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

BRENDA support

Literature summary for 4.3.1.1 extracted from

  • Mizuta, K.; Tokushige, M.
    Alteration of enzymatic properties upon trypsin-mediated activation (1976), Biochim. Biophys. Acta, 452, 253-261.
    View publication on PubMed
Search for more literature for 4.3.1.1

Activating Compound

Activating Compound Comment Organism Structure
Trypsin enzyme is activated several-fold by limited treatment Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
48500
-
 4 * 48500, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-aspartate = fumarate + NH3 mechanism Escherichia coli
a

Renatured (Commentary)

Renatured (Comment) Organism
regains its activity and quaternary structure upon dilution Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate r Escherichia coli fumarate + NH3
-
 ?
L-aspartate natural substrate Escherichia coli fumarate + NH3
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 48500, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 trypsin-activated enzyme in the absence of MgCl2 Escherichia coli
7.5
-
 native enzyme in the absence of MgCl2 Escherichia coli
8.8
-
 trypsin-activated enzyme and native enzyme in the presence of MgCl2 Escherichia coli