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Literature summary for 3.4.21.26 extracted from

  • Juhasz, T.; Szeltner, Z.; Fueloep, V.; Polgar, L.
    Unclosed beta-propellers display stable structures: implications for substrate access to the active site of prolyl oligopeptidase (2005), J. Mol. Biol., 346, 907-917.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information expression of beta-propeller domain of enzyme as a stable, soluble protein with seven blades. Propeller domain is more stable than parent prolyl oligopeptidase. Deletion of the seventh blade of the propeller leads to a stable six-bladed propeller that dimerizes in contrast to the monomeric seven-bladed propeller Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa P23687
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-

Source Tissue

Source Tissue Comment Organism Textmining
brain
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Sus scrofa
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