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Literature summary 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)

EC Number Cloned (Comment) Organism
4.1.1.25
-
 Arabidopsis thaliana
4.1.1.25
-
 Thalictrum flavum subsp. glaucum
4.1.1.25
-
 Petroselinum crispum
4.1.1.28
-
 Catharanthus roseus
4.1.1.28
-
 Papaver somniferum

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.25 F338Y alteration in the primary activity from decarboxylation/deamination to decarboxylation. Mutant displays a very low activity to tyrosine, i.e. about 5% of its activity to phenylalanine, and strong activity to DOPA Arabidopsis thaliana
4.1.1.25 F346Y alteration in the primary activity from decarboxylation-deamination to decarboxylation. Mutant retains a small percentage of decarboxylation-deamination activity Petroselinum crispum
4.1.1.25 additional information generation of a chimeric protein composed of Thalictrum flavum tyrosine decarboxylase residues 1–300 and Petroselinum crispum romatic acetaldehyde synthase residues 300–514. The hybrid enzyme behaves primarily as a wild-type Petroselinum crispum acetaldehyde synthase Thalictrum flavum subsp. glaucum
4.1.1.25 additional information generation of a chimeric protein composed of Thalictrum flavum tyrosine decarboxylase residues 1–300 and Petroselinum crispum romatic acetaldehyde synthase residues 300–514. The hybrid enzyme behaves primarily as a wild-type Petroselinum crispum acetaldehyde synthase Petroselinum crispum
4.1.1.28 Y348F mutation results in conversion of enzyme into an indole-3-acetaldehyde synthase Catharanthus roseus
4.1.1.28 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.25 4.6
-
 L-phenylalanine mutant F338Y, pH 7., 25°C Arabidopsis thaliana
4.1.1.25 5.1
-
 L-phenylalanine wild-type, pH 7., 25°C Arabidopsis thaliana
4.1.1.28 0.095
-
 L-tryptophan mutant Y348F, pH 7., 25°C Catharanthus roseus
4.1.1.28 0.1 2 L-tryptophan wild-type, pH 7., 25°C Catharanthus roseus

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.25 Arabidopsis thaliana Q8RY79
-
-
4.1.1.25 Petroselinum crispum Q06086
-
-
4.1.1.25 Thalictrum flavum subsp. glaucum Q9AXN7
-
-
4.1.1.28 Catharanthus roseus P17770
-
-
4.1.1.28 Papaver somniferum O82415
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.25 L-phenylalanine + H2O
-
 Arabidopsis thaliana phenylethylamine + H2O2 reaction of mutant F338Y ?
4.1.1.25 L-tyrosine + H2O
-
 Petroselinum crispum 4-hydroxyphenylacetaldehyde + CO2 + NH3 enzyme catalyzes decarboxylation and subsequent deamination of substrate ?
4.1.1.28 L-tryptophan
-
 Catharanthus roseus tryptamine + CO2
-
 ?
4.1.1.28 L-tryptophan
-
 Papaver somniferum tryptamine + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.25 TyrDC-2
-
 Petroselinum crispum
4.1.1.28 Tydc9
-
 Papaver somniferum

General Information

EC Number General Information Comment Organism
4.1.1.25 physiological function the phenylalanine residue in the catalytic loop region could serve as a signature residue to reliably distinguish plant arylalkylamine and aldehyde synthesizing aromaic amino acid decarboxylases Petroselinum crispum
4.1.1.28 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
4.1.1.28 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