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Literature summary for 4.1.1.28 extracted from

  • Torrens-Spence, M.P.; Liu, P.; Ding, H.; Harich, K.; Gillaspy, G.; Li, J.
    Biochemical evaluation of the decarboxylation and decarboxylation-deamination activities of plant aromatic amino acid decarboxylases (2013), J. Biol. Chem., 288, 2376-2387.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Catharanthus roseus
-
Papaver somniferum

Protein Variants

Protein Variants Comment Organism
Y348F mutation results in conversion of enzyme into an indole-3-acetaldehyde synthase Catharanthus roseus
Y348F mutation results in conversion of enzyme into an indole-3-acetaldehyde synthase, mutant retains a small percentage of its original decarboxylation activity Papaver somniferum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.095
-
L-tryptophan mutant Y348F, pH 7., 25°C Catharanthus roseus
0.1 2 L-tryptophan wild-type, pH 7., 25°C Catharanthus roseus

Organism

Organism UniProt Comment Textmining
Catharanthus roseus P17770
-
-
Papaver somniferum O82415
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan
-
Catharanthus roseus tryptamine + CO2
-
?
L-tryptophan
-
Papaver somniferum tryptamine + CO2
-
?

Synonyms

Synonyms Comment Organism
Tydc9
-
Papaver somniferum

General Information

General Information Comment Organism
physiological function the tyrosine or phenylalanine residue in the catalytic loop region could serve as a signature residue to reliably distinguish plant arylalkylamine and aldehyde synthesizing aromatic amino acid decarboxylases Catharanthus roseus
physiological function the tyrosine or phenylalanine residue in the catalytic loop region could serve as a signature residue to reliably distinguish plant arylalkylamine and aldehyde synthesizing aromatic amino acid decarboxylases Papaver somniferum