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3.4.21.107: peptidase Do

This is an abbreviated version!
For detailed information about peptidase Do, go to the full flat file.

Word Map on EC 3.4.21.107

Reaction

acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-/-Val =

Synonyms

bacterial PQC factor, BB_0104, BCAL2829, CD630_32840, Deg1, DEG2, DEG5, DEG7, DEG8, Deg9, DegP, DegP protease, DegP/HtrA, DegQ, DegS, DepP9, Do, Do protease, HhoA, HhoB, high temperature requirement A, high temperature requirement A protease, high temperature requirement A1, high temperature requirement factor A, high-temperature requirement A, high-temperature requirement A protease, high-temperature requirement A-1, high-temperature requirement A1, high-temperature requirement A1 protease, high-temperature requirement factor A, HtrA, HtrA (DegP) protease, HtrA heat shock protease, HtrA protease, HTRA serine peptidase 1, HtrA-like protease, HtrA/DegP, HtrA1, HtrA2, HtrA3, HTRA4, MAL8P1.126, More, MucD, Nma111p, Omi/HtrA protease orthologue Ynm3p, protease do, protease Do-like 5, protease Do-like 8, PRSS11, S01.273, serine protease, serine protease HtrA, serine protease HtrA1, YNL123w

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.107 peptidase Do

Temperature Range

Temperature Range on EC 3.4.21.107 - peptidase Do

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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 30
-
almost no activity below 20°C, activity rapidly increases above 30°C
20 - 85
-
at least 50% of maximum activity
30 - 42
-
enzyme activity is constant within this temperature range
34 - 55
-
low activity below 34°C, rapid loss of activity at 55°C
37 - 44
-
the HtrA mutant forms colonies with the same frequency as the wild type at 37°C and 42°C, the ability of the mutant to form colonies at 44°C was greatly reduced as compared to the wild type
37 - 45
37 - 55
-
activity rapidly increases with temperature
44
-
at 44 °C function of DegP in mutant strain CLC198 can be complemented by HtrA2