Literature summary for 1.13.12.15 extracted from

Bertoldi, M.; Cellini, B.; Montioli, R.; Borri Voltattorni, C.
Insights into the mechanism of oxidative deamination catalyzed by DOPA decarboxylase (2008), Biochemistry, 47, 7187-7195.

Search for more literature for 1.13.12.15

Cloned(Commentary)

Cloned (Comment)	Organism
cloning and expression of wild-type 3,4-dihydroxyphenylalanine oxidative deaminase and Y332F and T246A mutants in SVS370 Escherichia coli cells.	Sus scrofa

Protein Variants

Protein Variants	Comment	Organism
T246A	T246 act as an essential general base for the oxidative deamination reaction	Sus scrofa
Y332F	wild-type enzyme and Y332F variant are able to perform the oxidation toward aromatic amines or aromatic L-amino acids, without the aid of any cofactor related to oxygen chemistry.	Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
3-(3,4-dihydroxyphenyl)-2-hydrazino-2-methyl propionic acid	carbiDOPA, addition of 10 microM inhibitor to reaction mixtures (Y332F mutant with L-dopa) in the presence or in the absence of catalase or superoxide dismutase, immediately stops the O2 consumption.	Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
aromatic amine + 1/2 O2	Sus scrofa	oxidative deamination, unusual oxygen-consuming reaction catalyzed by the enzyme toward aromatic amines (serotonin, dopamine, and alpha-methyldopamine) and D-tryptophan methyl ester	aromatic aldehyde + NH3 + H2O	production in equivalent amounts depending on the nature of the substrate, and ammonia with concomitant O2 consumption in a 1:2 molar ratio with respect to the products. A ketimine accumulates during the linear phase of product formation. This species is reactive since it is converted back to pyridoxal 5'-phosphate when the substrate is consumed. Superoxide anion and hydrogen peroxide are both generated during the catalytic cycles.	?
D-tryptophan methyl ester + 1/2 O2	Sus scrofa	production depending on the nature of the substrate, and ammonia with concomitant O2 consumption in a 1:2 molar ratio with respect to the products	methyl 3-(1H-indol-3yl)-2-oxopropanoate + NH3	-	?
L-DOPA + O2	Sus scrofa	-	?	-	?
additional information	Sus scrofa	The novelty in DDC is the possibility of catalyzing a reaction involving dioxygen although the enzyme lacks of any cofactor or metal related to O2 chemistry. The external aldimine intermediate undergoes a decarboxylation or a deprotonation leading to a quinonoid species, that is protonated at C4 producing the ketimine intermediate. Although it cannot be ruled out that this intermediate could be attacked by dioxygen, it seems much more likely, regarding enzymes proceeding through a carbanion chemistry on DDC, that the more electron dense quinonoid intermediate, in equilibrium with the ketimine, is reactive toward O2. Aerobiosis shifts the quinonoid-ketimine equilibrium toward quinonoid, while anaerobiosis shifts the equilibrium toward ketimine. The reaction between dioxygen and the quinonoid give rise directly to a superoxide anion and semiquinone. Superoxide is deprotonated and its anionic form is thus able to couple with the semiquinone giving rise to a peroxide species that is further protonated, and thus forming a hydroperoxy-pyridoxal 5'-phosphate intermediate. This rearranges to produce aldehyde, ammonia and hydrogen peroxide.	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Sus scrofa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
aromatic amine + 1/2 O2	oxidative deamination, unusual oxygen-consuming reaction catalyzed by the enzyme toward aromatic amines (serotonin, dopamine, and alpha-methyldopamine) and D-tryptophan methyl ester	Sus scrofa	aromatic aldehyde + NH3 + H2O	production in equivalent amounts depending on the nature of the substrate, and ammonia with concomitant O2 consumption in a 1:2 molar ratio with respect to the products. A ketimine accumulates during the linear phase of product formation. This species is reactive since it is converted back to pyridoxal 5'-phosphate when the substrate is consumed. Superoxide anion and hydrogen peroxide are both generated during the catalytic cycles.	?
D-tryptophan methyl ester + 1/2 O2	production depending on the nature of the substrate, and ammonia with concomitant O2 consumption in a 1:2 molar ratio with respect to the products	Sus scrofa	methyl 3-(1H-indol-3yl)-2-oxopropanoate + NH3	-	?
L-DOPA + O2	-	Sus scrofa	?	-	?
additional information	The novelty in DDC is the possibility of catalyzing a reaction involving dioxygen although the enzyme lacks of any cofactor or metal related to O2 chemistry. The external aldimine intermediate undergoes a decarboxylation or a deprotonation leading to a quinonoid species, that is protonated at C4 producing the ketimine intermediate. Although it cannot be ruled out that this intermediate could be attacked by dioxygen, it seems much more likely, regarding enzymes proceeding through a carbanion chemistry on DDC, that the more electron dense quinonoid intermediate, in equilibrium with the ketimine, is reactive toward O2. Aerobiosis shifts the quinonoid-ketimine equilibrium toward quinonoid, while anaerobiosis shifts the equilibrium toward ketimine. The reaction between dioxygen and the quinonoid give rise directly to a superoxide anion and semiquinone. Superoxide is deprotonated and its anionic form is thus able to couple with the semiquinone giving rise to a peroxide species that is further protonated, and thus forming a hydroperoxy-pyridoxal 5'-phosphate intermediate. This rearranges to produce aldehyde, ammonia and hydrogen peroxide.	Sus scrofa	?	-	?

Synonyms

Synonyms	Comment	Organism
3,4-dihydroxyphenylalanine oxidative deaminase	-	Sus scrofa
DDC	-	Sus scrofa
DOPA decarboxylase	-	Sus scrofa

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	mutant T246A presents a decarboxylase activity, the kcat value is decreased by 29fold with respect to wild-type, an oxidative deamination reaction of aromatic amines does not occur	Sus scrofa
additional information	-	additional information	T246A mutant catalyzes the oxidative deamination of D-tryptophan methyl ester with a kcat value approximately 5% with respect to the measured value for wild-type	Sus scrofa
4.5	-	L-Dopa	Y332F DDC mutant, reaction in 50 mM Hepes, pH 7.5, at 25°C causes the production of ammonia and 3,4-dihydroxyphenylacetaldehyde along with the consumption of molecular oxygen in a 1:2 molar ratio	Sus scrofa

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Release 2023.1 (January 2023)