1w8o: Difference between revisions

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[[Image:1w8o.~~gif~~|left|200px]]

[[Image:1w8o.png|left|200px]]

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~~'''~~CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS~~'''~~

===CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS===

~~==Overview==~~

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~~A recombinant D92G mutant sialidase from Micromonospora viridifaciens has been cloned~~, ~~expressed and purified. Kinetic studies reveal that the replacement of~~ the conserved aspartic acid with glycine results in a catalytically competent retaining sialidase that possesses significant activity against activated substrates. The contribution of this aspartate residue to the ~~free energy of hydrolysis for natural substrates is greater than 19 kJ~~/~~mol~~. ~~The three dimensional structure of the D92G mutant shows that the removal of aspartic acid 92 causes no significant re-arrangement of the active site~~, ~~and that an ordered water molecule substitutes for~~ the ~~carboxylate group of D92~~.

The line below this paragraph, {{ABSTRACT_PUBMED_15527797}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15527797 is the PubMed ID number.

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==About this Structure==

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[[Category: Hydrolase]]

[[Category: Sialidase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 13~~:18:41 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:00:19 2008''

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-[[Image:1w8o.gif|left|200px]]
+{{Seed}}
+[[Image:1w8o.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1w8o|  PDB=1w8o  |  SCENE=  }}
-'''CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS'''
+===CONTRIBUTION OF THE ACTIVE SITE ASPARTIC ACID TO CATALYSIS IN THE BACTERIAL NEURAMINIDASE FROM MICROMONOSPORA VIRIDIFACIENS===
-==Overview==
+<!--
-A recombinant D92G mutant sialidase from Micromonospora viridifaciens has been cloned, expressed and purified. Kinetic studies reveal that the replacement of the conserved aspartic acid with glycine results in a catalytically competent retaining sialidase that possesses significant activity against activated substrates. The contribution of this aspartate residue to the free energy of hydrolysis for natural substrates is greater than 19 kJ/mol. The three dimensional structure of the D92G mutant shows that the removal of aspartic acid 92 causes no significant re-arrangement of the active site, and that an ordered water molecule substitutes for the carboxylate group of D92.
+The line below this paragraph, {{ABSTRACT_PUBMED_15527797}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15527797 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15527797}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Hydrolase]]
 [[Category: Sialidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:18:41 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:00:19 2008''