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Literature summary for 3.4.14.10 extracted from

  • Ekino, K.; Yonei, S.; Oyama, H.; Oka, T.; Nomura, Y.; Shin, T.
    Cloning, purification, and characterization of tripeptidyl peptidase from Streptomyces herbaricolor TY-21 (2018), Appl. Biochem. Biotechnol., 184, 239-252 .
    View publication on PubMed
Search for more literature for 3.4.14.10

Activating Compound

Activating Compound Comment Organism Structure
actinonin slight activation at 0.1 mM Kitasatospora herbaricolor
Arphamenine B slight activation at 0.1 mM Kitasatospora herbaricolor
leuhistin slight activation at 0.1 mM Kitasatospora herbaricolor
MAPI slight activation at 0.1 mg/ml Kitasatospora herbaricolor

Cloned(Commentary)

Cloned (Comment) Organism
gene tpp, DNA and amino acid sequence determination and analysis, recombinant expression of extracellular enzyme in Escherichia coli strains JM109 and XL-1 Blue Kitasatospora herbaricolor

Inhibitors

Inhibitors Comment Organism Structure
antipain
-
 Kitasatospora herbaricolor
APMSF
-
 Kitasatospora herbaricolor
Diprotin A
-
 Kitasatospora herbaricolor
EDTA
-
 Kitasatospora herbaricolor
leupeptin
-
 Kitasatospora herbaricolor
additional information no or poor inhibition by Streptomyces subtilisin inhibitor (SSI), API-2, 4-chloromercuribenzoate, 2,2'-dithiodipyridine, iodoacetate, talopeptin, Streptomyces pepsin inhibitor (S-PI), amastatin, bestatin, and arphamenine A Kitasatospora herbaricolor
PMSF
-
 Kitasatospora herbaricolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.88
-
 Ala-Ala-Phe-4-nitroanilide pH 7.5, 37°C, recombinant enzyme Kitasatospora herbaricolor

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Kitasatospora herbaricolor
-
-

Organism

Organism UniProt Comment Textmining
Kitasatospora herbaricolor D1MVE1 i.e. Kitasatospora herbaricolor
-
Kitasatospora herbaricolor TY-21 D1MVE1 i.e. Kitasatospora herbaricolor
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli 790fold by ammonium sulfate fractionation, anion exchange chromatography, ultrafiltration, and gel filtration Kitasatospora herbaricolor

Source Tissue

Source Tissue Comment Organism Textmining
cell culture the extracellular enzyme is produced by the bacterium Streptomyces herbaricolor strain TY-21 during the late stationary growth phase Kitasatospora herbaricolor
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
15.7
-
 pH 7.5, 37°C, purified recombinant enzyme, substrate Ala-Ala-Phe-4-nitroanilide Kitasatospora herbaricolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ala-Phe-4-nitroanilide + H2O
-
 Kitasatospora herbaricolor Ala-Ala-Phe + 4-nitroaniline
-
 ?
Ala-Ala-Phe-4-nitroanilide + H2O
-
 Kitasatospora herbaricolor TY-21 Ala-Ala-Phe + 4-nitroaniline
-
 ?
Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower Kitasatospora herbaricolor Ala-Pro-Gly + Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
-
 ?
Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower Kitasatospora herbaricolor TY-21 Ala-Pro-Gly + Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
-
 ?
Ala-Pro-Val-Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower Kitasatospora herbaricolor Ala-Pro-Val + Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
-
 ?
Ala-Pro-Val-Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala + H2O sequence from interleukin-6, the first attack for tripeptide cleavage is relatively fast, but the second one is slower Kitasatospora herbaricolor TY-21 Ala-Pro-Val + Ala-Pro-Gly-Glu-Asp-Ser-Lys-Asp-Val-Ala-Ala
-
 ?
Gly-Ser-His-Leu-Leu-Glu-Ala + H2O sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower Kitasatospora herbaricolor Gly-Ser-His + Leu-Leu-Glu-Ala
-
 ?
Gly-Ser-His-Leu-Leu-Glu-Ala + H2O sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower Kitasatospora herbaricolor TY-21 Gly-Ser-His + Leu-Leu-Glu-Ala
-
 ?
Leu-Leu-Glu-Ala + H2O sequence from insulin B chain, the first attack for tripeptide cleavage is relatively fast, but the second one is slower Kitasatospora herbaricolor Leu-Leu-Glu + Ala
-
 ?
additional information tripeptidyl peptidase (TPP) is an exopeptidase that sequentially hydrolyzes tripeptides from the N-terminus of oligopeptides or polypeptides. Ala-Phe-pNA, Phe-pNA, Leu-pNA, and N-terminal-blocked peptides (Cbz-Ala-Ala-Phe-pNA and Cbz-Ala-Ala-Leu-pNA) are not hydrolyzed at all Kitasatospora herbaricolor ?
-
 ?
additional information tripeptidyl peptidase (TPP) is an exopeptidase that sequentially hydrolyzes tripeptides from the N-terminus of oligopeptides or polypeptides. Ala-Phe-pNA, Phe-pNA, Leu-pNA, and N-terminal-blocked peptides (Cbz-Ala-Ala-Phe-pNA and Cbz-Ala-Ala-Leu-pNA) are not hydrolyzed at all Kitasatospora herbaricolor TY-21 ?
-
 ?

Subunits

Subunits Comment Organism
? x * 38000, recombinant enzyme, SDS-PAGE Kitasatospora herbaricolor
More enzyme N-terminal peptide mapping Kitasatospora herbaricolor

Synonyms

Synonyms Comment Organism
TPP
-
 Kitasatospora herbaricolor
tripeptidyl peptidase
-
 Kitasatospora herbaricolor
TY-21 TPP
-
 Kitasatospora herbaricolor

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Kitasatospora herbaricolor

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 purified recombinant enzyme, 60 min, stable Kitasatospora herbaricolor

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
43
-
 Ala-Ala-Phe-4-nitroanilide pH 7.5, 37°C, recombinant enzyme Kitasatospora herbaricolor

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Kitasatospora herbaricolor

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 9 purified recombinant enzyme, 4°C, 24 h, stable Kitasatospora herbaricolor

General Information

General Information Comment Organism
evolution the enzyme belongs to the peptidase S8 family. TY-21 TPP shows no homology with mammalian TPPII, but shows relatively higher homology with TPP S (49%). Alignment of the protein sequences of TY-21 TPP with TPP S and subtilisin reveal three conserved regions around the catalytic triad in the active site in these enzymes that are specific for subtilisin Kitasatospora herbaricolor
physiological function tripeptidyl peptidases (TPPs) are unique exopeptidases that cleave tripeptide units from oligopeptides or polypeptides. It is required to degrade unnecessary proteins in cells for sustaining life. In this process, TPP plays an important role and is present in lysosomes and the cytosol. There are two kinds of TPPs in mammals, TPPI (EC 3.4.14.9) and TPPII (EC 3.4.14.10) Kitasatospora herbaricolor

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
48.9
-
 Ala-Ala-Phe-4-nitroanilide pH 7.5, 37°C, recombinant enzyme Kitasatospora herbaricolor