EC Number   |
General Information |
Reference |
|---|
    4.1.1.11 | malfunction |
a mutation in the aspartate decarboxylase gene (BmADC) causes melanized pupae with melanization specifically only at the pupal stage, the bp mutant phenotype. In the bp mutant, a SINE-like transposon insertion causes a sharp reduction in BmADC transcript levels in bp mutants, leading to deficiency of beta-alanine and N-beta-alanyl dopamine (NBAD), but accumulation of dopamine. Enzyme knockout also leads to the melanic pupae. The color pattern is reverted to that of the wild-type silkworms following injection of beta-alanine into bp mutants. Larvaeal bp phenotype, overview. Absence of beta-alanine and excessive accumulation of dopamine in the bp mutant |
749304 |
| 4.1.1.11 | malfunction |
ADC suppression favors formation of melanic pigment with a decrease in protein cross-linking |
714398 |
| 4.1.1.11 | malfunction |
an in vivo-selected pyrazinoic acid-resistant Mycobacterium tuberculosis strain harbors a missense mutation in the aspartate decarboxylase PanD. Mice infected with wild-type Mycobacterium tuberculosis are treated with pyrazinoic acid (POA), and POA-resistant colonies are confirmed for pyrazinamide (PZA) and POA resistance. Genome sequencing reveals that 82% and 18% of the strains contain missense mutations in panD and clpC1, respectively. POA/PZA resistance-conferring panD mutations are observed in POA-treated mice but not yet among clinical strains isolated from PZA-treated human patients |
746598 |
| 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 | malfunction |
both regulatory protein PanZ overexpression-linked beta-alanine auxotrophy and pentyl pantothenamide toxicity are due to formation of the PanDZ complex between enzyme PanD and effector protein PanZ. Formation of such a complex between activated aspartate decarboxylase (PanD) and PanZ leads to sequestration of the pyruvoyl cofactor as a ketone hydrate and demonstrates that both PanZ overexpression-linked beta-alanine auxotrophy and pentyl pantothenamide toxicity are due to formation of this complex. Substitution of the Escherichia coli panD for the noninteracting Bacillus panD suppresses the phenotype |
747128 |
| 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 | metabolism |
enzyme PanD is responsible for the production of beta-alanine in the pantothenate biosynthesis pathway. The production of beta-alanine is feedback-regulated by the PanZ-AcCoA complex |
747128 |
| 4.1.1.11 | malfunction |
gene disruption of TK1814 results in a strain that cannot grow in standard medium. Addition of beta-alanine, 4'-phosphopantothenate, or CoA complements the growth defect, whereas gamma-aminobutyrate (GABA) cannot complement |
-, 748086 |
| 4.1.1.11 | more |
homology modeling and substrate docking, evaluation of potential substrate interacting residues, overview |
727622 |
| 4.1.1.11 | evolution |
L-aspartate alpha-decarboxylase belongs to a class of pyruvoyl dependent enzymes |
728571 |
