3.4.14.9: tripeptidyl-peptidase I

This is an abbreviated version!
For detailed information about tripeptidyl-peptidase I, go to the full flat file.

Reaction

Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity =

Synonyms

aminopeptidase, tripeptidyl, I, AO090166000084, ceroid lipofuscinosis 2 protease, CLN2, CLN2 protein, CLN2p, EC 3.4.14.8, LPIC, lysosomal pepstatin insensitive protease, N-terminal tripeptidyl exopeptidase, SedB, SedC, SedD, sedolisin B, sedolisin C, sedolisin D, TPP I, TPP-I, Tpp1, TPP1F, TPPI, tripeptidyl aminopeptidase, tripeptidyl aminopeptidase I, tripeptidyl exopeptidase, tripeptidyl peptidase, tripeptidyl peptidase 1, tripeptidyl peptidase I, tripeptidyl peptidase-I, tripeptidyl-peptidase 1, tripeptidyl-peptidase I, TTP-I, v4-7

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases

                3.4.14.9 tripeptidyl-peptidase I

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Results	in table
3	Activating Compound
1114	AA Sequence
7	Application
1	CAS Registry Number
19	Cloned(Commentary)
2	Crystallization (Commentary)
363	Disease/ Diagnostics
17	General Information
3	General Stability
5	IC50 Value
67	Inhibitors
3	kcat/KM [mM/s]
8	Ki Value [mM]
32	KM Value [mM]
35	Localization
5	Metals/Ions
25	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
60	Organism
3	PDB ID
23	pH Optimum
10	pH Range
9	pH Stability
3	pI Value
17	Posttranslational Modification
64	Protein Variants
14	Purification (Commentary)
3	Reaction
1	Reaction Type
60	Reference
93	Source Tissue
5	Specific Activity [micromol/min/mg]
2	Storage Stability
123	Substrates and Products (Substrate)
11	Subunits
100	Synonyms
5	Temperature Optimum [°C]
1	Temperature Stability [°C]
32	Turnover Number [1/s]

pH Stability

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pH Stability on EC 3.4.14.9 - tripeptidyl-peptidase I

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

2 - 5

Homo sapiens

-

optimal activation occurs in the range pH 3.0-4.0, the proteolytic processing takes place in a wider pH range (2.0-5.0), at pH 3.0 and lower, TPP I is quickly inactivated, whereas the polypeptide generated at higher pH (4.5-5.0) possesses 6- and 13-aa N-terminal extensions and is inactive, the enzyme is unstable at alkaline and neutral pH

678513

2.5 - 5

Homo sapiens

-

stable

665428

3

Homo sapiens

-

has weak endoproteolytic activity at pH 3

678398

3 - 6

Rattus norvegicus

-

at pH 3.0 the activity of TPP I is less than 75% of its maximal activity at pH 4.5, most stable at pH 3-4, no activity at pH above 6.0

679200

3.5

Homo sapiens

-

TPP I is an acidic protease that is quickly inactivated under alkaline pH conditions, in the absence of prosegment, the enzyme is quickly denatured with a rate constant of around 0.107/min, amounting to a half-life of 6.472 min, whereas in the presence of the prosegment, the inactivation rate is reduced to about 0.035/min, and approximately 84% of the activity is preserved after over 2 h of incubation

698756

3.5 - 4.5

Rattus norvegicus

-

stable

647183

5 - 6

Rattus norvegicus

-

48 h, stable

647186

7

Rattus norvegicus

-

48 h, unstable above

647186

7.4

Homo sapiens

-

37°C, half-life: of mature enzyme in absence of heparin is 2.5 min, of mature enzyme in presence of heparin is 21.5 min

665697