EC Number   |
Title |
Organism |
|---|
   3.4.13.21 | Structure of Asp-bound peptidase E from Salmonella enterica Active site at dimer interface illuminates Asp recognition |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.13.21 | Aspartate-specific peptidases in Salmonella typhimurium: mutants deficient in peptidase E |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.13.21 | Cloning and nucleotide sequence of the cyclic AMP receptor protein-regulated Salmonella typhimurium pepE gene and crystallization of its product, an alpha-aspartyl dipeptidase |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.13.21 | Directed evolution of alpha-aspartyl dipeptidase from Salmonella typhimurium |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.13.21 | Electrophoretic variations of peptidase E (PEPE) in characterizing clones and isolates of Plasmodium falciparum from different geographical areas |
Plasmodium falciparum |
| 3.4.13.21 | Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase |
Salmonella enterica subsp. enterica serovar Typhimurium |
| 3.4.13.21 | Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase |
Xenopus laevis |
| 3.4.13.21 | Screening, purification, and identification of the enzyme producing N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester from l-isoasparagine and L-phenylalanine methyl ester |
Klebsiella aerogenes |
| 3.4.13.21 | Screening, purification, and identification of the enzyme producing N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester from l-isoasparagine and L-phenylalanine methyl ester |
Escherichia coli |
| 3.4.13.21 | Screening, purification, and identification of the enzyme producing N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester from l-isoasparagine and L-phenylalanine methyl ester |
Hafnia alvei |
