EC Number   |
General Information |
Reference  |
|---|
    4.1.1.11 | malfunction |
ADC suppression favors formation of melanic pigment with a decrease in protein cross-linking |
714398 |
| 4.1.1.11 | metabolism |
the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, pathway overview |
726592 |
| 4.1.1.11 | more |
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 |
726592 |
| 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 | evolution |
the enzyme is a member of a small class of pyruvoyl-dependent decarboxylases, in which the enzyme-bound pyruvoyl cofactor is generated via the autocatalytic rearrangement of a serine residue via an ester intermediate |
726617 |
| 4.1.1.11 | more |
regulatory mechanisms for PanD activation and inactivation in vivo, overview |
726873 |
| 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 | more |
homology modeling and substrate docking, evaluation of potential substrate interacting residues, overview |
727622 |
| 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 | evolution |
the enzyme is a member of the small class of pyruvoyl-dependent enzymes, which contain a covalently-bound pyruvoyl cofactor |
-, 728266 |
