Literature summary for 4.1.1.11 extracted from

Webb, M.; Yorke, B.; Kershaw, T.; Lovelock, S.; Lobley, C.; Kilkenny, M.; Smith, A.; Blundell, T.; Pearson, A.; Abell, C.
Threonine 57 is required for the post-translational activation of Escherichia coli aspartate alpha-decarboxylase (2014), Acta Crystallogr. Sect. D, 70, 1166-1172.

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Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	role for Thr57 in the activation of the enzyme, while neither Tyr58 nor Tyr22 is required for the activation reaction, overview	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant T57V mutant enzyme, hanging drops by vapour diffusion with a 1:1 ratio of protein to precipitant, 7.5 mg/ml protein, 1.5-3.4 M sodium malonate, pH 4.0, method optimization, 17°C, X-ray diffraction structure determination and analysis at 1.62 A resolution, modeling	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
I60A	site-directed mutagenesis, the PanD activation activity is affected	Escherichia coli
I86A	site-directed mutagenesis, the PanD activation activity is affected	Escherichia coli
S70A	site-directed mutagenesis, the PanD activation activity is affected	Escherichia coli
T57V	site-directed mutagenesis, mutation of Thr57 leads to abolition of the activation reaction at 37°C, structural consequences of mutation of Thr57, crystal structure, in the T57V mutant the unprocessed chain is displaced from the active site owing to the binding of a single molecule of the cryoprotectant malonate, overview	Escherichia coli
W47A	site-directed mutagenesis, the PanD activation activity is affected	Escherichia coli
Y22F	site-directed mutagenesis, the PanD activation activity is affected	Escherichia coli
Y58F	site-directed mutagenesis, the PanD activation activity is affected	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-aspartate	Escherichia coli	-	beta-alanine + CO2	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A790	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	role for Thr57 in the activation of the enzyme, while neither Tyr58 nor Tyr22 is required for the activation reaction, overview	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate	-	Escherichia coli	beta-alanine + CO2	-	?

Synonyms

Synonyms	Comment	Organism
ADC	-	Escherichia coli
Aspartate alpha-decarboxylase	-	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
pyruvoyl cofactor	dependent on. Pathway for the formation of the pyruvoyl-dependent cofactor in ADC: the beta-hydroxyl of Ser25 attacks the carbonyl of the previous amino-acid residue (i) to form an oxyoxazolidine intermediate, which decomposes (ii) to form an ester intermediate. E1cB elimination (iii) forms a N-terminal dehydroalanyl residue which is hydrolysed (iv) to form the pyruvoyl cofactor (the alpha'-chain). The ester intermediate can also be hydrolysed to yield the inactive alpha'-chain	Escherichia coli

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, pathway overview	Escherichia coli
additional information	role for Thr57 in the activation of the enzyme, its first role is that it acts as a general acid to support the formation of the ester intermediate by supporting the formation of the negative charge in the oxyoxazolidine intermediate, the second role is that after formation of the ester intermediate it acts as a general base to deprotonate the alpha-proton of Ser25, leading to chain cleavage and the formation of a dehydroalanine residue. Neither Tyr58 nor Tyr22 is required for the activation reaction, overview	Escherichia coli
physiological function	aspartate alpha-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of beta-alanine in the bacterial pantothenate (vitamin B5) biosynthesis pathway	Escherichia coli

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Release 2023.1 (January 2023)