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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

Specific Activity

Specific Activity on EC 3.4.21.107 - peptidase Do

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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.001
-
using PMMGKASPV-4-nitroanilide as substrate, in 50 mM NaH2PO4, pH 8.0, temperature not specified in the publication
0.018
0.032
-
using VFNTLPMMGKASPV-4-nitroanilide as substrate, in 50 mM NaH2PO4, pH 8.0, temperature not specified in the publication
0.473
-
using DPMFKLV-4-nitroanilide as substrate, in 50 mM NaH2PO4, pH 8.0, temperature not specified in the publication
79.3
-
pH 8.0, 37°C
additional information
-
DegP protease exhibits a concentration effect: an 8fold increase in the concentration of DegP results in an 2.4fold increase in the specific protease activity