3.4.19.6: pyroglutamyl-peptidase II

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

Reaction

release of the N-terminal pyroglutamyl group from pGlu-/-His-Xaa tripeptides and pGlu-/-His-Xaa-Gly tetrapeptides =

Synonyms

aminopeptidase, thyrotropin-releasing factor pyroglutamate, PAP type II, PPII, pyroglutamate aminopeptidase II, pyroglutamyl aminopeptidase II, pyroglutamyl peptidase II, pyrrolidone carboxypeptidase type II, thyroliberin-hydrolyzing pyroglutamate aminopeptidase, thyroliberinase, thyrotropin-releasing hormone-degrading peptidase, thyrotropin-releasing hormone-degrading pyroglutamate aminopeptidase, TRH aminopeptidase, TRH-DE, TRH-degrading ectoenzyme, TRH-degrading enzyme, TRH-specific aminopeptidase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.19 Omega peptidases

                3.4.19.6 pyroglutamyl-peptidase II

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Results	in table
4	Activating Compound
11	AA Sequence
5	Application
1	CAS Registry Number
2	Cloned(Commentary)
7	General Information
8	General Stability
126	Inhibitors
77	Ki Value [mM]
23	KM Value [mM]
20	Localization
6	Metals/Ions
12	Molecular Weight [Da]
8	Natural Substrates/ Products (Substrates)
37	Organism
4	pH Optimum
2	pH Range
1	pH Stability
4	Posttranslational Modification
13	Protein Variants
8	Purification (Commentary)
1	Reaction
5	Reaction Type
37	Reference
66	Source Tissue
5	Specific Activity [micromol/min/mg]
4	Storage Stability
64	Substrates and Products (Substrate)
7	Subunits
36	Synonyms
3	Temperature Optimum [°C]
2	Temperature Range [°C]
6	Temperature Stability [°C]
2	Turnover Number [1/s]

Cloned

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Cloned on EC 3.4.19.6 - pyroglutamyl-peptidase II

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

detection of a RNA species derived from an alternative processing at the exon 14–intron 14 boundary. The alternatively processed RNA encodes a shorter version of PPII (PPII*), lacking part of the C-terminal domain. PPII* is expressed in COS-7 (or C6 glioma) cells but it does not exhibit any PPII activity. Co-transfection of PPII and increasing amounts of PPII* expression vectors results in a dose-dependent reduction in PPII activity and the formation of covalent PPII–PPII* heterodimers. PPII* is therefore a powerful dominant-negative isoform of PPII, and heterodimerization may be its mechanism of action. Natural expression of shortened versions of M1 aminopeptidases may constitute a new mode of regulation of their activity

Rattus norvegicus

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669931

full-length enzyme, mutant enzymes and truncated enzyme

Rattus norvegicus

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647287