1SLL

SIALIDASE L FROM LEECH MACROBDELLA DECORA

1SLL の概要

• エントリーDOI: 10.2210/pdb1sll/pdb
• 分子名称: SIALIDASE L (2 entities in total)
• 機能のキーワード: hydrolase, sialidase
• 由来する生物種: Macrobdella decora (North American leech)
• 細胞内の位置: Secreted, extracellular space: Q27701
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 74565.69

構造登録者

Luo, Y.,Li, S.C.,Chou, M.Y.,Li, Y.T.,Luo, M. (登録日: 1997-10-14, 公開日: 1998-12-16, 最終更新日: 2024-02-14)

主引用文献

Luo, Y.,Li, S.C.,Chou, M.Y.,Li, Y.T.,Luo, M.
The crystal structure of an intramolecular trans-sialidase with a NeuAc alpha2-->3Gal specificity.
Structure, 6:521-530, 1998

PubMed Abstract: Intramolecular trans-sialidase from leech (Macrobdella decora) is a unique enzyme which cleaves the terminal neuraminic acid (NeuAc) residue from sialoglycoconjugates, releasing 2, 7-anhydro-neuraminic acid (2,7-anhydro-NeuAc). It is the first enzyme found to exhibit strictly specific cleavage of NeuAc alpha2-->3Gal linkages in sialoglycoconjugates. The release of 2,7-anhydro-NeuAc instead of NeuAc implies a unique mechanism, in which the sialosyl linkage is transferred within the sialoglycoconjugate rather than hydrolyzed. The aims of the structural study were to gain structural insight into the strict specificity and unique mechanism of this unusual enzyme.

PubMed: 9562562
DOI: 10.1016/S0969-2126(98)00053-7

実験手法

X-RAY DIFFRACTION (2 Å)