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3.4.14.10: tripeptidyl-peptidase II

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

Word Map on EC 3.4.14.10

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

General Stability

General Stability on EC 3.4.14.10 - tripeptidyl-peptidase II

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 2 mM Tris-HCl dissociation buffer, 0.5 mM 2-mercaptoethanol, 3% w/v glycerol, pH 8, gradually decreases activity, 30% glycerol stabilizes
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dithiothreitol and glycerol stabilize
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purified enzyme undergos a spontaneous dissociation upon storage, the dissociated enzyme has a specific activity which is 1/10th of that of the normal high MW complex
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spindle formation (at TPP II concentrations above 0.03 mg/ml) by strand paring causes both significant thermodynamic and kinetic stabilization
Drosophila sp. (in: flies)
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