3.4.24.20: peptidyl-Lys metalloendopeptidase
This is an abbreviated version!
For detailed information about peptidyl-Lys metalloendopeptidase, go to the full flat file.
Word Map on EC 3.4.24.20
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3.4.24.20
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frondosa
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collision
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grifola
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collision-induced
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pleurotus
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ostreatus
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b-ions
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molecular biology
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silac
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lysine-specific
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synthesis
- 3.4.24.20
- frondosa
-
collision
-
grifola
-
collision-induced
-
pleurotus
- ostreatus
-
b-ions
- molecular biology
-
silac
-
lysine-specific
- synthesis
Reaction
Preferential cleavage in proteins: -Xaa-/-Lys- (in which Xaa may be Pro) =
Synonyms
Am-LysN, Armillaria mellea neutral proteinase, aspzincin metalloendopeptidase, aspzincin metalloprotease, EC 3.4.99.30, EC 3.4.99.32, GFMEP, Lys-N, LysN, MEP, peptidyl-Lys metalloendopeptidase, peptidyl-Lys metallopeptidase, Peptidyllysine metalloproteinase, POMEP, Proteinase, peptidyllysine metallo-
ECTree
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Application
Application on EC 3.4.24.20 - peptidyl-Lys metalloendopeptidase
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molecular biology
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biological application for enzyme-based proteolytic 18O labeling method characterizing the proteome changes of cytokine/lipolysaccharide-treated versus untreated human retinal pigment epithelium cell line
molecular biology
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proteolytic 18O labeling method employing enzyme for use in comparative proteomics. Enzyme incorporates only a single 18O atom into the carboxyl terminus of each proteolytically generated peptide. Method provides accurate quantification results for isotopically labeled peptides
molecular biology
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a method for detecting protein termini on both the amino and the carboxyl side, regardless of terminal modifications, such as N-acetylation is established. This method requires LC-MS/MS combined with two endopeptidases (lysyl endopeptidase) Lys-C and peptidyl-Lys metalloendopeptidase (Lys-N)