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Literature summary for 3.4.14.9 extracted from

  • Kondo, M.Y.; Gouvea, I.E.; Okamoto, D.N.; Santos, J.A.; Souccar, C.; Oda, K.; Juliano, L.; Juliano, M.A.
    Analysis of catalytic properties of tripeptidyl peptidase I (TTP-I), a serine carboxyl lysosomal protease, and its detection in tissue extracts using selective FRET peptide substrate (2016), Peptides, 76, 80-86 .
    View publication on PubMed
Search for more literature for 3.4.14.9

Activating Compound

Activating Compound Comment Organism Structure
KCl activates TPP-I at up to 1 M Rattus norvegicus
additional information tripeptidylamino peptidase activity is enhanced by the presence of amino acids in the prime side Rattus norvegicus

Application

Application Comment Organism
analysis development of fluorescence resonance energy transfer peptides using tryptophan as the fluorophore to study TPP-I hydrolytic properties. Assay can be applied to spleen and kidney homogenate Homo sapiens

General Stability

General Stability Organism
the enzyme shows resistance to hydrolysis by cathepsin D Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
Ac-RWFVIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
-
 Homo sapiens
Ca2+ activating up to 0.1, inhibitory above Homo sapiens
Ca2+
-
 Rattus norvegicus
K+ activating up to 0.1, inhibitory above Homo sapiens
additional information the enzyme is not inhibited by pepstatin, E-64, EDTA or PMSF. The enzyme shows resistance to hydrolysis by cathepsin D Rattus norvegicus
Na+ activating up to 0.1, inhibitory above Homo sapiens
NaCl
-
 Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00055
-
 RWFVIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens
0.0007
-
 RWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens
0.0007
-
 KWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome a serine carboxyl lysosomal protease Rattus norvegicus 5764
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activating up to 0.1, inhibitory above Homo sapiens
K+ activating up to 0.1, inhibitory above Homo sapiens
Na+ activating up to 0.1, inhibitory above Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O14773
-
-
Rattus norvegicus Q9EQV6
-
-
Rattus norvegicus Wistar Q9EQV6
-
-

Reaction

Reaction Comment Organism Reaction ID
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity the S4 subsite of TPP-I is occluded and there is an electrostatic interaction of the positively charged substrate N-terminus amino group and a negative locus in the region of the enzyme active site Rattus norvegicus
a

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
 Rattus norvegicus
-
spleen
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
-
 Rattus norvegicus Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
 ?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
-
 Rattus norvegicus Wistar Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
 ?
epsilon-aminocaproyl-WFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] + H2O
-
 Homo sapiens epsilon-aminocaproyl-WF + FIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
-
 ?
KWFFIQ-EDDnp + H2O rat spleen and kidney homogenates cleave only at F-F bond Rattus norvegicus KWF + FIQ-EDDnp
-
 ?
KWFFIQ-EDDnp + H2O rat spleen and kidney homogenates cleave only at F-F bond Rattus norvegicus Wistar KWF + FIQ-EDDnp
-
 ?
KWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] + H2O
-
 Homo sapiens KWF + FIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
-
 ?
additional information development of fluorescence resonance energy transfer (FRET) peptides using tryptophan as the fluorophore to study TPP-I hydrolytic properties. Solvent kinetic isotope effects show the importance of the free N-terminus amino group of the substrates, whose absence results in a more complex solvent-dependent enzyme-substrate interaction and catalytic process. To investigate the exopeptidase activity of TPP-I, the randomized sequence MCA-GXXFXXQ-EDDnp is assayed and the products of hydrolysis analyzed by Edman degradation. TTP-I retains its N-terminus tripeptidase character even in randomized sequences and the preferences at the prime sites are similar to those reported for tripeptidyl amino peptidase Rattus norvegicus ?
-
 ?
additional information development of fluorescence resonance energy transfer (FRET) peptides using tryptophan as the fluorophore to study TPP-I hydrolytic properties. Solvent kinetic isotope effects show the importance of the free N-terminus amino group of the substrates, whose absence results in a more complex solvent-dependent enzyme-substrate interaction and catalytic process. To investigate the exopeptidase activity of TPP-I, the randomized sequence MCA-GXXFXXQ-EDDnp is assayed and the products of hydrolysis analyzed by Edman degradation. TTP-I retains its N-terminus tripeptidase character even in randomized sequences and the preferences at the prime sites are similar to those reported for tripeptidyl amino peptidase Rattus norvegicus Wistar ?
-
 ?
RWFFIQ-EDDnp + H2O best substrate, rat spleen and kidney homogenates cleave only at F-F bond Rattus norvegicus RWF + FIQ-EDDnp
-
 ?
RWFFIQ-EDDnp + H2O best substrate, rat spleen and kidney homogenates cleave only at F-F bond Rattus norvegicus Wistar RWF + FIQ-EDDnp
-
 ?
RWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] + H2O FRET substrate Homo sapiens RWF + FIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
-
 ?
RWFVIQ-EDDnp + H2O rat spleen and kidney homogenates cleave only at F-V bond Rattus norvegicus RWF + VIQ-EDDnp
-
 ?
RWFVIQ-EDDnp + H2O rat spleen and kidney homogenates cleave only at F-V bond Rattus norvegicus Wistar RWF + VIQ-EDDnp
-
 ?
RWFVIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] + H2O
-
 Homo sapiens RWF + VIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
-
 ?

Synonyms

Synonyms Comment Organism
ceroid lipofuscinosis 2 protease
-
 Homo sapiens
ceroid lipofuscinosis 2 protease
-
 Rattus norvegicus
CLN2
-
 Homo sapiens
CLN2
-
 Rattus norvegicus
CLN2p
-
 Rattus norvegicus
TPP-I
-
 Homo sapiens
Tpp1
-
 Rattus norvegicus
tripeptidyl peptidase I
-
 Rattus norvegicus
TTP-I
-
 Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5
-
 RWFVIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens
2
-
 KWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens
5.04
-
 RWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5 4 with substrate RWFVIQ-EDDnp Rattus norvegicus
5
-
 with substrate RWFFIQ-EDDnp Rattus norvegicus
5.5
-
 with substrate and KWFFIQ-EDDnp Rattus norvegicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00065
-
 Ac-RWFVIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens

General Information

General Information Comment Organism
additional information tripeptidyl peptidase I (TPP-I), also named ceroid lipofuscinosis 2 protease (CLN2p), is a serine carboxyllysosomal protease involved in neurodegenerative diseases, and has both tripeptidyl amino- and endo-peptidase activities under different pH conditions. The enzyme shows resistance to hydrolysis by cathepsin D Rattus norvegicus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2727
-
 RWFVIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens
2857
-
 KWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens
7200
-
 RWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] pH 4.3, 37°C Homo sapiens