Flavastacin
| Flavastacin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.76 | ||||||||
| CAS no. | 167973-66-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Flavastacin (EC 3.4.24.76) is an enzyme.[1] This enzyme catalyses the following chemical reaction
- Hydrolyses polypeptides on the amino-side of Asp in -Xaa-Asp-. Acts very slowly on -Xaa-Glu
This zinc metalloendopeptidase belong to the peptidase family M12. It has recently been described as cleaving specifically after N-glycosylated asparagine, making it a potentially useful as a tool to analytically characterize glycoproteins.[2]
References
[edit]- ^ Tarentino, A.L.; Quinones, G.; Grimwood, B.G.; Hauer, C.R.; Plummer, T.H. Jr. (1995). "Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase". Arch. Biochem. Biophys. 319: 281–285. doi:10.1006/abbi.1995.1293. PMID 7771796.
- ^ Pralow A, Hoffmann M, Nguyen-Khuong T, Rapp E, Reichl U (2017). "Improvement of the glycoproteomic toolbox with the discovery of a unique C-terminal cleavage specificity of flavastacin for N-glycosylated asparagine". Sci Rep. 7 (1): 11419. doi:10.1038/s41598-017-11668-1. PMC 5595805. PMID 28900186.
External links
[edit]- Flavastacin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
