EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.11.10 | DNA and amino acid sequence determination and analysis | Vibrio proteolyticus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.4.11.10 | free Zn-enzyme or enzyme in complex with synthetic inhibitor 4-iodo-D-phenylalanine hydroxamate, X-ray diffraction structure determination and analysis at 1.8 A resolution | Vibrio proteolyticus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.11.10 | 4-iodo-D-phenylalanine hydroxamate | - |
Vibrio proteolyticus | |
3.4.11.10 | D-Leu-4-nitroanilide | D-isomers of the substrates inhibit the enzyme | Vibrio proteolyticus | |
3.4.11.10 | D-Val-4-nitroanilide | D-isomers of the substrates inhibit the enzyme | Vibrio proteolyticus | |
3.4.11.10 | L-leucinethiol | - |
Vibrio proteolyticus | |
3.4.11.10 | additional information | inhibition mechanisms, overview | Vibrio proteolyticus | |
3.4.11.10 | N-mercapto-leucyl-4-nitroanilides | - |
Vibrio proteolyticus |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.11.10 | extracellular | - |
Vibrio proteolyticus | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.11.10 | Zn2+ | the enzyme is a two-zinc metallopeptidase, zinc-binding involved residues His97, Asp117, Glu152, Asp179, and His256 | Vibrio proteolyticus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.11.10 | Vibrio proteolyticus | - |
formerly Aeromonas proteolytica, marine bacterium | - |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.4.11.10 | proteolytic modification | the proenzyme contains a 21-amino acid-signal peptide, and a 84-amino acid N-terminal propeptide, 299 amino acids form the mature protein part, and 100 amino acids form the C-terminal propeptide | Vibrio proteolyticus |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.4.11.10 | extracellular enzyme to homogeneity by ion exchange and hydrophobic interaction chromatography, or by heat treatment at 70°C | Vibrio proteolyticus |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.4.11.10 | Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. | structure-activity relationship, active site structure involving zinc-binding ligands His97, Asp117, Asp179, Glu151, Glu152, and His256 | Vibrio proteolyticus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.11.10 | L-Leu-4-nitroanilide + H2O | - |
Vibrio proteolyticus | L-Leu + 4-nitroaniline | - |
? | |
3.4.11.10 | additional information | the enzyme prefers substrates with large and hydrophobic N-terminal amino acid residues | Vibrio proteolyticus | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.4.11.10 | monomer | 1 * 30000-32000, mature active enzyme | Vibrio proteolyticus |
3.4.11.10 | More | the proenzyme contains a 21-amino acid-signal peptide, and a 84-amino acid N-terminal propeptide, 299 amino acids form the mature protein part, and 100 amino acids form the C-terminal propeptide | Vibrio proteolyticus |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.11.10 | aminopeptidase Ap1 | - |
Vibrio proteolyticus |
3.4.11.10 | More | the enzyme belongs to the peptidase family M28A | Vibrio proteolyticus |
3.4.11.10 | Vibrio aminopeptidase | - |
Vibrio proteolyticus |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.4.11.10 | 70 | - |
several hours, stable | Vibrio proteolyticus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.4.11.10 | 0.0000025 | 0.000057 | N-mercapto-leucyl-4-nitroanilides | - |
Vibrio proteolyticus | |
3.4.11.10 | 0.000007 | - |
L-leucinethiol | - |
Vibrio proteolyticus |