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Literature summary for 3.4.11.1 extracted from

  • Zhang, S.; Cai, X.; Luo, X.; Wang, S.; Guo, A.; Hou, J.; Wu, R.
    Molecular cloning and characterization of leucine aminopeptidase gene from Taenia pisiformis (2018), Exp. Parasitol., 186, 1-9 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
TpLAP, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative real-time PCR enzyme expression analysis, recombinant expression of soluble GST-tagged TpLAP in Escherichia coli strain Transetta (DE3), subcloning in Escherichia coli strain DH5alpha cells Taenia pisiformis

Inhibitors

Inhibitors Comment Organism Structure
bestatin complete inhibition at 20 nM Taenia pisiformis
EDTA complete inhibition at 0.15 mM Taenia pisiformis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ activates Taenia pisiformis
Mn2+ strong activation Taenia pisiformis
additional information a metalloexopeptidase, TpLAP activity is metal-ion dependent and strongly enhanced by the addition of Mn2+ and Co2+. In contrast, Mg2+, Zn2+, Ca2+, and Ba2+ do not influence enzymatic activities Taenia pisiformis

Organism

Organism UniProt Comment Textmining
Taenia pisiformis A0A2I7M6F6
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-

Source Tissue

Source Tissue Comment Organism Textmining
additional information native TpLAP enzyme is detected specifically in ES components of adult Taenia pisiformis by immunohistochemistry. Quantitative real-time PCR reveals that the TpLAP gene is expressed at a high level in adult worm tissues, especially in the gravid proglottids. TpLAP is located primarily in the subtegumental parenchyma zone and the uterine wall of adult worms. The enzyme is a stage-differentially expressed protein. The enzyme is significantly upregulated in immature proglottids and gravid proglottids (10.36fold and 50.71fold, respectively) in the adult stage compared against the larval stage Taenia pisiformis
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parenchyma subtegumental parenchyma zone Taenia pisiformis
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proglottid the enzyme is significantly upregulated in immature proglottids and gravid proglottids (10.36fold and 50.71fold, respectively) in the adult stage compared against the larval stage Taenia pisiformis
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uterus wall Taenia pisiformis
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
recombinant GST-TpLAP displays a hydrolyzing activity for Leu-4-nitroanilide with a maximum activity of 46 U/ml Taenia pisiformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Leu-4-nitroanilide + H2O
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Taenia pisiformis Leu + 4-nitroaniline
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?

Subunits

Subunits Comment Organism
? x * 56400, about, sequence calculation Taenia pisiformis

Synonyms

Synonyms Comment Organism
LAP
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Taenia pisiformis
leucine aminopeptidase
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Taenia pisiformis
TpLAP
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Taenia pisiformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
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recombinant enzyme Taenia pisiformis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4 65 activity range, profile overview Taenia pisiformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5
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recombinant enzyme Taenia pisiformis

pH Range

pH Minimum pH Maximum Comment Organism
7.5 11 activity range, profile overview Taenia pisiformis

General Information

General Information Comment Organism
evolution the enzyme belongs to the M17 family of proteases Taenia pisiformis
physiological function leucine aminopeptidase is an important metalloexopeptidase that catalyze the hydrolysis of N-terminal leucine residues from polypeptides and proteins Taenia pisiformis