EC Number   |
General Information |
Reference |
|---|
    4.1.1.11 | more |
three key amino acid residues, R54, Y58, and R3, of L-aspartate alpha-decarboxylase act remotely from its cleavage site for its functional self-cleavage as well as for its catalytic activity. Highly conserved R54 residue contributes to the enzyme substrate specificity, and the highly conserved Y58 residue acts as the proton donor in the decarboxylation reaction. R54 and Y58 residues are also related with the self-cleavage process. The R54 and Y58 residues also block the formation of the active pyruvoyl cofactor, therefore the R54 and Y58 residues are assisting the R3 residue in the ADC self-cleavage process |
-, 727234 |
| 4.1.1.11 | 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 |
726592 |
| 4.1.1.11 | physiological function |
enzyme BmADC plays a crucial role in melanin metabolism and in the pigmentation pattern of the silkworm pupal stage |
749304 |
| 4.1.1.11 | physiological function |
L-aspartate alpha-decarboxylase is the key enzyme that catalyzes the decarboxylation of L-aspartate to beta-alanine, the only naturally occurring beta-amino acid |
-, 749207 |
| 4.1.1.11 | physiological function |
regulation of PanD by PanZ allows these organisms to closely regulate production of beta-alanine and hence pantothenate in response to metabolic demand in host gut flora, where pantothenate is abundant |
-, 728266 |
| 4.1.1.11 | physiological function |
the enzyme is a a glutamate decarboxylase (GAD) homologue encoded by gene TK1814. The recombinant bifunctional TK1814 protein displays not only GAD activity but also ADC activity using pyridoxal 5'-phosphate as a cofactor. The GAD activity of TK1814 is not necessary for growth |
-, 748086 |
| 4.1.1.11 | physiological function |
the enzyme is involved in the regulation of pantothenate biosynthesis |
747497 |
| 4.1.1.11 | physiological function |
the MJ0050 gene complements the Escherichia coli panD deletion mutant cells, in which panD encoding aspartate decarboxylase in Escherichia coli has been knocked out, thus confirming the function of this gene in vivo |
-, 727784 |
| 4.1.1.11 | physiological function |
the PanDZ complex regulates the pantothenate biosynthetic pathway in a cellular context in Escherichia coli by limiting the supply of beta-alanine in response to coenzyme A concentration. Formation of such a complex between activated aspartate decarboxylase (PanD) and regulatory protein PanZ leads to sequestration of the pyruvoyl cofactor as a ketone hydrate. Regulation of PanD is due to CoA-dependent interaction of PanZ and PanD |
747128 |
