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Information on EC 3.4.21.83 - Oligopeptidase B and Organism(s) Trypanosoma brucei brucei and UniProt Accession O76728

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.83 Oligopeptidase B
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Trypanosoma brucei brucei
UNIPROT: O76728 not found.
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Word Map
The taxonomic range for the selected organisms is: Trypanosoma brucei brucei
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
trypsin-like protease, oligopeptidase b, protease ii, op-tb, la_opb, opbtc, tb-op, tc-op, tc 120, oligopeptidase b2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Protease II
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Proteinase, Escherichia coli alkaline, II
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
57657-67-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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oligopeptidase B null mutant parasites grow at a significantly faster rate in vitro, and are as virulent as wild type strains during infection in mice. Parasites are revealed in extra vascular regions showing that OPB is not involved in assisting Trypanosoma brucei parasites to cross microvascular endothelial cells. Null mutants show an increase in discrete cysteine peptidase activities when compared to wild type strains. A significant increase of prolyl oligopeptidase activity is observed in mutant, but no concomitant increase in prolyl oligopeptidase protein levels
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
O76728_TRYBB
715
0
80681
TrEMBL
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kangethe, R.T.; Boulange, A.F.; Coustou, V.; Baltz, T.; Coetzer, T.H.
Trypanosoma brucei brucei oligopeptidase B null mutants display increased prolyl oligopeptidase-like activity
Mol. Biochem. Parasitol.
182
7-16
2011
Trypanosoma brucei brucei
Manually annotated by BRENDA team
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
PLoS ONE
8
e79349
2013
Trypanosoma brucei brucei (O76728)
Manually annotated by BRENDA team