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

BRENDA support

Literature summary for 4.1.1.53 extracted from

  • Jebai, F.; Hanoun, N.; Hamon, M.; Thibault, J.; Peltre, G.; Gros, F.; Krieger, M.
    Expression, purification, and characterization of rat aromatic L-amino acid decarboxylase in Escherichia coli (1997), Protein Expr. Purif., 11, 185-194.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.14
-
L-dihydroxyphenylalanine cloned enzyme Rattus norvegicus
0.066
-
5-hydroxytryptamine cloned enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
rat
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1500
-
-
Rattus norvegicus
8444
-
L-dihydroxyphenylalanine, cloned enzyme Rattus norvegicus
1813
-
5-hydroxytryptamine, cloned enzyme Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-Hydroxytryptophan
-
Rattus norvegicus Serotonin + CO2
-
?
3,4-Dihydroxyphenylalanine
-
Rattus norvegicus Dopamine + CO2
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
enzyme assay at Rattus norvegicus