CMP-dependent sialidase activity
US11788108B2 · kind B2 · utility
Assignee
Inventors
Key dates
| Filing date | Jun 23, 2021 |
| Grant date | Oct 17, 2023 |
| Priority date | — |
| Expiry date | Jun 23, 2041 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC07K2317/41
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
The properties of certain glycosyltransferase variants having N-terminal truncation deletions or internal deletions are disclosed. Particularly, mutants that exhibit α-2,6-sialyltransferase enzymatic activity in the presence of CMP-activated sialic acid as co-substrate, and in the presence of a suitable acceptor site, are disclosed. A fundamental finding documented in the present disclosure is that enzymes are not only capable of catalyzing transfer of a sialidyl moiety but they are also capable of catalyzing hydrolytic cleavage of terminally bound sialic acid from a glycan.
Source: USPTO / EPO open patent data. Objective bibliographic and citation counts.