3.4.14.10: tripeptidyl-peptidase II

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For detailed information about tripeptidyl-peptidase II, go to the full flat file.

Reaction

Release of an N-terminal tripeptide from a polypeptide =

Synonyms

aminopeptidase, tripeptidyl, II, cholecystokinin-inactivating peptidase, dTPP II, EC 3.4.14.8, hTPP II, mTPP II, PTP-A, TPII, TPP, TPP II, TPP-2, TPP-II, TPP2, TPPII, tripeptidyl aminopeptidase, tripeptidyl aminopeptidase I, tripeptidyl aminopeptidase I I, tripeptidyl aminopeptidase II, tripeptidyl peptidase, tripeptidyl peptidase II, tripeptidyl-peptidase-II, tripeptidylpeptidase II, TY-21 TPP

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases

                3.4.14.10 tripeptidyl-peptidase II

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Results	in table
5	Activating Compound
2690	AA Sequence
3	Application
1	CAS Registry Number
17	Cloned(Commentary)
1	Crystallization (Commentary)
47	Disease/ Diagnostics
2	Expression
13	General Information
4	General Stability
6	IC50 Value
144	Inhibitors
111	kcat/KM [mM/s]
68	Ki Value [mM]
122	KM Value [mM]
32	Localization
15	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
86	Organism
1	PDB ID
15	pH Optimum
9	pH Range
1	pH Stability
19	Protein Variants
15	Purification (Commentary)
1	Reaction
1	Reaction Type
77	Reference
95	Source Tissue
7	Specific Activity [micromol/min/mg]
6	Storage Stability
102	Substrates and Products (Substrate)
22	Subunits
70	Synonyms
5	Temperature Optimum [°C]
1	Temperature Stability [°C]
111	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.14.10 - tripeptidyl-peptidase II

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

cryoelectron microscopy and single-particle analysis show that the complex is built from two strands forming a quasihelical structure harboring a complex system of inner cavities. The dimensions of the TPP2 spindle are 55 x 28 nm and the strands are built of nine stacked dimers. The interior of each strand is permeated by a cavity system that features a suite of chambers at each dimer-dimer interface

Homo sapiens

P29144

732922