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Literature summary for 3.4.21.50 extracted from

  • Achour, B.; Barber, J.
    The activities of Achromobacter lysyl endopeptidase and Lysobacter lysyl endoproteinase as digestive enzymes for quantitative proteomics (2013), Rapid Commun. Mass Spectrom., 27, 1669-1672.
    View publication on PubMed
Search for more literature for 3.4.21.50

Application

Application Comment Organism
analysis the enzyme is attractive for the proteolytic generation of peptides to be analyzed by mass spectrometry, usage in quantitative mass spectrometry, overview. It can be used in the presence of protein denaturants which allow better access to cleavage sites and hence better proteolysis. The enzyme has advantages over trypsin, namely, reduced missed cleavage (because KR and RK are cleaved specifically), tolerance to denaturants and requirement for only a single labelled amino acid in experiments using isotopic labelling Achromobacter lyticus
analysis the enzyme is attractive for the proteolytic generation of peptides to be analyzed by mass spectrometry, usage in quantitative mass spectrometry, overview. It can be used in the presence of protein denaturants which allow better access to cleavage sites and hence better proteolysis. The enzyme has advantages over trypsin, namely, reduced missed cleavage (because KR and RK are cleaved specifically), tolerance to denaturants and requirement for only a single labelled amino acid in experiments using isotopic labelling Lysobacter enzymogenes

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Achromobacter lyticus
Ca2+ required Lysobacter enzymogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
30000
-
 about Achromobacter lyticus
30000
-
 about Lysobacter enzymogenes

Organism

Organism UniProt Comment Textmining
Achromobacter lyticus P15636 gene lysC
-
Lysobacter enzymogenes Q7M135 gene lysC
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Achromobacter lyticus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
50S ribosomal protein L7/L12 + H2O cleavage into 5 peptide fragments Achromobacter lyticus ?
-
 ?
50S ribosomal protein L7/L12 + H2O cleavage into 5 peptide fragments Lysobacter enzymogenes ?
-
 ?
6-phosphogluconate dehydrogenase + H2O cleavage into 6 peptide fragments Lysobacter enzymogenes ?
-
 ?
6-phosphogluconate dehydrogenase + H2O cleavage into 7 peptide fragments Achromobacter lyticus ?
-
 ?
acyl carrier protein + H2O cleavage into 3 peptide fragments Achromobacter lyticus ?
-
 ?
acyl carrier protein + H2O cleavage into 3 peptide fragments Lysobacter enzymogenes ?
-
 ?
chaperone protein DNA kinase + H2O cleavage into 10 peptide fragments Achromobacter lyticus ?
-
 ?
chaperone protein DNA kinase + H2O cleavage into 9 peptide fragments Lysobacter enzymogenes ?
-
 ?
elongation factor G + H2O cleavage into 5 peptide fragments Lysobacter enzymogenes ?
-
 ?
elongation factor G + H2O cleavage into 8 peptide fragments Achromobacter lyticus ?
-
 ?
elongation factor Tu + H2O cleavage into 5 peptide fragments Lysobacter enzymogenes ?
-
 ?
elongation factor Tu + H2O cleavage into 7 peptide fragments Achromobacter lyticus ?
-
 ?
enolase + H2O cleavage into 4 peptide fragments Achromobacter lyticus ?
-
 ?
enolase + H2O cleavage into 4 peptide fragments Lysobacter enzymogenes ?
-
 ?
fructose-bisphosphate aldolase class 2 + H2O cleavage into 4 peptide fragments Lysobacter enzymogenes ?
-
 ?
fructose-bisphosphate aldolase class 2 + H2O cleavage into 5 peptide fragments Achromobacter lyticus ?
-
 ?
glyceraldehyde-3-phosphate dehydrogenase A + H2O cleavage into 5 peptide fragments Achromobacter lyticus ?
-
 ?
glyceraldehyde-3-phosphate dehydrogenase A + H2O cleavage into 6 peptide fragments Lysobacter enzymogenes ?
-
 ?
additional information the enzyme is specific for the C-terminal side of lysine residues, protein and peptide digestion efficiency, usage of quantitative mass spectrometry, analysis of miscleavage and non-cleavage, overview Achromobacter lyticus ?
-
 ?
additional information the enzyme is specific for the C-terminal side of lysine residues, protein and peptide digestion efficiency, usage of quantitative mass spectrometry, analysis of miscleavage and non-cleavage, overview Lysobacter enzymogenes ?
-
 ?
phosphoglycerate kinase + H2O cleavage into 4 peptide fragments Achromobacter lyticus ?
-
 ?
phosphoglycerate kinase + H2O cleavage into 4 peptide fragments Lysobacter enzymogenes ?
-
 ?

Synonyms

Synonyms Comment Organism
Achromobacter lysyl endopeptidase
-
 Achromobacter lyticus
Lys-C
-
 Achromobacter lyticus
Lys-C
-
 Lysobacter enzymogenes
Lysobacter lysyl endoproteinase
-
 Lysobacter enzymogenes

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Achromobacter lyticus
37
-
 assay at Lysobacter enzymogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Achromobacter lyticus
8
-
 assay at Lysobacter enzymogenes

General Information

General Information Comment Organism
evolution the enzyme belongs to the family of serine proteases Achromobacter lyticus
evolution the enzyme belongs to the family of serine proteases Lysobacter enzymogenes
additional information the additional disulfide bond (Cys6-Cys216) in the structure of lysyl endopeptidases, compared to trypsin, is thought to be responsible for their optimum activity at basic pH-values, 8.5-10.7, and their high resistance to denaturants Achromobacter lyticus
additional information the additional disulfide bond (Cys6-Cys216) in the structure of lysyl endopeptidases, compared to trypsin, is thought to be responsible for their optimum activity at basic pH-values, 8.5-10.7, and their high resistance to denaturants Lysobacter enzymogenes