1SLL

SIALIDASE L FROM LEECH MACROBDELLA DECORA

Summary for 1SLL

• Entry DOI: 10.2210/pdb1sll/pdb
• Descriptor: SIALIDASE L (2 entities in total)
• Functional Keywords: hydrolase, sialidase
• Biological source: Macrobdella decora (North American leech)
• Cellular location: Secreted, extracellular space: Q27701
• Total number of polymer chains: 1
• Total formula weight: 74565.69

Authors

Luo, Y.,Li, S.C.,Chou, M.Y.,Li, Y.T.,Luo, M. (deposition date: 1997-10-14, release date: 1998-12-16, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)