3.4.14.12: Xaa-Xaa-Pro tripeptidyl-peptidase
This is an abbreviated version!
For detailed information about Xaa-Xaa-Pro tripeptidyl-peptidase, go to the full flat file.
Reaction
Hydrolysis of Xaa-Xaa-Pro-/-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline =
Synonyms
prolyl tripeptidyl aminopeptidase, prolyl tripeptidyl peptidase, prolyltripeptidyl aminopeptidase, PTP, PTP39, PtpA
ECTree
3.4.14.12 Xaa-Xaa-Pro tripeptidyl-peptidaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 3.4.14.12 - Xaa-Xaa-Pro tripeptidyl-peptidase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, with 1.1 M potassium/sodium tartrate, 100 mM Ches buffer (pH 9.0), and 200 mM lithium sulfate
hanging drop vapour diffusion method, with 100 mM Ches (pH 9.0), 1.1 M potassium/sodium tartrate, 200 mM lithium sulfate
the structure of the ligand-free enzyme is solved at 2.1 A resolution, the structure of the S603A mutant-substrate complex is solved at 2.9 A resolution
the structure of the prolyl tripeptidyl aminopeptidase complexed with the inhibitor is determined at 2.2 A resolution, the structure of the mutant E636A at 2.0 A, and in complex with the inhibitor at 1.95 A resolution
