1w8o
From Proteopedia
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==Overview== | ==Overview== | ||
| - | A recombinant D92G mutant sialidase from Micromonospora viridifaciens has | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Micromonospora viridifaciens]] | [[Category: Micromonospora viridifaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bennet, A | + | [[Category: Bennet, A J.]] |
[[Category: Dookhun, V.]] | [[Category: Dookhun, V.]] | ||
[[Category: Newstead, S.]] | [[Category: Newstead, S.]] | ||
[[Category: Taylor, G.]] | [[Category: Taylor, G.]] | ||
| - | [[Category: Watson, J | + | [[Category: Watson, J N.]] |
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: sialidase]] | [[Category: sialidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:36 2008'' |
Revision as of 13:41, 21 February 2008
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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.
About this Structure
1W8O is a Single protein structure of sequence from Micromonospora viridifaciens with , , and as ligands. Active as Exo-alpha-sialidase, with EC number 3.2.1.18 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Contribution of the active site aspartic acid to catalysis in the bacterial neuraminidase from Micromonospora viridifaciens., Watson JN, Newstead S, Dookhun V, Taylor G, Bennet AJ, FEBS Lett. 2004 Nov 5;577(1-2):265-9. PMID:15527797
Page seeded by OCA on Thu Feb 21 15:41:36 2008
Categories: Exo-alpha-sialidase | Micromonospora viridifaciens | Single protein | Bennet, A J. | Dookhun, V. | Newstead, S. | Taylor, G. | Watson, J N. | CIT | GOL | LBT | NA | 3d-structure | Beta-propeller | Glycosidase | Hydrolase | Sialidase
