Literature summary extracted from

Bouchard, S.; Roberge, A.G.
Biochemical properties and kinetic parameters of dihydroxyphenylalanine-5-hydroxytryptophan decarboxylase in brain, liver, and adrenals of cat (1979), Can. J. Biochem., 57, 1014-1018.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
4.1.1.28	additional information	-	additional information	-	Felis catus

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.1.1.28	Felis catus	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
4.1.1.28	adrenal gland	-	Felis catus	-
4.1.1.28	brain	-	Felis catus	-
4.1.1.28	liver	-	Felis catus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.1.1.28	3,4-Dihydroxyphenylalanine	-	Felis catus	3-Hydroxytyramine + CO2	-	?
4.1.1.28	5-Hydroxytryptophan	-	Felis catus	Serotonin + CO2	-	?

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.1.1.28	7.5	8.5	broad, brain enzyme	Felis catus
4.1.1.28	8	-	liver enzyme	Felis catus
4.1.1.28	8	8.5	adrenal enzyme	Felis catus

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
4.1.1.28	pyridoxal 5'-phosphate	5-hydroxytryptophan can be decarboxylated without exogenous addition of pyridoxal 5'-phosphate, addition of pyridoxal 5'-phosphate substantially increases enzyme activity. Excess of coenzyme, above 0.06 mM, induces inhibition in adrenals and liver but not in the central nervous system	Felis catus

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Release 2023.1 (January 2023)