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 (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 | 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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | Escherichia coli | - |
beta-alanine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A790 | - |
- |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | - |
Escherichia coli | beta-alanine + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ADC | - |
Escherichia coli |
Aspartate alpha-decarboxylase | - |
Escherichia coli |
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 | 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 |