Literature summary 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.

General Stability

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

Inhibitors

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

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
1.14.16.4	0.0865	-	L-tryptophan	-	Rattus norvegicus

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.14.16.4	55000	-	x * 55000, brain enzyme, SDS-PAGE	Rattus norvegicus
1.14.16.4	260000	-	enzyme from brain, gradient PAGE	Rattus norvegicus

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.16.4	Rattus norvegicus	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.14.16.4	-	Rattus norvegicus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining

Specific Activity [micromol/min/mg]

EC Number	Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
1.14.16.4	0.367	-	brain tryptophan hydroxylase	Rattus norvegicus

Storage Stability

EC Number	Storage Stability	Organism
1.14.16.4	0°C, 20 h, 60% loss of activity	Rattus norvegicus

Substrates and Products (Substrate)

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

Subunits

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

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Release 2023.1 (January 2023)