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Literature summary for 3.4.21.19 extracted from

  • Kalyankar, P.; Zhu, Y.; OKeeffe, M.; OCuinn, G.; FitzGerald, R.J.
    Substrate specificity of glutamyl endopeptidase (GE): hydrolysis studies with a bovine alpha-casein preparation (2013), Food Chem., 136, 501-512.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
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Purification (Commentary)

Purification (Comment) Organism
phenyl Sepharose 6 column chromatography and HiTrap-CM column chromatography Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O the enzyme is highly specific and hydrolyses the peptide bond predominantly on the carboxy side of Glu residues while hydrolysis on the carboxyl side of Asp residues is also observed. Hydrolysis does not occur while Pro is at the P1' position. In Glu-Glu-X (X equals Arg, Asn, Ile and Ser) and Glu-Glu-Glu-Lys sequences, hydrolysis of Glu-X and Glu-Lys is preferred Bacillus licheniformis ?
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N-acetyl-L-Glu-4-nitroanilide + H2O
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Bacillus licheniformis N-acetyl-L-Glu + 4-nitroaniline
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Synonyms

Synonyms Comment Organism
Alcalase commercial preparation containing subtilisin and glutamyl endopeptidase activities Bacillus licheniformis