Literature summary for 3.4.24.33 extracted from

Tetaz, T.; Morrison, J.R.; Andreou, J.; Fidge, N.H.
Relaxed specificity of endoproteinase Asp-N: this enzyme cleaves at peptide bonds N-terminal to glutamate as well as aspartate and cysteic acid residues (1990), Biochem. Int., 22, 561-566.

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Organism

Organism	UniProt	Comment	Textmining
Pseudomonas fragi	-	mutant	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Apolipoprotein A-I + H2O	2 CNBr-fragments, cleavage at 12 Asp-residues and 5 out of 18 Glu-residues, cleaves N-terminal to Glu as well as to Asp and cysteic acid	Pseudomonas fragi	Peptides	amino acid sequences	?
additional information	cleavage specificity	Pseudomonas fragi	?	-	?

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Release 2023.1 (January 2023)