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Information on EC 4.1.1.11 - aspartate 1-decarboxylase and Organism(s) Escherichia coli and UniProt Accession P0A790
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4.1.1.11 aspartate 1-decarboxylaseIUBMB Comments
The Escherichia coli enzyme contains a pyruvoyl group.
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Word Map
- 4.1.1.11
- pantothenate
- pyrazinamide
-
pyrazinoic
-
self-processing
-
pza-resistant
- synthesis
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aspartate decarboxylase, adcbs, aspartate 1-decarboxylase, l-aspartate-alpha-decarboxylase, aspartate-alpha-decarboxylase, tk1814, bmadc, mj0050, mtbadc, aspdc, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aspartate alpha-decarboxylase
Aspartic alpha-decarboxylase
-
-
-
-
L-Aspartate alpha-decarboxylase
-
-
-
-
L-Aspartate-alpha-decarboxylase
Aspartate alpha-decarboxylase
-
-
-
-
L-Aspartate-alpha-decarboxylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-
SYSTEMATIC NAME
IUBMB Comments
L-aspartate 1-carboxy-lyase (beta-alanine-forming)
The Escherichia coli enzyme contains a pyruvoyl group.
CAS REGISTRY NUMBER
COMMENTARY
9024-58-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate
beta-alanine + CO2
-
-
-
?
L-aspartate
beta-alanine + CO2
Thr-57 and a water molecule are probable catalytic residues able to support acid-base catalysis, enzyme structure
-
?
L-aspartate
beta-alanine + CO2
involved in pantothenate biosynthesis
-
?
L-aspartate
beta-alanine + CO2
major route of beta-alanine production essential for the biosynthesis of pantothenate
-
?
L-aspartate
beta-alanine + CO2
-
reaction occurs with retention of configuration, Tyr58 acts as proton donor in the decarboxylation mechanism, the active sites are between subunits, mechanism involves formation of an imine between the amino group of aspartate and an integral pyruvoyl group formed by an autocatalytic posttranslational modification
-
?
L-aspartate
beta-alanine + CO2
-
involved in the biosynthesis of pantothenate
-
?
additional information
?
-
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection
-
-
?
additional information
?
-
-
(2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid can act as substrates of ADC enzymes for single turnover, but not catalytic, reactions
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-aspartate
beta-alanine + CO2
-
-
-
?
L-aspartate
beta-alanine + CO2
involved in pantothenate biosynthesis
-
?
L-aspartate
beta-alanine + CO2
major route of beta-alanine production essential for the biosynthesis of pantothenate
-
?
L-aspartate
beta-alanine + CO2
-
involved in the biosynthesis of pantothenate
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyruvoyl cofactor
dependent on. Pathway for the formation of the pyruvoyl-dependent cofactor in ADC: the beta-hydroxyl of Ser25 attacks the carbonyl of the previous amino-acid residue (i) to form an oxyoxazolidine intermediate, which decomposes (ii) to form an ester intermediate. E1cB elimination (iii) forms a N-terminal dehydroalanyl residue which is hydrolysed (iv) to form the pyruvoyl cofactor (the alpha'-chain). The ester intermediate can also be hydrolysed to yield the inactive alpha'-chain
pyruvoyl cofactor
-
dependent on, the enzyme contains a covalently-bound pyruvoyl cofactor
additional information
requires pyruvate as a covalently bound, catalytically active prosthetic group, pyruvoyl-dependent enzyme, the pyruvoyl group is generated at a specific internal serine residue of the inactive pi-protein with the coincident cleavage of the Gly-Ser bond
-
additional information
-
requires pyruvate as a covalently bound, catalytically active prosthetic group, pyruvoyl-dependent enzyme, the pyruvoyl group is generated at a specific internal serine residue of the inactive pi-protein with the coincident cleavage of the Gly-Ser bond
-
additional information
the translated inactive proenzyme, pi-enzyme, self-processes to create its own covalently bound prosthetic group, a pyruvoyl cofactor, mechanism
-
additional information
the enzyme requires PanZ, an activator involved in the cleavage of ADCE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
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CoA-dependent interaction of PanZ and PanD. Growth inhibition is due to the CoA-dependent PanD-PanZ interaction and the inhibition occurs at native concentrations of PanD and PanZ in the cell. The production of beta-alanine is feedback-regulated by the PanZ-AcCoA complex
CoA
-
the CoA-dependent interaction inhibits catalysis by the activated enzyme. Binding of acetyl-CoA to PanZ is required to form the PanZ/PanD interface. PanZ.AcCoA inhibits the activated enzyme regulating pantothenate biosynthesis. The binding site for AcCoA is very close to the protein-protein interface. Structure of the complex of PanD and its activating factor PanZ with bound CoA, overview
PanZ
-
structure of the complex of PanD and its activating factor PanZ, overview. Binding of acetyl-CoA to PanZ is required to form the PanZ/PanD interface. PanZ-AcCoA activates PanD via selection of a reactive conformation of PanD. PanZ is essential for activation of the zymogen PanD to form the mature enzyme in vivo, and its deletion leads to beta-alanine auxotrophy. NMR spectroscopy dmonstrates that CoA is an absolute requirement for PanD-PanZ complex formation. PanZ inhibits catalytic activity by activated PanD
-
pentyl pantothenamide
-
high-potency growth inhibition by pentyl pantothenamide is dependent upon the PanD-PanZ interaction. Substitution of the Escherichia coli panD for the noninteracting Bacillus panD leads to resistance against the inhibitor
additional information
-
not inhibited by (2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PanZ
the enzyme requires activation by PanZ to be posttranslationally cleaved
-
CoA
-
NMR spectroscopy demonstrates that CoA is an absolute requirement for PanD-PanZ complex formation, the binding site for AcCoA is very close to the protein-protein interface. PanZ promotes the activation of the zymogen of PanD to form aspartate alpha-decarboxylase (ADC) in a CoA-dependent manner
additional information
role for Thr57 in the activation of the enzyme, while neither Tyr58 nor Tyr22 is required for the activation reaction, overview
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PanZ
-
analysis of the protein complex between Escherichia coli PanD and PanZ in vitro using isothermal titration calorimetry and mass spectrometry and thereby determine the stoichiometry and affinity of the components of this protein complex, high affinity 4:4 heterooctameric complex, overview. Non-covalent interaction between the acetyl group of acetyl-CoA and the PanD zymogen may be required to induce activation
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PanZ
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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. Gene panZ is conserved only in Escherichia coli-related enterobacterial species including Shigella, Salmonella, Klebsiella and Yersinia
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PanZ
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structure of the complex of PanD and its activating factor PanZ, overview. Binding of AcCoA to PanZ is required to form the PanZ/PanD interface. PanZ-AcCoA activates PanD via selection of a reactive conformation of PanD. PanZ is essential for activation of the zymogen PanD to form the mature enzyme in vivo, and its deletion leads to beta-alanine auxotrophy. NMR spectroscopy demonstrates that CoA is an absolute requirement for PanD-PanZ complex formation. PanZ inhibits catalytic activity by activated PanD. Structural basis for activation, overview
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PanZ
-
the Escherichia coli enzyme requires the regulatroy factor PanZ for proteolytic cleavage of the zymogen to form the mature enzyme, the PanZ mutant N45A is unable to complement a panZ deletion strain. 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
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Pyruvoyl group
-
1 mol of pyruvate is covalently bound per mol of enzyme
Pyruvoyl group
-
catalytic pyruvoyl groups at three active sites and an ester at the fourth. The ester is an intermediate in the autocatalytic self-processing leading to formation of the pyruvoyl group
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, pathway overview
physiological function
evolution
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the enzyme is a member of the small class of pyruvoyl-dependent enzymes, which contain a covalently-bound pyruvoyl cofactor
malfunction
metabolism
physiological function
additional information
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
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
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
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
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
malfunction
-
protein PanZ is essential for activation of the zymogen PanD to form ADC in vivo, and its deletion leads to beta-alanine auxotrophy
metabolism
-
the enzyme catalyzes the first step in the biosynthetic pathway of pantothenate and coenzyme A, 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 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
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 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
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
-
regulatory mechanisms for PanD activation and inactivation in vivo, overview
additional information
-
PanD-PanZ complex three-dimensional structure analysis, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14000
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
11000
-
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine
13800
13800
-
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE
tetramer
tetramer
tetramer
active enzyme is a tetramer composed of three alpha- and beta-subunits and an incompletely processed pi-protein
tetramer
the bacterial ADC is a tetramer containing approximately 120 amino acids in each subunit
tetramer
-
crystallographic data. Tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits
tetramer
-
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
additional information
-
the Escherichia coli enzyme requires the regulatroy factor PanZ for proteolytic cleavage of the zymogen to form the mature enzyme
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
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
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
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
-
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 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
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of an unprocessed native proenzyme and of the mutants G24S, S25A, S25C, S25T, H11A, Ala-24 and Ala-26 insertion mutants, hanging-drop vapour-diffusion method
purified recombinant mutant N72A, hanging drop vapour diffusion method, mixing of 0.001 ml of 19 mg /ml protein in 50 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.6 M ammonium sulfate, pH 4.0, and equilibration against 0.5 ml of reservoir solution, 19°C, 3 days, cryoprotection by 1.8 M ammonium sulfate, 0.1 M citric acid, 30% glycerol pH 4.0 using 5% increments in glycerol concentration to prevent crystal dissolution, X-ray diffraction structure determination and analysis at 1.7 A resolution
purified recombinant T57V mutant enzyme, hanging drops by vapour diffusion with a 1:1 ratio of protein to precipitant, 7.5 mg/ml protein, 1.5-3.4 M sodium malonate, pH 4.0, method optimization, 17°C, X-ray diffraction structure determination and analysis at 1.62 A resolution, modeling
co-crystallization of fully activated PanD and PanZ in complex, in a 10:11 PanD:PanZ ratio (protomer to monomer), hanging drop vapor diffusion method, mixing of 0.003 ml of 9 mg/ml protein in 50 mM Tris, 100 mM NaCl, and 0.1 mM DTT, pH 7.5, with 00.001 ml of reservoir solution containing 200 mM KSCN, 100 mM Bis-Tris propane, pH 6.5, and 20% w/v PEG 3350 at 18°C, X-ray diffraction structure determination and analysis at 1.16 A resolution. The same structure is observed using both room-temperature and cryo-cooled crystals, indicating that the hydrate is formed from the pyruvoyl cofactor and is not an intermediate in the activation reaction. This state is stabilized by a hydrogen bond to the amide of Gly24, which is held in place by interactions with PanZ
-
purified recombinant protein complex PanD-PanZ-AcCoA, protein complexes are prepared with a 10:11 ratio of PanD to PanZ at a total protein concentration of 9-11 mg/ml, and a 2fold molar excess (with respect to PanZ) of acetyl-CoA. Crystals are obtained in 20% w/v PEG 3350, 0.1 M Bis-Tris propane, pH 7.4, and 0.2 M potassium thiocyanate, X-ray diffraction structure determination and analysis at 1.6 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I60A
site-directed mutagenesis, the PanD activation activity is affected
I86A
site-directed mutagenesis, the PanD activation activity is affected
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
S70A
site-directed mutagenesis, the PanD activation activity is affected
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
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
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
T57V
additional information
additional information
inactive Ala-24 and Ala-26 insertion mutants, study of the structure and processing activity
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
thermotolerance of transgenic tobacco plants expressing the enzyme, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme mutant N72A from Escherichia coli strain C41 (DE3) to homogeneity
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 90% purity
recombinant His-tagged enzyme mutant T57V and PanZ from Escherichia coli strain DELTApanD DELTApanZ (DE3) by nickel affinity chromatography and gel filtration
-
recombinant nontagged enzyme in Escherichia coli panZ-deficient strain SN227 by ultrafiltration, ammonium sulfate fractionation, dialysis, and anionexchange chromatography, recombinant His-tagged wild-type and mutant enzymes and flag3-tagged enzyme from Escherichia coli strain MG1655 by affinity chromatography and dialysis
-
recombinant wild-type and mutant enzymes from Escherichia coli strain C41(DE3) by sequential immobilized metal affinity chromatography and gel filtration
-
recomnbinant enzyme from strain BL21(DE3) by anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene panD, expression of enzyme mutant N72A in Escherichia coli strain C41 (DE3)
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, 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
panD gene, overexpression in Corynebacterium glutamicum with 4fold increased enzyme activity and in Escherichia coli with 3fold increased enzyme activity
gene panD, expression of His-tagged enzyme mutant T57V and PanZ in Escherichia coli strain DELTApanD DELTApanZ (DE3)
-
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
-
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
the enzyme is used for industrial production of beta-alanine from L-aspartate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Williamson, J.M.
L-Aspartate alpha-decarboxylase
Methods Enzymol.
113
589-595
1985
Escherichia coli, Escherichia coli B / ATCC 11303
Williamson, J.M.; Brown, G.M.
Purification and properties of L-aspartate-alpha-decarboxylase, an enzyme that catalyzes the formation of beta-alanine in Escherichia coli
J. Biol. Chem.
254
8074-8082
1979
Escherichia coli, Escherichia coli B / ATCC 11303
Albert, A.; Dhanaraj, V.; Genschel, U.; Khan, G.; Ramjee, M.K.; Pulido, R.; Sibanda, B.L.; von Delft, F.; Witty, M.; Blundell, T.L.; Smith, A.G.; Abell, C.
Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing
Nat. Struct. Biol.
5
289-293
1998
Escherichia coli
Ramjee, M.K.; Genschel, U.; Abell, C.; Smith, A.G.
Escherichia coli L-aspartate alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry
Biochem. J.
323
661-669
1997
Escherichia coli
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
Appl. Environ. Microbiol.
65
1530-1539
1999
Corynebacterium glutamicum (Q9X4N0), Corynebacterium glutamicum, Escherichia coli (P0A790), Escherichia coli, Escherichia coli MG1655 (P0A790)
Saldanha, S.A.; Birch, L.M.; Webb, M.E.; Nabbs, B.K.; von Delft, F.; Smith, A.G.; Abell, C.
Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction
Chem. Commun. (Camb.)
2001
1760-1761
2001
Escherichia coli
-
Schmitzberger, F.; Kilkenny, M.L.; Lobley, C.M.C.; Webb, M.E.; Vinkovic, M.; Matak-Vinkovic, D.; Witty, M.; Chirgadze, D.Y.; Smith, A.G.; Abell, C.; Blundell, T.L.
Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase
EMBO J.
22
6193-6204
2003
Escherichia coli (P0A790)
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.
60
495-505
2006
Escherichia coli
Fouad, W.M.; Altpeter, F.
Transplastomic expression of bacterial L-aspartate-alpha-decarboxylase enhances photosynthesis and biomass production in response to high temperature stress
Transgenic Res.
18
707-718
2009
Escherichia coli
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
16
10030-10041
2010
Escherichia coli, Mycobacterium tuberculosis
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
70
1166-1172
2014
Escherichia coli (P0A790)
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
68
414-417
2012
Escherichia coli (P0A790)
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.
426
350-355
2012
Escherichia coli
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
1
298-310
2012
Escherichia coli, Escherichia coli MG1655
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
Appl. Microbiol. Biotechnol.
101
6015-6021
2017
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)
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
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
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)
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
Escherichia coli (P0A790), Escherichia coli, no activity in Zymomonas mobilis, no activity in Zymomonas mobilis ZM4 / ATCC 31821 / CP4
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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