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4.1.1.28: aromatic-L-amino-acid decarboxylase

This is an abbreviated version!
For detailed information about aromatic-L-amino-acid decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.28

Reaction

5-hydroxy-L-tryptophan
=
5-hydroxytryptamine
 +
CO2

Synonyms

3,4-dihydroxyphenylalanine carboxylase, 3,4-Dihydroxyphenylalanine decarboxylase, 5-Hydroxy-L-tryptophan decarboxylase, 5-Hydroxytryptophan decarboxylase, 5-hydroxytryptophan hydroxylase, 5HTP decarboxylase, AAAC, AAAD, AACD, AADC, AADC1A, AADC1B, AADC393, AADC438, AADC486, Alt-DDC, aromatic acid acid decarboxylase, Aromatic amino acid decarboxylase, aromatic amino acid decarboxylase 1A, aromatic amino acid decarboxylase 1B, Aromatic L-amino acid decarboxylase, aromatic L-aminoacid decarboxylase, aromatic-L-amino-acid decarboxylase, CrTDC, DDC, Decarboxylase, aromatic amino acid, Di-ADC, Dihydroxyphenylalanine-5-hydroxytryptophan decarboxylase, DOPA DC, dopa decarboxilase, DOPA decarboxylase, DOPA-5-hydroxytryptophan decarboxylase, DOPA/5HTP decarboxylase, dopamine decarboxylase, EC 4.1.1.26, EC 4.1.1.27, HsDDC, Hydroxytryptophan decarboxylase, L-3,4-Dihydroxyphenylalanine decarboxylase, L-5-Hydroxytryptophan decarboxylase, L-amino acid decarboxylase, L-amino-acid decarboxylase, L-Aromatic amino acid decarboxylase, L-aromatic aminoacid decarboxylase, L-DOPA decarboxylase, L-Tryptophan decarboxylase, neural-type DDC, non-neural DDC, PP_2552, TDC, TDC2, Tenebrio Dopa decarboxylase, Trp decarboxylase, Tryptophan decarboxylase, tryptophan decarboxylase-1, tryptophan decarboxylase-2, TYDC, Tydc9, Tyrosine/Dopa decarboxylase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.28 aromatic-L-amino-acid decarboxylase

Engineering

Engineering on EC 4.1.1.28 - aromatic-L-amino-acid decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y348F
mutation results in conversion of enzyme into an indole-3-acetaldehyde synthase
A275T
naturally occuring mutation involved in aromatic-L-amino-acid decarboxylase deficiency
A91V
naturally occuring mutation involved in aromatic-L-amino-acid decarboxylase deficiency
E227A/R228A/D229A/K230A
-
replacement of amino acids 227-230 (ERDK) with alanine residues reduces reactivity to 13.6% compared to the wild type enzyme
E608D
-
c.1824A>C, naturally occuring mutation in enzyme DDC
F309L
naturally occuring mutation, involved in aromatic-L-amino-acid decarboxylase deficiency
G102S
naturally occuring mutation, involved in aromatic-L-amino-acid decarboxylase deficiency
G143D
-
c.428G>A, naturally occuring mutation in enzyme DDC
H632Q
-
c.1896C>A, naturally occuring mutation in enzyme DDC
I170L
-
c.508A>C, naturally occuring mutation in enzyme DDC
K303A
-
the mutant binds pyridoxal 5'-phosphate with a 100fold decreased apparent equilibrium binding affinity with respect to the wild type enzyme. Unlike the wild-type, K303A in the presence of L-Dopa displays a parallel progress course of formation of both dopamine and 3,4-dihydroxyphenylacetaldehyde (plus ammonia) with a burst followed by a linear phase
R347Q
naturally occuring mutation involved in aromatic-L-amino-acid decarboxylase deficiency
S143N
-
c.428G>A, naturally occuring mutation in enzyme DDC
S147R
naturally occuring mutation, involved in aromatic-L-amino-acid decarboxylase deficiency
S250F
T58M
-
c.173C>T, naturally occuring mutation in enzyme DDC
V614A
Y348F
mutation results in conversion of enzyme into an indole-3-acetaldehyde synthase, mutant retains a small percentage of its original decarboxylation activity
Y350F
the mutant enzyme activities demonstrate a conversion of activity from decarboxylation to decarboxylation-deamination
A53T
-
shows minimal dopamine synthesis
T246A
T246 act as an essential general base for the oxidative deamination reaction
Y332F
additional information
-
Model chemistry by second-order Moller-Plessett perturbation theory calculations, phenylalanine in position 103 is replaced by all native amino acids. The mutant residues which conserve an aromatic side chain (tyrosine and tryptophan) retain near 100% interaction energy with the carbidopa, and thus most likely retain full protein function. Arginine has an interaction energy of 555% of the wild-type. This is due to the fact that the long, polar side chain is able to find a geometry where a hydrogen bond is being made with the hydroxyl group of the carbidopa. The small side chains are not close enough to the carbidopa to have a large deal of dispersion/induction interactions. Residues are arranged by the size of the side chain, and with a few exception, the interaction energy generally increases with size of the side chain. Glycine, alanine, serine, threonine, and histidine all fall below the above mentioned 20% threshold and would likely cause a loss of protein function. Serine contains a polar side chain and histidine has pi-electrons, yet these residues are too small and too far removed to have strong interactions.