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Literature summary for 3.4.21.108 extracted from

  • Glaza, P.; Osipiuk, J.; Wenta, T.; Zurawa-Janicka, D.; Jarzab, M.; Lesner, A.; Banecki, B.; Skorko-Glonek, J.; Joachimiak, A.; Lipinska, B.
    Structural and functional analysis of human HtrA3 protease and its subdomains (2015), PLoS ONE, 10, e0131142 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the HtrA3 protease domain together with the PDZ domain. The protein forms a trimer Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information a variant lacking the N-terminal domain forms stable trimers while both the catalytic domain alone and the short natural isoform are monomeric. The protease domain with the PDZ domain removed and an N-terminally truncated short natural isoform are fully active at a wide range of temperatures and their substrate affinity is not impaired Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00074
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) short natural isoform lacking the N-terminal domain, pH 7.5, temperature not specified in the publication Homo sapiens
0.00088
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) protease domain, pH 7.5, temperature not specified in the publication Homo sapiens
0.00096
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) variant lacking the N-terminal domain, pH 7.5, temperature not specified in the publication Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P83110 isoform Htra3
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
More the presence of the PDZ domain influences HtrA3 trimer formation. The C-terminal sequence of HtrA3 appears to have little effect on activity and oligomerization Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.029
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) protease domain, pH 7.5, temperature not specified in the publication Homo sapiens
0.029
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) variant lacking the N-terminal domain, pH 7.5, temperature not specified in the publication Homo sapiens
0.03
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) short natural isoform lacking the N-terminal domain, pH 7.5, temperature not specified in the publication Homo sapiens

General Information

General Information Comment Organism
physiological function the PDZ domain is dispensable for HtrA3 activity Homo sapiens

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
30.27
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) variant lacking the N-terminal domain, pH 7.5, temperature not specified in the publication Homo sapiens
33.03
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) protease domain, pH 7.5, temperature not specified in the publication Homo sapiens
40.5
-
Ala(7-methoxycoumarin-4-acetic acid)-IRRVSYSF-(5-amido-2-nitrobenzamide) short natural isoform lacking the N-terminal domain, pH 7.5, temperature not specified in the publication Homo sapiens