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

BRENDA support

Literature summary for 3.4.23.5 extracted from

  • Suzuki, H.; Takeda, M.; Nishimura, T.
    Enzymatic characterization of cathepsin D in rabbit brains with experimental neurofibrillary changes (1994), Biochem. Mol. Biol. Int., 32, 1033-1039.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0263
-
hemoglobin control animals Oryctolagus cuniculus
0.0293
-
hemoglobin enzyme from animals with experimental neurofibrillary changes Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
wild type enzyme and enzyme from rabbit brains with experimental neurofibrillary changes
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Hemoglobin + H2O
-
Oryctolagus cuniculus ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
46
-
heat inactivation proceeds linearly with time for the control enzyme but biphasically for the enzyme from animals with experimental neurofibrillary changes Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1
-
bovine hemoglobin Oryctolagus cuniculus