1W8N

Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens.

1W8N の概要

• エントリーDOI: 10.2210/pdb1w8n/pdb
• 関連するPDBエントリー: 1EUR 1EUS 1EUT 1EUU
• 分子名称: BACTERIAL SIALIDASE, beta-D-galactopyranose, 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID, ... (5 entities in total)
• 機能のキーワード: glycosidase, hydrolase, neuraminidase, beta- propeller fold.
• 由来する生物種: MICROMONOSPORA VIRIDIFACIENS
• 細胞内の位置: Secreted: Q02834
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64735.00

構造登録者

Newstead, S.,Watson, J.N.,Dookhun, V.,Bennet, A.J.,Taylor, G. (登録日: 2004-09-24, 公開日: 2004-09-30, 最終更新日: 2024-11-06)

主引用文献

Watson, J.N.,Newstead, S.,Dookhun, V.,Taylor, G.,Bennet, A.J.
Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora Viridifaciens
FEBS Lett., 577:265-, 2004

PubMed Abstract: 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.

PubMed: 15527797
DOI: 10.1016/J.FEBSLET.2004.10.016

実験手法

X-RAY DIFFRACTION (2.1 Å)