and that the phenolic hydroxyl group interacts specifically with the backbone amide of Gly175. These results provide the first nonamino acid inhibitors of this class of enzyme and have the potential to be exploited as leads in antifungal compound design.
+The line below this paragraph, {{ABSTRACT_PUBMED_15210149}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15210149 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15210149}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Antifungal]]
 [[Category: Small molecule screening]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:24:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:08:31 2008''