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Literature summary extracted from
- Cloning and characterization of a leucine aminopeptidase from Pseudoalteromonas telluritireducens DSM 16098, a strain isolated from hydrothermal vents fluid (2018), Deep-Sea Res. Part I: Oceanogr. Res. Pap., 138, 114-121 .
No PubMed abstract available
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.1 | gene lap, sequence comparisons, functional recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Transetta (DE3) | Pseudoalteromonas telluritireducens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.1 | Ca2+ | 40% inhibition at 1 mM, 54% at 10 mM | Pseudoalteromonas telluritireducens |  |
| 3.4.11.1 | Cd2+ | complete inhibition at 10 mM | Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | Co2+ | 17% inhibition at 1 mM, 63% at 10 mM | Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | Cu2+ | complete inhibition at 0.1 mM | Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | EDTA | strong inhibition | Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | Mg2+ | 34% inhibition at 1 mM, 55% at 10 mM | Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | Mn2+ | 19% inhibition at 1 mM, 53% at 10 mM | Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | PMSF | - |
Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | Zn2+ | complete inhibition at 1.0 mM | Pseudoalteromonas telluritireducens | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.1 | additional information | - |
additional information | Michaelis-Menten kinetics | Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | 0.04456 | - |
L-Leu 7-amido-4-methylcoumarin | pH 7.2, 28°C, recombinant enzyme | Pseudoalteromonas telluritireducens | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.11.1 | extracellular | - |
Pseudoalteromonas telluritireducens | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.1 | additional information | the enzyme is relatively tolerant to Mn2+ which is enriched in hydrothermal vent fluids | Pseudoalteromonas telluritireducens | |
| 3.4.11.1 | NaCl | activates | Pseudoalteromonas telluritireducens | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.1 | Pseudoalteromonas telluritireducens | A0A3S6IVW5 | a strain of deep-sea bacteria isolated from hydrothermal vents fluid | - |
| 3.4.11.1 | Pseudoalteromonas telluritireducens DSM 16098 | A0A3S6IVW5 | a strain of deep-sea bacteria isolated from hydrothermal vents fluid | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.1 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Transetta (DE3) by nickel affinity chromatography | Pseudoalteromonas telluritireducens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.1 | L-Leu 7-amido-4-methylcoumarin + H2O | - |
Pseudoalteromonas telluritireducens | L-Leu + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.11.1 | L-Leu 7-amido-4-methylcoumarin + H2O | - |
Pseudoalteromonas telluritireducens DSM 16098 | L-Leu + 7-amino-4-methylcoumarin | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.1 | ? | x * 69370, sequence calculation | Pseudoalteromonas telluritireducens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.1 | LAP | - |
Pseudoalteromonas telluritireducens |
| 3.4.11.1 | leucine aminopeptidase | - |
Pseudoalteromonas telluritireducens |
| 3.4.11.1 | PtLAP | - |
Pseudoalteromonas telluritireducens |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.1 | 42 | - |
assay at | Pseudoalteromonas telluritireducens |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.1 | 4 | 60 | activity range, profile overview | Pseudoalteromonas telluritireducens |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.1 | 30 | - |
purified recombinant enzyme, pH 7.2, 90 min, 86.78% activity remaining | Pseudoalteromonas telluritireducens |
| 3.4.11.1 | 40 | - |
purified recombinant enzyme, pH 7.2, 90 min, 72.88% activity remaining | Pseudoalteromonas telluritireducens |
| 3.4.11.1 | 50 | - |
purified recombinant enzyme, pH 7.2, 3 min, 50% activity remaining | Pseudoalteromonas telluritireducens |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.1 | 7.2 | - |
assay at | Pseudoalteromonas telluritireducens |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.1 | 6 | 12.5 | activity range, the maximal activity ranging at pH 7.2-8.0, relative activity is 37.61-35.51% at pH 9.0-10.5. At pH 6.6 and 12.2, only 5.8% and 7.76% of the maximal activity is retained, respectively, while activity is hardly detected at pH lower than 6.0 or higher than pH 12.5 | Pseudoalteromonas telluritireducens |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.4.11.1 | Pseudoalteromonas telluritireducens | sequence calculation | - |
5.42 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.11.1 | evolution | the putative substrate binding site GGMEN, zinc-binding motif HEXXHX18E and the catalytic residues involved in aminopeptidase activity are all conserved, PtLAP is a member of M1 leucine aminopeptidases | Pseudoalteromonas telluritireducens |
| 3.4.11.1 | additional information | the enzyme contains a signal peptide (residues 1-21), a peptidase_M1 domain (Pfam 01433, residues 32-398) and a leuk-A4-hydro_C domain (SMART 001263, residues 474-612) in PtLAP. Both of the putative substrate binding site GGMEN and zinc-binding motif HEXXHX18E in peptidase_M1 domain are conserved in PtLAP, locating from ressidues 282-286 and 309-332, respectively. The catalytic residues involved in aminopeptidase activity are Glu285 and Tyr395 in PtLAP, which probably act as a general base and a proton donor | Pseudoalteromonas telluritireducens |
| 3.4.11.1 | physiological function | leucine aminopeptidases (LAPs) are metallopeptidases that catalyze the hydrolysis of leucine residues and other N-terminal residues from proteins and peptides. The extracellular enzyme PtLAP executes the degradation of organic matters, contributes to the adaptive survival of microbe in deep-sea environment and may play important roles in marine biogeochemical cycles. The recombinant enzyme rPtLAP can significantly promote the proliferation of tumor cells, including the cell lines HCT116, BEL-7402 and Hela, while displays no effect on that of normal cell line 3T3 | Pseudoalteromonas telluritireducens |
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