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

BRENDA support

Literature summary for 1.14.16.4 extracted from

  • Cash, C.D.; Vayer, P.; Mandel, P.; Maitre, M.
    Tryptophan 5-hydroxylase. Rapid purification from whole rat brain and production of a specific antiserum (1985), Eur. J. Biochem., 149, 239-245.
    View publication on PubMed

General Stability

General Stability Organism
catalase is necessary to protect the enzyme during purification Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
desferrioxamine 0.010 mM or higher, irreversible loss of activity Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0865
-
L-tryptophan
-
Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
x * 55000, brain enzyme, SDS-PAGE Rattus norvegicus
260000
-
enzyme from brain, gradient PAGE Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.367
-
brain tryptophan hydroxylase Rattus norvegicus

Storage Stability

Storage Stability Organism
0°C, 20 h, 60% loss of activity Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + tetrahydropteridine + O2
-
Rattus norvegicus 5-hydroxy-L-tryptophan + dihydropteridine + H2O
-
?

Subunits

Subunits Comment Organism
? x * 55000, brain enzyme, SDS-PAGE Rattus norvegicus