3.4.19.3: pyroglutamyl-peptidase I

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

Reaction

release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro =

Synonyms

5-oxoprolyl-peptidase, aminopeptidase, pyroglutamate, cysteine-free PCP, EC 3.4.11.8, L-pyrrolidonecarboxylate peptidase, PAP, PAP-I, PAP1, PCP, PCP-0SH, PGAP, PGP I, PGP-1, PGPEP1, PPI, PYR, PYRase, pyroglutamate aminopeptidase, pyroglutamidase, pyroglutamyl aminopeptidase, pyroglutamyl aminopeptidase I, pyroglutamyl peptidase I, pyroglutamyl peptidase type-1, pyroglutamyl type I aminopeptidase, pyroglutamyl-peptidase 1, pyroglutamylaminopeptidase, pyrrolidone carboxyeptidase, pyrrolidone carboxyl peptidase, pyrrolidone carboxypeptidase type I, pyrrolidone-carboxylate peptidase, pyrrolidonecarboxy peptidase, pyrrolidonecarboxylyl peptidase, pyrrolidonyl arylamidase, pyrrolidonyl peptidase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.19 Omega peptidases

                3.4.19.3 pyroglutamyl-peptidase I

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
19	Activating Compound
8134	AA Sequence
30	Application
1	CAS Registry Number
18	Cloned(Commentary)
8	Crystallization (Commentary)
125	Disease/ Diagnostics
9	General Stability
173	Inhibitors
7	Ki Value [mM]
89	KM Value [mM]
17	Localization
8	Metals/Ions
48	Molecular Weight [Da]
20	Natural Substrates/ Products (Substrates)
11	Organic Solvent Stability
127	Organism
1	Pathway
78	PDB ID
25	pH Optimum
7	pH Range
7	pH Stability
30	Protein Variants
23	Purification (Commentary)
1	Reaction
1	Reaction Type
126	Reference
2	Renatured (Commentary)
74	Source Tissue
18	Specific Activity [micromol/min/mg]
13	Storage Stability
198	Substrates and Products (Substrate)
24	Subunits
92	Synonyms
10	Temperature Optimum [°C]
4	Temperature Range [°C]
29	Temperature Stability [°C]
45	Turnover Number [1/s]

Crystallization

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Crystallization on EC 3.4.19.3 - pyroglutamyl-peptidase I

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Crystallization (commentary) Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Bacillus amyloliquefaciens

-

95291

crystallographic analysis of enzyme-inhibitor complex with pyroglutaminal and of the mutant enzyme F142, hanging drop vapour diffusion method

Bacillus amyloliquefaciens

-

652124

crystal structure of wild-type and mutant enzyme C142S/C188S determined at 2.2 and 2.7 A resolution

Pyrococcus furiosus

-

651784

PCP-0SH polar mutants C142S/C188S/E192D andC142S/C188S/E192Q crystallize at a 6.5% PEG4000, while the apolar mutants C142S/C188S/E192A, C142S/C188S/E192I and C142S/C188S/E192V crystallize at a 5.7-6.0% PEG4000. The protein molecules crystallize in two different space groups. E192Q and E192V form isomorphic monoclinic crystals in the space group P2(1), which agree with those of the wild-type PCP and cysteine-free PCP-0SH (C142S/C188S), while E192A, E192D, and E192I form orthorhombic crystals in the space group P2(1)2(1)2(1). In both crystal systems, four subunit (monomer) molecules are contained in the asymmetric unit. A systematic analysis of individual structures indicates that the mutation does not have any significant effect on the overall structure

Pyrococcus furiosus

O73944

667733

hanging drop vapor diffusion method at 4°C, 1.6 A resolution

Pyrococcus horikoshii

O58321

723069

-

Thermococcus litoralis

-

95304, 95316

crystallized from both ammonium phosphate and ammonium sulfate, structure determined at 1.7 A resolution

Thermococcus litoralis

-

653129