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Literature summary extracted from

  • Jarzab, M.; Wenta, T.; Zurawa-Janicka, D.; Polit, A.; Gieldon, A.J.; Wysocka, M.; Glaza, P.; Skorko-Glonek, J.; Ciarkowski, J.; Lesner, A.; Lipinska, B.
    Intra- and intersubunit changes accompanying thermal activation of the HtrA2(Omi) protease homotrimer (2016), Biochim. Biophys. Acta, 1864, 283-296.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.108 E425L variant has an increased activity, especially at lower temperatures (25-30°C) and the highest affinity for the substrate and catalytic efficiency among all studied variants Homo sapiens
3.4.21.108 I373N mutant shows a significant loss of cooperativity Homo sapiens
3.4.21.108 additional information a PDZ domain deletion mutant at 37°C shows 2.0fold higher cleavage activity assayed with beta-casein than wild-type Homo sapiens
3.4.21.108 R337L mutant has an increased activity at all temperatures tested, higher affinity for the substrate and a higher turnover rate Homo sapiens
3.4.21.108 R432L variant has an increased activity with beta-casein and the peptide Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitro benzoic acid) at various temperatures Homo sapiens
3.4.21.108 V226K variant has an increased activity with beta-casein and the peptide Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitro benzoic acid) at various temperatures Homo sapiens
3.4.21.108 V431D variant has a decreased activity, especially with beta-casein Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.21.108 mitochondrion
-
 Homo sapiens 5739
-

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.108 Homo sapiens O43464
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.108 Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) + H2O
-
 Homo sapiens ?
-
 ?
3.4.21.108 beta-casein + H2O
-
 Homo sapiens ?
-
 ?

General Information

EC Number General Information Comment Organism
3.4.21.108 physiological function during thermal activation, the PDZ domain changes its position versus the protease domain inside a subunit, including a prominent change affecting the L3 regulatory loop of the protease domain, and also changes its interactions with the protease domain of the adjacent subunit, specifically with its L1* regulatory loop containing the active site serine. The alpha5 helix of PDZ is involved in both, the intra- and intersubunit changes of interactions and seems to play an important role in HtrA2 activation Homo sapiens