4.1.1.11	evolution	L-aspartate alpha-decarboxylase belongs to a class of pyruvoyl dependent enzymes	728571	
4.1.1.11	evolution	Salmonella enterica and Corynebacterium glutamicum L-aspartate-alpha-decarboxylases represent two different classes of homologues of these enzymes. Class I homologues require PanM for activation, while class II self cleave in the absence of PanM. Computer modeling of conserved amino acids using structure coordinates of PanM and L-aspartate-alpha-decarboxylase available in the protein data bank (RCSB PDB) reveal a putative site of interactions, analysis of self-cleavage mechanism of L-aspartate-alpha-decarboxylases. Phylogenetic distribution of prokaryotic L-aspartate-alpha-decarboxylase and PanM proteins, distribution of the two classes of PanD in the prokaryotes, overview	-, 747435	
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	evolution	the enzyme is a member of the small class of pyruvoyl-dependent enzymes, which contain a covalently-bound pyruvoyl cofactor	-, 728266	
4.1.1.11	evolution	there are two primary types of ADCs produced from living organisms. One type is an insect ADC, which uses pyridoxal 5'-phosphate (PLP) as a cofactor. The other is bacterial ADC, which uses pyruvate as a cofactor	-, 749207	
4.1.1.11	evolution	TK1814 homologues are distributed in a wide range of archaea and may be responsible for beta-alanine biosynthesis in these organisms. The GAD-type proteins from bacteria and those from plants, fungi, and yeast are actually GADs, as diverse members of this clade have been experimentally shown to display GAD activity. The six members of GAD-type proteins from mammals and acari (an arachnid subclass) are proven to be authentic GADs, but GADL1 from mammals and GAD-type proteins from insects within this clade have been shown to be ADCs and do not harbor the corresponding Asn residues that are important for recognition of gamma-carboxylate of Glu in human GAD65 (Asn203 in human GAD65). The ADC-type proteins from bacteria can be expected to function as ADCs, but none of the ADC-type proteins from hyperthermophilic bacteria (from Aquifex aeolicus) or from archaea have been examined	-, 748086	
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	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