Literature summary for 4.1.1.28 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 4.1.1.28

Cloned(Commentary)

Cloned (Comment)	Organism
cloning and expression of wild-type DDC 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
5-hydroxy-L-tryptophan	substrate inhibition	Sus scrofa
L-Dopa	substrate inhibition	Sus scrofa

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.049	-	5-hydroxy-L-tryptophan	wild-type enzyme	Sus scrofa
0.058	-	L-Dopa	wild-type enzyme	Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5-hydroxy-L-tryptophan	Sus scrofa	-	serotonin + CO2	-	?
L-Dopa	Sus scrofa	-	dopamine + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	P80041	-	-

Purification (Commentary)

Purification (Comment)	Organism
commentary	Sus scrofa

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	The course of the reaction of Y332 mutant with 0.3 mM L-dopa has been followed at different enzyme concentrations. Although the shapes of the profiles for the interconversion of the 2 coenzymatic forms (pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate) are similar at all the enzyme concentrations tested. At each enzyme concentration there are 2 phases: at first, pyridoxamine 5'-phosphate increases at the expense of pyridoxal 5'-phosphate, and then this tendency is reversed until approximately 85% of the pyridoxal 5'-phosphate cofactor is regenerated, the amount of pyridoxamine 5'-phosphate formed relative to the initial pyridoxal 5'-phosphate content of the enzyme, during consumption of L-dopa, increases as the enzyme concentration decreases. At higher enzyme concentrations, where L-dopa consumption is faster, the accumulation of the pyridoxamine 5'-phosphate-intermediate is less appreciable. In every case the pyridoxamine 5'-phosphate species is generated during the course of linear formation of products.	Sus scrofa

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5-hydroxy-L-tryptophan	-	Sus scrofa	serotonin + CO2	-	?
L-Dopa	-	Sus scrofa	dopamine + CO2	-	?

Synonyms

Synonyms	Comment	Organism
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	Sus scrofa
additional information	-	additional information	When 50 microM Y332F DDC is mixed with 0.1 mM L-dopa under single turnover conditions up to 4 sec a gradual conversion of the pyridoxal 5'-phosphate of the enzyme takes place concomitantly to pyridoxamine 5'-phosphate and aldehyde formation while L-dopa is consumed. After 3.6 sec, 23% of the original pyridoxal 5'-phosphate is converted into pyridoxamine 5'-phosphate and 25% of the original L-dopa is transformed into 3,4-dihydroxyphenylacetaldehyde. A pyridoxamine 5'-phosphate intermediate forms during the first catalytic cycle.	Sus scrofa
0.67	-	5-hydroxy-L-tryptophan	wild-type enzyme	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
8.8	-	L-Dopa	wild-type enzyme	Sus scrofa

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Sus scrofa

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
5.7	-	5-hydroxy-L-tryptophan	wild-type enzyme, the data of initial velocity for decarboxylation of 5-hydroxy-L-tryptophan versus substrate concentration exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation.	Sus scrofa
10	-	L-Dopa	wild-type enzyme, the data of initial velocity for decarboxylation of L-dopa versus substrate concentration curiously exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation.	Sus scrofa

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)