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Literature summary extracted from

  • Wagh, A.R.; Bose, K.
    Structural basis of inactivation of human counterpart of mouse motor neuron degeneration 2 mutant in serine protease HtrA2 (2018), Biosci. Rep., 38, BSR20181072 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.108 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.21.108 comparison of wild-type and mutan S276C. In wild-type, water molecule number 377 forms an interaction between side chains of S276 and I270* of the adjacent molecule. In mutant S276C, this water molecule is absent Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.108 R280A inactive Homo sapiens
3.4.21.108 R280A/S276C inactive Homo sapiens
3.4.21.108 S276C inactive. Mutation does not affect the oligomeric properties and maintains proper hydrogen bonding distances in the active-site triad residues Homo sapiens

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.108 beta-casein + H2O
-
 Homo sapiens ?
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.21.108 74
-
 melting temperature, mutant S276C Homo sapiens