Literature summary for 3.4.21.83 extracted from

Canning, P.; Rea, D.; Morty, R.E.; Fueloep, V.
Crystal structures of Trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymes (2013), PLoS ONE, 8, e79349.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Trypanosoma brucei brucei

Crystallization (Commentary)

Crystallization (Comment)	Organism
ligand-free open state and inhibitor-bound closed state crystal structures, to 2.4 and 2.85 A resolution, respectively. Peptides over 30 residues cannot fit the enzyme cavity, preventing the complete domain closure required for a key propeller Asp/Glu to fix the catalytic His and Arg in the catalytically competent conformation. This size exclusion mechanism protects larger peptides and proteins from degradation	Trypanosoma brucei brucei

Crystallization (Comment)

Organism

ligand-free open state and inhibitor-bound closed state crystal structures, to 2.4 and 2.85 A resolution, respectively. Peptides over 30 residues cannot fit the enzyme cavity, preventing the complete domain closure required for a key propeller Asp/Glu to fix the catalytic His and Arg in the catalytically competent conformation. This size exclusion mechanism protects larger peptides and proteins from degradation

Trypanosoma brucei brucei

Organism

Organism	UniProt	Comment	Textmining
Trypanosoma brucei brucei	O76728	-	-

Synonyms

Synonyms	Comment	Organism
OPB	-	Trypanosoma brucei brucei

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Release 2023.1 (January 2023)