Activating Compound | Comment | Organism | Structure |
---|---|---|---|
bicarbonate | activates | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
crystallization at pH 8.0 of enzyme in high salt Tris buffer against low salt concentration, X-ray diffraction crystal structure determination and analysis at 2.5 A resolution | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | metallopeptidase, dimetal site structure, overview | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Escherichia coli | PepA acts as DNA-binding protein in Xer site-specific DNA recombination serving as accessory protein | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. | catalytic mechanism | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Leu-4-nitroanilide + H2O | - |
Escherichia coli | L-Leu + 4-nitroaniline | - |
? | |
additional information | PepA acts as DNA-binding protein in Xer site-specific DNA recombination serving as accessory protein | Escherichia coli | ? | - |
? | |
additional information | PepA binds DNA probably along the large groove that runs from the lower trimer face across the twofold molecular axis to the upper trimer face | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexamer | lens enzyme three-dimensional structure and protein fold, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
LAP | - |
Escherichia coli |
leucine aminopeptidase | - |
Escherichia coli |
More | the enzyme belongs to the peptidase family M17 | Escherichia coli |
PepA | - |
Escherichia coli |