Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.107 extracted from

  • Huston, W.M.; Swedberg, J.E.; Harris, J.M.; Walsh, T.P.; Mathews, S.A.; Timms, P.
    The temperature activated HtrA protease from pathogen Chlamydia trachomatis acts as both a chaperone and protease at 37°C (2007), FEBS Lett., 581, 3382-3386.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
DTT only when incubated in the presence of 20 mM dithiothreitol, which reduces the structural disulfide bonds and unfold the protein, and above 34°C, is CtHtrA able to proteolyse alpha-lactalbumin Chlamydia trachomatis

Cloned(Commentary)

Cloned (Comment) Organism
gene htrA, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) using a vector containing pelB secretion signal sequence Chlamydia trachomatis

Protein Variants

Protein Variants Comment Organism
S247A proteolytically inactive mutant Chlamydia trachomatis

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Chlamydia trachomatis
additional information no inhibition by aprotinin and trypsin inhibitor Chlamydia trachomatis
PMSF
-
Chlamydia trachomatis

Metals/Ions

Metals/Ions Comment Organism Structure
MgCl2 activates at 20 mM Chlamydia trachomatis
MgSO4 activates at 20 mM Chlamydia trachomatis
NaCl activates at 20 mM Chlamydia trachomatis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
6 * 50000, SDS-PAGE Chlamydia trachomatis
307000
-
recombinant enzyme, gel filtration Chlamydia trachomatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
insulin beta-chain + H2O Chlamydia trachomatis
-
?
-
?

Organism

Organism UniProt Comment Textmining
Chlamydia trachomatis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-lactalbumin + H2O only when incubated in the presence of 20 mM dithiothreitol, which reduces the structural disulfide bonds and unfold the protein, and above 34°C, is CtHtrA able to proteolyse alpha-lactalbumin Chlamydia trachomatis ?
-
?
beta-casein + H2O the cleavage activity at 37°C is ATP independent, not significantly influenced by buffer composition, active over a broad range of pH, and with a broad optimum at pH 6.5, and 20 mM salts, e.g. magnesium sulfate, magnesium chloride, or sodium chloride, improving activity, determination of cleavage sites Chlamydia trachomatis beta-casein peptide fragments
-
?
insulin beta-chain + H2O
-
Chlamydia trachomatis ?
-
?
additional information HtrA sequence specificity, overview, no activity with albumin and myoglobin at 37°C, HtrA acts as both a chaperone and protease, HtrA mutant S247A is able to chaperone insulin B-chain, irrespective of temperature, but at 30°C only HtrA and not mutant S247A displays significant chaperone activity for alpha-lactalbumin, overview Chlamydia trachomatis ?
-
?

Subunits

Subunits Comment Organism
hexamer 6 * 50000, SDS-PAGE Chlamydia trachomatis
More secondary structures for activated protease at different temperatures Chlamydia trachomatis

Synonyms

Synonyms Comment Organism
HtrA protease
-
Chlamydia trachomatis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at, chaperone and protease activities Chlamydia trachomatis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
34 55 low activity below 34°C, rapid loss of activity at 55°C Chlamydia trachomatis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
broad optimum Chlamydia trachomatis

pH Range

pH Minimum pH Maximum Comment Organism
6 10
-
Chlamydia trachomatis

Cofactor

Cofactor Comment Organism Structure
additional information ATP is not required Chlamydia trachomatis