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evolution
-
L-aspartate alpha-decarboxylase belongs to a class of pyruvoyl dependent enzymes
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
evolution
-
the enzyme is a member of the small class of pyruvoyl-dependent enzymes, which contain a covalently-bound pyruvoyl cofactor
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
evolution
Halalkalibacterium halodurans
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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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
-
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
-
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
-
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
-
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
-
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
-
evolution
-
the enzyme is a member of the small class of pyruvoyl-dependent enzymes, which contain a covalently-bound pyruvoyl cofactor
-
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
-
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
-
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
-
evolution
Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125
-
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
-
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
-
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
-
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
-
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
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malfunction
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ADC suppression favors formation of melanic pigment with a decrease in protein cross-linking
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
malfunction
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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
malfunction
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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
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
malfunction
-
protein PanZ is essential for activation of the zymogen PanD to form ADC in vivo, and its deletion leads to beta-alanine auxotrophy
malfunction
the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production. The E56S mutant shows an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuated the mechanism-based inactivation of the enzyme
malfunction
when expressed in the Salmonella enterica DELTApanM strain, all panD homologues from bacteria that also contain a panM gene (Salmonella enterica, Klebsiella pneumoniae, Pseudomonas aeruginosa) fail to restore growth on minimal medium
malfunction
-
the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production. The E56S mutant shows an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuated the mechanism-based inactivation of the enzyme
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malfunction
-
when expressed in the Salmonella enterica DELTApanM strain, all panD homologues from bacteria that also contain a panM gene (Salmonella enterica, Klebsiella pneumoniae, Pseudomonas aeruginosa) fail to restore growth on minimal medium
-
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
-
metabolism
-
L-aspartate alpha-decarboxylase catalyzes the conversion of aspartate to beta-alanine in the pantothenate pathway, which is critical for the growth of Mycobacterium tuberculosis
metabolism
-
the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, overview
metabolism
the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, pathway overview
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
metabolism
the enzyme is involved in the melanin metabolism pathway and in the melanin metabolism from dopamine to N-beta-alanyl dopamine (NBAD)
metabolism
-
the structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A, regulatory model whereby the mature enzyme activity is limited and regulated by the concentration of CoA in the cell. Inhibition of mature enzyme catalysis reveals a second global role for PanZ in regulation of pantothenate biosynthesis. Such inhibitory activity is actually the primary metabolic role of PanZ, although the activation is also clearly essential
metabolism
-
the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, overview
-
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
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
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
physiological function
enzyme BmADC plays a crucial role in melanin metabolism and in the pigmentation pattern of the silkworm pupal stage
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
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
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
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
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
physiological function
-
the enzyme is involved in the regulation of pantothenate biosynthesis
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
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
-
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
-
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
-
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
-
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
-
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
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additional information
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homology modeling and substrate docking, evaluation of potential substrate interacting residues, overview
additional information
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regulatory mechanisms for PanD activation and inactivation in vivo, overview
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
additional information
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the enzyme active site is formed by the interface of a dimer, with relatively small volume. This cleft can support only molecules of relatively small size
additional information
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the enzyme PanD is synthesized as pro-PanD, which undergoes an auto-proteolytic cleavage at residue Ser25 to yield the catalytic pyruvoyl moiety of the enzyme
additional information
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
additional information
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NMR analysis of the PanD-PanZ-AcCoA complex
additional information
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PanD-PanZ complex three-dimensional structure analysis, overview
additional information
structural homology modeling BsADC using the Escherichia coli ADC structure, PDB ID 1PQE, as template
additional information
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen
additional information
the L-aspartate-alpha-decarboxylase zymogen from Corynebacterium glutamicum does not require PanM to process its own maturation
additional information
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structural homology modeling BsADC using the Escherichia coli ADC structure, PDB ID 1PQE, as template
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additional information
-
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
-
additional information
-
the L-aspartate-alpha-decarboxylase zymogen from Corynebacterium glutamicum does not require PanM to process its own maturation
-
additional information
-
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen
-
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proteolytic modification
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
proteolytic modification
the enzyme performs self-cleavage posttranslationally
proteolytic modification
-
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
-
proteolytic modification
-
the enzyme performs self-cleavage posttranslationally
-
proteolytic modification
-
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
-
proteolytic modification
the panD gene product is efficiently proteolytically processed into two subunits, an 11 kDa alpha-subunit and a 2.7 kDa beta-subunit, Gly-24/Ser-25 may be the processing site of the initially translated pi-protein
proteolytic modification
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Corynebacterium glutamicum after expression in Escherichia coli is almost complete
proteolytic modification
the enzyme performs self-cleavage posttranslationally
proteolytic modification
-
the ADC protein is initially translated as an inactive Pi-protein and then proteolytically cleaved at a site to generate the active species comprising the pyruvoyl-containing alpha-subunit and a smaller beta-subunit. The cleavage of the recombinant ADC protein from Corynebacterium glutamicum after expression in Escherichia coli is almost complete
-
proteolytic modification
-
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
-
proteolytic modification
-
the enzyme performs self-cleavage posttranslationally
-
proteolytic modification
ADC, which is translated as inactive pro-protein, i.e. pi-protein, undergoes intramolecular self-cleavage at Gly-24/Ser-25 producing the alpha- and beta-subunit, molecular mechanism of self-processing, slow process
proteolytic modification
-
an integral pyruvoyl group is formed by an autocatalytic posttranslational modification which cleaves the Gly-24/Ser-25 bond and converts Ser-25 into the pyruvoyl group
proteolytic modification
panD is initially translated as inactive precursor pi-protein which is slowly proteolytically cleaved at a specific Gly-Ser bond producing two dissimilar subunits, autocatalytic mechanism
proteolytic modification
-
PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD, cleavage of the recombinant FLAG-tag PanD by recombinant His-tagged PanZ
proteolytic modification
role for Thr57 in the activation of the enzyme, while neither Tyr58 nor Tyr22 is required for the activation reaction, overview
proteolytic modification
bacterial ADC is usually translated into an inactive zymogen. The zymogen is proteolytically cleaved at the Gly24-Ser25 site. The Escherichia coli ADC requires a Gcn5-like N-acetyltransferase, named PanM (also called PanZ), to help it reach complete maturation
proteolytic modification
-
PanZ promotes the activation of the zymogen of PanD to form aspartate alpha-decarboxylase (ADC) in a CoA-dependent manner. Binding of PanZ promotes PanD processing, catalytic mechanism, detailed overview. Before binding of PanZ, the carbonyl of Gly24 forms a hydrogen bond to the side chain of Thr57. Binding of PanZ induces a conformation change in the peptide chain rotating the carbonyl of Gly24 to hydrogen bond to Tyr58 and shifting the hydroxyl of Ser25 to a position where reaction is possible. Following attack of the Ser25 hydroxyl on the carbonyl of Gly24 to form the oxyoxazolidine intermediate III, the side chain of Thr57 donates a proton to facilitate cleavage of the C-N bond to form the ester intermediate IV. The deprotonated Thr57 residue is then able to remove the a proton from Ser25 to cleave the peptide chain and generate a dehydroalanine residue V, which hydrolyzes to form the active enzyme
proteolytic modification
the ADC protein is initially translated as an inactive Pi-protein (14 kDa) and then proteolytically cleaved at the Gly24-Ser25 site to generate the active species comprising the pyruvoyl-containing alpha-subunit (11 kDa) and a smaller beta-subunit (3 kDa). The enzyme requires PanZ as an activator involved in the cleavage of ADCE. The recombinant ADC protein expressed from Escherichia coli strain BL21(DE3) is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
proteolytic modification
the enzyme requires activation by PanZ to be posttranslationally cleaved
proteolytic modification
-
the ADC protein is initially translated as an inactive Pi-protein (14 kDa) and then proteolytically cleaved at the Gly24-Ser25 site to generate the active species comprising the pyruvoyl-containing alpha-subunit (11 kDa) and a smaller beta-subunit (3 kDa). The enzyme requires PanZ as an activator involved in the cleavage of ADCE. The recombinant ADC protein expressed from Escherichia coli strain BL21(DE3) is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
-
proteolytic modification
-
PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD, cleavage of the recombinant FLAG-tag PanD by recombinant His-tagged PanZ
-
proteolytic modification
-
panD is initially translated as inactive precursor pi-protein which is slowly proteolytically cleaved at a specific Gly-Ser bond producing two dissimilar subunits, autocatalytic mechanism
-
proteolytic modification
self-processing of subunits at Gly24-Ser25 producing beta-chain with residues 1-24 and alpha chain with residues 25-117. In the apo structure, Ser25, which forms the N-terminus of alpha chain, is converted to a pyruvoyl group
proteolytic modification
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
proteolytic modification
-
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
-
proteolytic modification
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
proteolytic modification
-
bacterial ADC is usually translated into an inactive zymogen. The initially inactive recombinant Pi-protein ADC of approximately 14 kDa self-cleaves to form an active enzyme consisting of alpha-protein (approximately 11 kDa) and beta-protein (approximately 3 kDa). The enzyme completely self-cleaves and self-maturates, zymogen is proteolytically cleaved at the Gly24-Ser25 site
-
proteolytic modification
-
incubation of panD at 37°C for several hours results in a complete cleavage of the inactive pi-form into the two subunits alpha and beta, optimal cleavage at 37°C for 48 h, cleavage mechanism
proteolytic modification
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the enzyme is autocatalytically self-processing, overview
proteolytic modification
-
incubation of panD at 37°C for several hours results in a complete cleavage of the inactive pi-form into the two subunits alpha and beta, optimal cleavage at 37°C for 48 h, cleavage mechanism
-
proteolytic modification
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
proteolytic modification
-
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
-
proteolytic modification
-
PanD is a pyruvoyl enzyme that is synthesized by the cell as an inactive precursor, pro-PanD. Maturation of pro-PanD into PanD occurs via a self-cleavage event at residue Ser25, which forms the catalytic pyruvoyl moiety. Salmonella enterica PanM, a Gcn5-like N-acetyltransferase, is necessary for pro-PanD maturation, both in vitro and in vivo
proteolytic modification
-
the enzyme PanD is synthesized as pro-PanD, which undergoes an auto-proteolytic cleavage at residue Ser25 to yield the catalytic pyruvoyl moiety of the enzyme, interaction with YhhK, i.e. PanM, accelerates the maturation process
proteolytic modification
-
PanD is a pyruvoyl enzyme that is synthesized by the cell as an inactive precursor, pro-PanD. Maturation of pro-PanD into PanD occurs via a self-cleavage event at residue Ser25, which forms the catalytic pyruvoyl moiety. Salmonella enterica PanM, a Gcn5-like N-acetyltransferase, is necessary for pro-PanD maturation, both in vitro and in vivo
-
proteolytic modification
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
proteolytic modification
-
the ancillary protein PanM (formerly YhhK) is required in vitro and in vivo for cleavage of the L-aspartate-alpha-decarboxylase zymogen. Conserved regions of PanM form a domain where putative interactions with L-aspartate-alpha-decarboxylases may interact, PanD and PanM structure comparisons, overview
-
additional information
the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation
additional information
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the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation
-
additional information
the L-aspartate-alpha-decarboxylase zymogen from Corynebacterium glutamicum does not require PanM to process its own maturation
additional information
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the L-aspartate-alpha-decarboxylase zymogen from Corynebacterium glutamicum does not require PanM to process its own maturation
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additional information
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the Escherichia coli enzyme requires the regulatroy factor PanZ for proteolytic cleavage of the zymogen to form the mature enzyme
additional information
Halalkalibacterium halodurans
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the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation
additional information
Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125
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the L-aspartate-alpha-decarboxylase zymogen from Bacillus halodurans does not require PanM to process its own maturation
-
additional information
the L-aspartate-alpha-decarboxylase zymogen from Helicobacter pylori does not require PanM to process its own maturation
additional information
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the L-aspartate-alpha-decarboxylase zymogen from Helicobacter pylori does not require PanM to process its own maturation
-
additional information
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the L-aspartate-alpha-decarboxylase zymogen from Legionella phneumophila does not require PanM to process its own maturation
additional information
the L-aspartate-alpha-decarboxylase zymogen Magnetospirillum magneticum does not require PanM to process its own maturation
additional information
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the L-aspartate-alpha-decarboxylase zymogen Magnetospirillum magneticum does not require PanM to process its own maturation
-
additional information
the L-aspartate-alpha-decarboxylase zymogen from Moorella thermoacetica does not require PanM to process its own maturation
additional information
-
the L-aspartate-alpha-decarboxylase zymogen from Moorella thermoacetica does not require PanM to process its own maturation
-
additional information
the L-aspartate-alpha-decarboxylase zymogen from Neisseria gonorrhoeae does not require PanM to process its own maturation
additional information
-
the L-aspartate-alpha-decarboxylase zymogen from Neisseria gonorrhoeae does not require PanM to process its own maturation
-
additional information
the L-aspartate-alpha-decarboxylase zymogen from Ralstonia solanacearum does not require PanM to process its own maturation
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Q377L
-
site-directed mutagenesis, mutation at position 377 from glutamine to leucine in aspartate 1-decarboxylase diminishes its decarboxylation activity to aspartate with no major effect on its cysteine sulfinic acid decarboxylase activity
D41G
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
E56S
site-directed mutagenesis, the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production, but no significant effect on the cell growth properties or the molecular weight of BsADC. The E56S mutant shows a 1.6fold higher activity and an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuates the mechanism-based inactivation of the enzyme. The mutant enzyme catalyzes the beta-alanine synthesis with a very high product yield of 215.3 g per liter culture. In BsADC, Glu56 corresponds to Ser56 in the center channel of the homotetramer ADC from Escherichia coli. Due to the shorter side chain of Ser56, the Glu56-to-Ser56 mutation may enhance the import of the Asp substrate and export of the beta-alanine product in the tetramer channel
I188M
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type
K63E
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
D41G
-
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
-
E56S
-
site-directed mutagenesis, the Glu56Ser mutation improves the enzymatic activity and catalytic stability of L-aspartate alpha-decarboxylase for an efficient beta-alanine production, but no significant effect on the cell growth properties or the molecular weight of BsADC. The E56S mutant shows a 1.6fold higher activity and an approximately 1.4fold increased residual activity compared with the wild-type during 2 h reaction at 37°C, suggesting that the E56S mutation attenuates the mechanism-based inactivation of the enzyme. The mutant enzyme catalyzes the beta-alanine synthesis with a very high product yield of 215.3 g per liter culture. In BsADC, Glu56 corresponds to Ser56 in the center channel of the homotetramer ADC from Escherichia coli. Due to the shorter side chain of Ser56, the Glu56-to-Ser56 mutation may enhance the import of the Asp substrate and export of the beta-alanine product in the tetramer channel
-
I188M
-
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type
-
K63E
-
site-directed mutagenesis, the mutation improves the enzyme activity compared to wild-type
-
R3A
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3D
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3E
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3L
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3N
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R3Q
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
R54A
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
R54K
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
Y58A
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
Y58T
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
R3A
-
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
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R3Q
-
site-directed mutagenesis, the mutant is no longer able to activate via self-cleavage
-
R54A
-
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
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R54K
-
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
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Y58A
-
site-directed mutagenesis, the mutant shows highly reduced self-cleavage activity compared to the wild-type enzyme
-
G24S
study of the structure and processing activity
H11A
study of the structure and processing activity
I60A
site-directed mutagenesis, the PanD activation activity is affected
I86A
site-directed mutagenesis, the PanD activation activity is affected
K115A
-
site-directed mutagenesis, the mutation is introduced in vitro by overlap extension PCR
K119A
-
site-directed mutagenesis, the mutation is introduced in vitro by overlap extension PCR. Complex formation of the site-directed mutants PanZ(R73A) and PanD(K119A) leads to a complex that still complements the beta-alanine auxotrophy of the DELTApanZ and DELTApanD strains, indicating that catalytically active PanD is formed, but no growth inhibition is observed as a result of PanZ overexpression
K14A
-
site-directed mutagenesis, the mutation is introduced in vitro by overlap extension PCR
K53A
-
site-directed mutagenesis, the mutation is introduced in vitro by overlap extension PCR
N72A
site-directed mutagenesis, in the Asn72Ala mutant the C-terminal region residues are ordered, in contrast to the wild-type enzyme, owing to an interaction with the active site of the neighbouring symmetry-related multimer
S25A
inactive mutant, study of the structure and processing activity
S25C
study of the structure and processing activity
S25T
inactive mutant, study of the structure and processing activity
S70A
site-directed mutagenesis, the PanD activation activity is affected
W47A
site-directed mutagenesis, the PanD activation activity is affected
Y22F
site-directed mutagenesis, the PanD activation activity is affected
Y58F
site-directed mutagenesis, the PanD activation activity is affected
A128E
-
naturally occuring mutation after treatment with pyrazinoic acid
A128S
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naturally occuring mutation after treatment with pyrazinoic acid
C17R
-
naturally occuring mutation after treatment with pyrazinoic acid
D116Y
-
naturally occuring mutation after treatment with pyrazinoic acid
E130G
-
naturally occuring mutation after treatment with pyrazinoic acid
F107L
-
naturally occuring mutation after treatment with pyrazinoic acid
H21N
-
naturally occuring mutation after treatment with pyrazinoic acid
H21Q
-
naturally occuring mutation after treatment with pyrazinoic acid
I115V
-
naturally occuring mutation after treatment with pyrazinoic acid
L131P
-
naturally occuring mutation after treatment with pyrazinoic acid
L136P
-
naturally occuring mutation after treatment with pyrazinoic acid
L136R
-
naturally occuring mutation after treatment with pyrazinoic acid
M117I
-
naturally occuring mutation after treatment with pyrazinoic acid
M117V
-
naturally occuring mutation after treatment with pyrazinoic acid
N127K
-
naturally occuring mutation after treatment with pyrazinoic acid
V138A
-
naturally occuring mutation after treatment with pyrazinoic acid
V138M
-
naturally occuring mutation after treatment with pyrazinoic acid
T57V
-
site-directed mutagenesis
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
T57V
-
site-directed mutagenesis, an inactivatable PanD mutant
additional information
mutation of nucleotide L127 increases the enzyme's thermostability compared to the wild-type, while mutation of nuclotide V68 does not significantly affect the thermostability
additional information
-
mutation of nucleotide L127 increases the enzyme's thermostability compared to the wild-type, while mutation of nuclotide V68 does not significantly affect the thermostability
-
additional information
construction of a bp mutant strain 16-100 (bp/bp). In the bp mutant, a SINE-like transposon with a length of 493 bp is detected about 2.2 kb upstream of the transcriptional start site of the BmADC gene. This 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. The mutant is specifically melanized only at the pupal stage. Following injection of beta-alanine into bp mutants, the color pattern is reverted to that of the wild-type silkworms. Additionally, melanic pupae resulting from knockdown of BmADC in the wild-type strain are obtained by RNAi of BmADC
additional information
-
construction of a bp mutant strain 16-100 (bp/bp). In the bp mutant, a SINE-like transposon with a length of 493 bp is detected about 2.2 kb upstream of the transcriptional start site of the BmADC gene. This 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. The mutant is specifically melanized only at the pupal stage. Following injection of beta-alanine into bp mutants, the color pattern is reverted to that of the wild-type silkworms. Additionally, melanic pupae resulting from knockdown of BmADC in the wild-type strain are obtained by RNAi of BmADC
additional information
panD insertion mutant ND2 completely lacks enzyme activity and exhibits beta-alanine auxotrophy
additional information
-
panD insertion mutant ND2 completely lacks enzyme activity and exhibits beta-alanine auxotrophy
additional information
synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum recombinantly expressed in Escherichia coli strain BL21(DE3). A pH-stat directed, fed-batch feeding strategy is developed for enzymatic synthesis of beta-alanine to keep the pH value within pH 6.0-7.2 and attenuate substrate inhibition. A maximum conversion of 97.2% is obtained with an initial 5 g L-aspartate/l and another three feedings of 0.5 % w/v L-aspartate at 8 h intervals. The final beta-alanine concentration is 12.85 g/l after 36 h, method optimization, overview. Recombinant enzyme ADC shows best activity in sodium phosphate buffer at pH 6 and more than 80% activity remained between pH 4-7. The Escherichia coli BL21 (DE3)-pET heterologous system provides higher expression efficiency compared with that of homologous expression, which results in a 24fold increase in specific activity of crude enzyme
additional information
-
synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum recombinantly expressed in Escherichia coli strain BL21(DE3). A pH-stat directed, fed-batch feeding strategy is developed for enzymatic synthesis of beta-alanine to keep the pH value within pH 6.0-7.2 and attenuate substrate inhibition. A maximum conversion of 97.2% is obtained with an initial 5 g L-aspartate/l and another three feedings of 0.5 % w/v L-aspartate at 8 h intervals. The final beta-alanine concentration is 12.85 g/l after 36 h, method optimization, overview. Recombinant enzyme ADC shows best activity in sodium phosphate buffer at pH 6 and more than 80% activity remained between pH 4-7. The Escherichia coli BL21 (DE3)-pET heterologous system provides higher expression efficiency compared with that of homologous expression, which results in a 24fold increase in specific activity of crude enzyme
-
additional information
-
black1 mutant flies have significantly reduced enzyme activity in adults and at purpuration formation, and no enzyme protein
additional information
inactive Ala-24 and Ala-26 insertion mutants, study of the structure and processing activity
additional information
panD mutants
additional information
-
panD mutants
additional information
-
the expression of the enzyme in transgenic Nicotiana tabacum cv. Havana 38 leads to increased beta-alanine and pantothenate levels and improved thermotolerance in the tobacco plants, growth of homozygous lines expressing the bacterial enzyme is less affected than that of the control lines when the plants are stressed for 1 week at 35°C, tobacco seed germination at 42C is improved, phenotype,overview
additional information
-
generation of diverse panD deletion mutant strains, overview
additional information
-
generation of diverse panD deletion mutant strains, overview
-
additional information
-
panD mutants
-
additional information
-
construction of a panD mutant strain, the panD mutant grows as well as the wild-type in infected mice. 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. Location of amino acid sequence polymorphisms in PanD of POA-resistant Mycobacterium tuberculosis strains isolated from POA-treated mice
additional information
-
the PanM-deficient Salmonella enterica strain JE13153 is inactive due to impaired activation of PanD
additional information
generation of knockout mutants DELTApanD (JE13233) and DELTApanM (JE12555) strains
additional information
-
generation of knockout mutants DELTApanD (JE13233) and DELTApanM (JE12555) strains
-
additional information
construction of a TK1814 gene disruption strain, phenotype, overview. The TK1814 strain does not show growth for 24 h, suggesting that the ADC and/or GAD activities of TK1814 are essential for growth in this medium. When exogenous beta-alanine, the product of ADC activity, is added to the medium, the growth defects are almost fully recovered. In contrast, the addition of GABA, the product of GAD activity, does not complement TK1814 disruption at all
additional information
-
construction of a TK1814 gene disruption strain, phenotype, overview. The TK1814 strain does not show growth for 24 h, suggesting that the ADC and/or GAD activities of TK1814 are essential for growth in this medium. When exogenous beta-alanine, the product of ADC activity, is added to the medium, the growth defects are almost fully recovered. In contrast, the addition of GABA, the product of GAD activity, does not complement TK1814 disruption at all
additional information
-
construction of a TK1814 gene disruption strain, phenotype, overview. The TK1814 strain does not show growth for 24 h, suggesting that the ADC and/or GAD activities of TK1814 are essential for growth in this medium. When exogenous beta-alanine, the product of ADC activity, is added to the medium, the growth defects are almost fully recovered. In contrast, the addition of GABA, the product of GAD activity, does not complement TK1814 disruption at all
-
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ADC expression analysis, expression of the HIs-tagged enzyme in Escherichia coli
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expressed in Nicotiana tabacum
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expression in Escherichia coli (DE3)
expression of His6tagged enzyme in Escherichia coli
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gene panD, expression of Corynebacterium glutamicum panD in Salmonella enterica panM deficient strain JE13233 shows functional complementation, thus the Corynebacterium glutamicum enzyme does not required panM activation
-
gene panD, expression of enzyme mutant N72A in Escherichia coli strain C41 (DE3)
gene panD, expression of His-tagged enzyme mutant T57V and PanZ in Escherichia coli strain DELTApanD DELTApanZ (DE3)
-
gene panD, expression of wild-type and mutant enzymes in Escherichia coli
gene panD, functional recombinant expression in enzyme-deficient Zymomonas mobilis strain ZM4, the heterologous expression of the Escherichia coli enzyme eliminates the need for exogenous pantothenate by the auxotrophic strain, that is incapable of making both beta-alanine and pantoate. beta-Alanine can substitute for pantothenate (pan) to support strain ZM4 growth
gene panD, heterologous expression in panM-deficient Salmonella enterica strain JE13153, functional complementation in PanD activity
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gene panD, phylogenetic tree, expression of nontagged enzyme in Escherichia coli panZ-deficient strain SN227, expression of His-tagged wild-type and mutant enzymes in Escherichia coli, expression of flag3-tagged enzyme from gene panD with the cat gene inserted between frt sites in Escherichia coli strain MG1655
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gene panD, recombinant expression in Escherichia coli strain BL21(DE3)
gene panD, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein
gene panD, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), the recombinant ADC protein is mainly in its inactive uncleaved form, possibly because of insufficience of panZ, an activator involved in the cleavage of ADCE
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3). The cleavage of the recombinant ADC protein from Bacillus subtilis after expression in Escherichia coli is almost complete
gene panD, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3). The cleavage of the recombinant ADC protein from Corynebacteriums glutamicum after expression in Escherichia coli is almost complete
gene panD, recombinant expression of the enzyme in Escherichia coli strain BL21(DE3)
gene panD, recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain C41(DE3), subcloning in Escherichia coli strain MG1655. Overexpression-linked growth inhibition is dependent upon CoA-dependent interaction of PanZ with PanD
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gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Bacillus halodurans enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Helicobacter pylori enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Klebsiella pneumoniae enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement only the DELTApanD strain, but fails to restore growth on minimal medium in the DELTApanM strain
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Legionella phneumophila enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
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gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Magnetospirillum magneticum enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Moorella thermoacetica enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Neisseria gonorrhoeae enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Pseudomonas aeruginosa enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement only the DELTApanD strain, but fails to restore growth on minimal medium in the DELTApanM strain
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Ralstonia solanacearum enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Samonella enterica enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement only the DELTApanD strain, but fails to restore growth on minimal medium in the DELTApanM strain
gene panD, sequence comparisons and phylogenetic analysis, the recombinant expression of the Corynabacterium glutamicum enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
gene panD, subcloning and expression in strain DH5alpha, BL21(DE3), and in an enzyme-deficient strain, functional expression under the constitutive CaMV 35S promoter in transgenic Nicotiana tabacum cv. Havana 38 leaves using the Agrobacterium tumefaciens transfection system
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gene TK1814, phylogenetic analysis, recombinant overexpression in Escherichia coli strain BL21-CodonPlus(DE3)-RIL
genetic mapping, sequence comparisons and phylogenetic analysis, quantitative RT-PCR enzyme expression analysis
overexpression in Escherichia coli
panD gene overexpression
-
panD gene, overexpression in Corynebacterium glutamicum with 4fold increased enzyme activity and in Escherichia coli with 3fold increased enzyme activity
panD gene, overexpression in Escherichia coli C41(DE3)
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panD gene, overexpression in Escherichia coli, sequencing
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panD gene, sequencing, overexpression in Corynebacterium glutamicum with 288fold increased enzyme activity and in Escherichia coli with 41fold increased enzyme activity
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gene panD, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein
gene panD, recombinant expression of His-tagged wild-type enzyme in Escherichia coli strain BL21(DE3), the enzyme is initially translated as inactive Pi-protein
gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Bacillus halodurans enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
Halalkalibacterium halodurans
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gene panD, sequence comparisons and phylogenetic analysis, recombinant expression of the Bacillus halodurans enzyme in DELTApanD as well as DELTApanM mutant Samonella enterica strains can functionally complement both mutant strains and restore growth on minimal medium
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Williamson, J.M.
L-Aspartate alpha-decarboxylase
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Escherichia coli, Escherichia coli B / ATCC 11303
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Purification and properties of L-aspartate-alpha-decarboxylase, an enzyme that catalyzes the formation of beta-alanine in Escherichia coli
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Escherichia coli, Escherichia coli B / ATCC 11303
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Crystallization and preliminary X-ray crystallographic analysis of aspartate 1-decarboxylase from Helicobacter pylori
Acta Crystallogr. Sect. D
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Helicobacter pylori
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Dusch, N.; Phler, A.; Kalinowski, J.
Expression of the Corynebacterium glutamicum panD gene encoding L-aspartate-alpha-decarboxylase leads to pantothenate overproduction in Escherichia coli
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Corynebacterium glutamicum (Q9X4N0), Corynebacterium glutamicum, Escherichia coli (P0A790), Escherichia coli, Escherichia coli MG1655 (P0A790)
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Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction
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Escherichia coli
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Escherichia coli (P0A790)
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Expression, purification, and biochemical characterization of Mycobacterium tuberculosis aspartate decarboxylase, PanD
Protein Expr. Purif.
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Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Phillips, A.M.; Smart, R.; Strauss, R.; Brembs, B.; Kelly, L.E.
The Drosophila black enigma: The molecular and behavioural characterization of the black1 mutant allele
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Drosophila melanogaster
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Helicobacter pylori (P56065), Helicobacter pylori
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Fouad, W.M.; Rathinasabapathi, B.
Expression of bacterial L-aspartate-alpha-decarboxylase in tobacco increases beta-alanine and pantothenate levels and improves thermotolerance
Plant Mol. Biol.
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Escherichia coli
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Gopalan, G.; Chopra, S.; Ranganathan, A.; Swaminathan, K.
Crystal structure of uncleaved L-aspartate-alpha-decarboxylase from Mycobacterium tuberculosis
Proteins
65
796-802
2006
Mycobacterium tuberculosis
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Arakane, Y.; Lomakin, J.; Beeman, R.W.; Muthukrishnan, S.; Gehrke, S.H.; Kanost, M.R.; Kramer, K.J.
Molecular and functional analyses of amino acid decarboxylases involved in cuticle tanning in Tribolium castaneum
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Tribolium castaneum (A7U8C7), Tribolium castaneum, Tribolium castaneum GA-1 (A7U8C7)
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Transplastomic expression of bacterial L-aspartate-alpha-decarboxylase enhances photosynthesis and biomass production in response to high temperature stress
Transgenic Res.
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Escherichia coli
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Lomakin, J.; Huber, P.A.; Eichler, C.; Arakane, Y.; Kramer, K.J.; Beeman, R.W.; Kanost, M.R.; Gehrke, S.H.
Mechanical properties of the beetle elytron, a biological composite material
Biomacromolecules
12
321-335
2011
Tribolium castaneum
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de Villiers, J.; Koekemoer, L.; Strauss, E.
3-Fluoroaspartate and pyruvoyl-dependant aspartate decarboxylase: exploiting the unique characteristics of fluorine to probe reactivity and binding
Chemistry
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10030-10041
2010
Escherichia coli, Mycobacterium tuberculosis
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Webb, M.; Yorke, B.; Kershaw, T.; Lovelock, S.; Lobley, C.; Kilkenny, M.; Smith, A.; Blundell, T.; Pearson, A.; Abell, C.
Threonine 57 is required for the post-translational activation of Escherichia coli aspartate alpha-decarboxylase
Acta Crystallogr. Sect. D
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Escherichia coli (P0A790)
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Webb, M.E.; Lobley, C.M.; Soliman, F.; Kilkenny, M.L.; Smith, A.G.; Blundell, T.L.; Abell, C.
Structure of Escherichia coli aspartate alpha-decarboxylase Asn72Ala: probing the role of Asn72 in pyruvoyl cofactor formation
Acta Crystallogr. Sect. F
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Escherichia coli (P0A790)
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Monteiro, D.C.; Rugen, M.D.; Shepherd, D.; Nozaki, S.; Niki, H.; Webb, M.E.
Formation of a heterooctameric complex between aspartate alpha-decarboxylase and its cognate activating factor, PanZ, is CoA-dependent
Biochem. Biophys. Res. Commun.
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Escherichia coli
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Cui, W.; Shi, Z.; Fang, Y.; Zhou, L.; Ding, N.; Zhou, Z.
Significance of Arg3, Arg54, and Tyr58 of L-aspartate alpha-decarboxylase from Corynebacterium glutamicum in the process of self-cleavage
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Corynebacterium glutamicum (Q9X4N0), Corynebacterium glutamicum ATCC 13032 (Q9X4N0)
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Synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum
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Corynebacterium glutamicum (Q9X4N0), Corynebacterium glutamicum ATCC 13032 (Q9X4N0)
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Liu, P.; Ding, H.; Christensen, B.M.; Li, J.
Cysteine sulfinic acid decarboxylase activity of Aedes aegypti aspartate 1-decarboxylase: the structural basis of its substrate selectivity
Insect Biochem. Mol. Biol.
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Aedes aegypti, Drosophila melanogaster
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beta-Alanine biosynthesis in Methanocaldococcus jannaschii
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Methanocaldococcus jannaschii (Q60358), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q60358)
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Stuecker, T.; Tucker, A.; Escalante-Semerena, J.
PanM, an acetyl-coenzyme a sensor required for maturation of L-aspartate decarboxylase (PanD)
mBio
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Salmonella enterica, Salmonella enterica DM10310
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Nozaki, S.; Webb, M.E.; Niki, H.
An activator for pyruvoyl-dependent l-aspartate alpha-decarboxylase is conserved in a small group of the gamma-proteobacteria including Escherichia coli
MicrobiologyOpen
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298-310
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Escherichia coli, Escherichia coli MG1655
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Stuecker, T.N.; Hodge, K.M.; Escalante-Semerena, J.C.
The missing link in coenzyme A biosynthesis: PanM (formerly YhhK), a yeast GCN5 acetyltransferase homologue triggers aspartate decarboxylase (PanD) maturation in Salmonella enterica
Mol. Microbiol.
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Corynebacterium glutamicum, Salmonella enterica
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Sharma, R.; Kothapalli, R.; Van Dongen, A.M.; Swaminathan, K.
Chemoinformatic identification of novel inhibitors against Mycobacterium tuberculosis L-aspartate alpha-decarboxylase
PLoS ONE
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Mycobacterium tuberculosis
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Sharma, R.; Florea, M.; Nau, W.M.; Swaminathan, K.
Validation of drug-like inhibitors against Mycobacterium tuberculosis L-aspartate alpha-decarboxylase using nuclear magnetic resonance (1H NMR)
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Mycobacterium tuberculosis
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Lee, E.; Kim, H.; Kim, D.; Kim, Y.; Nam, S.; Kim, B.; Jeon, S.
Gene expression and characterization of thermostable glutamate decarboxylase from Pyrococcus furiosus
Biotechnol. Bioprocess Eng.
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375-381
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Pyrococcus furiosus (Q8U1P6)
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Gopal, P.; Tasneen, R.; Yee, M.; Lanoix, J.; Sarathy, J.; Rasic, G.; Li, L.; Dartois, V.; Nuermberger, E.; Dick, T.
In vivo-selected pyrazinoic acid-resistant Mycobacterium tuberculosis strains harbor missense mutations in the aspartate decarboxylase PanD and the unfoldase ClpC1
ACS Infect. Dis.
3
492-501
2017
Mycobacterium tuberculosis
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Pei, W.; Zhang, J.; Deng, S.; Tigu, F.; Li, Y.; Li, Q.; Cai, Z.; Li, Y.
Molecular engineering of L-aspartate-alpha-decarboxylase for improved activity and catalytic stability
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101
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Escherichia coli (P0A790), Bacillus subtilis (P52999), Corynebacterium glutamicum (Q9X4N0), Bacillus subtilis 168 (P52999), Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 (Q9X4N0), Escherichia coli K-12 / DH5alpha (P0A790)
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Arnott, Z.L.P.; Nozaki, S.; Monteiro, D.C.F.; Morgan, H.E.; Pearson, A.R.; Niki, H.; Webb, M.E.
The mechanism of regulation of pantothenate biosynthesis by the PanD-PanZ-AcCoA complex reveals an additional mode of action for the antimetabolite N-pentyl pantothenamide (N5-Pan)
Biochemistry
56
4931-4939
2017
Escherichia coli
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Shen, Y.; Zhao, L.; Li, Y.; Zhang, L.; Shi, G.
Synthesis of beta-alanine from L-aspartate using L-aspartate-alpha-decarboxylase from Corynebacterium glutamicum
Biotechnol. Lett.
36
1681-1686
2014
Corynebacterium glutamicum (Q9X4N0), Corynebacterium glutamicum ATCC 13032 (Q9X4N0)
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Stuecker, T.N.; Bramhacharya, S.; Hodge-Hanson, K.M.; Suen, G.; Escalante-Semerena, J.C.
Phylogenetic and amino acid conservation analyses of bacterial L-aspartate-alpha-decarboxylase and of its zymogen-maturation protein reveal a putative interaction domain
BMC Res. Notes
8
354
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Halalkalibacterium halodurans, Legionella pneumophila, Klebsiella pneumoniae (A6T4S8), Helicobacter pylori (P56065), Salmonella enterica subsp. enterica serovar Typhimurium (P65662), Moorella thermoacetica (Q2RM59), Magnetospirillum magneticum (Q2VZZ9), Neisseria gonorrhoeae (Q5F8Y9), Bordetella pertussis (Q7VXF8), Ralstonia solanacearum (Q8XVU6), Pseudomonas aeruginosa (Q9HV68), Corynebacterium glutamicum (Q9X4N0), Neisseria gonorrhoeae ATCC 700825 / FA 1090 (Q5F8Y9), Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 (Q9X4N0), Magnetospirillum magneticum AMB-1 / ATCC 700264 (Q2VZZ9), Helicobacter pylori 26695 (P56065), Pseudomonas aeruginosa ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 (Q9HV68), Salmonella enterica subsp. enterica serovar Typhimurium LT2 / SGSC1412 / ATCC 700720 (P65662), Halalkalibacterium halodurans ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125, Klebsiella pneumoniae ATCC 700721 / MGH 78578 (A6T4S8), Moorella thermoacetica ATCC 39073 / JCM 9320 (Q2RM59), Bordetella pertussis Tohama I / ATCC BAA-589 / NCTC 13251 (Q7VXF8)
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Monteiro, D.C.F.; Patel, V.; Bartlett, C.P.; Nozaki, S.; Grant, T.D.; Gowdy, J.A.; Thompson, G.S.; Kalverda, A.P.; Snell, E.H.; Niki, H.; Pearson, A.R.; Webb, M.E.
The structure of the PanD/PanZ protein complex reveals negative feedback regulation of pantothenate biosynthesis by coenzyme A
Chem. Biol.
22
492-503
2015
Escherichia coli
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Deng, S.; Zhang, J.; Cai, Z.; Li, Y.
Characterization of L-aspartate-alpha-decarboxylase from Bacillus subtilis
Chin. J. Biotechnol.
31
1184-1193
2015
Escherichia coli (P0A790), Bacillus subtilis (P52999), Corynebacterium glutamicum (Q9X4N0), Bacillus subtilis 168 (P52999), Corynebacterium glutamicum DSM 20300 (Q9X4N0)
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Gliessman, J.R.; Kremer, T.A.; Sangani, A.A.; Jones-Burrage, S.E.; McKinlay, J.B.
Pantothenate auxotrophy in Zymomonas mobilis ZM4 is due to a lack of aspartate decarboxylase activity
FEMS Microbiol. Lett.
364
fnx113
2017
no activity in Zymomonas mobilis, Escherichia coli (P0A790), Escherichia coli, no activity in Zymomonas mobilis ZM4 / ATCC 31821 / CP4
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Tomita, H.; Yokooji, Y.; Ishibashi, T.; Imanaka, T.; Atomi, H.
An archaeal glutamate decarboxylase homolog functions as an aspartate decarboxylase and is involved in beta-alanine and coenzyme A biosynthesis
J. Bacteriol.
196
1222-1230
2014
Thermococcus kodakarensis (Q5JJ82), Thermococcus kodakarensis, Thermococcus kodakarensis ATCC BAA-918 / JCM 12380 / KOD1 (Q5JJ82)
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Zhang, T.; Zhang, R.; Xu, M.; Zhang, X.; Yang, T.; Liu, F.; Yang, S.; Rao, Z.
Glu56Ser mutation improves the enzymatic activity and catalytic stability of Bacillus subtilis L-aspartate alpha-decarboxylase for an efficient beta-alanine production
Process Biochem.
70
117-123
2018
Escherichia coli (P0A790), Bacillus subtilis (P52999), Lactiplantibacillus plantarum (Q88Z02), Corynebacterium glutamicum (Q9X4N0), Bacillus subtilis 168 (P52999), Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 (Q9X4N0), Lactiplantibacillus plantarum ATCC BAA-793 / NCIMB 8826 / WCFS1 (Q88Z02)
-
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Dai, F.; Qiao, L.; Cao, C.; Liu, X.; Tong, X.; He, S.; Hu, H.; Zhang, L.; Wu, S.; Tan, D.; Xiang, Z.; Lu, C.
Aspartate decarboxylase is required for a normal pupa pigmentation pattern in the silkworm, Bombyx mori
Sci. Rep.
5
10885
2015
Bombyx mori (H9JRC8), Bombyx mori
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