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Literature summary for 4.1.1.28 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.
    View publication on PubMed

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Felis catus
-
-
-

Source Tissue

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

Substrates and Products (Substrate)

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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