Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant E151HA and E151D enzymes in Escherichia coli strain BL21(DE3) | Vibrio proteolyticus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of apoenzyme and metal-bound wild-type and mutant enzymes, isothermal titration measurement, thermodynamics, overview | Vibrio proteolyticus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | can substitute for one or both Zn2+ ions | Vibrio proteolyticus | |
additional information | detailed metal binding structure and kinetic analysis with recombinant wild-type and mutant enzymes, overview | Vibrio proteolyticus | |
Zn2+ | dinuclear Zn2+ metal center | Vibrio proteolyticus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio proteolyticus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, dialysis, hydrophobic interaction and anion exchange chromatography | Vibrio proteolyticus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. | active site residue Glu151 is essential for activity acting as a general acid/base during the catalytic reaction, mechanism of peptide hydrolysis | Vibrio proteolyticus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-Leu-4-nitroanilide + H2O | - |
Vibrio proteolyticus | L-Leu + 4-nitroaniline | - |
? |
Synonyms | Comment | Organism |
---|---|---|
leucine aminopeptidase | - |
Vibrio proteolyticus |