Flavastacin

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
Flavastacin
Identifiers
EC number3.4.24.76
CAS number167973-66-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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

  1. 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.
  2. 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.
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