4.1.1.11: aspartate 1-decarboxylase
This is an abbreviated version!
For detailed information about aspartate 1-decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.11
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4.1.1.11
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pantothenate
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pyrazinamide
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pyrazinoic
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self-processing
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pza-resistant
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synthesis
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drug development
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pharmacology
- 4.1.1.11
- pantothenate
- pyrazinamide
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pyrazinoic
-
self-processing
-
pza-resistant
- synthesis
- drug development
- pharmacology
Reaction
Synonyms
ACD, ADC, ADCBs, ADCC.g, ADCCg, ADCE, Aspartate alpha-decarboxylase, aspartate decarboxylase, aspartate-alpha-decarboxylase, Aspartic alpha-decarboxylase, AspDC, BmADC, BsADC, CgADC, Dgad2, GcADC, L-Aspartate alpha-decarboxylase, L-Aspartate-alpha-decarboxylase, MfnA, MJ0050, More, MtbADC, PanD, PF1159, PLP-dependent L-aspartate decarboxylase, pyruvoyl-dependent l-aspartate alpha-decarboxylase, TK1814
ECTree
4.1.1.11 aspartate 1-decarboxylaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 4.1.1.11 - aspartate 1-decarboxylase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
(2S,3R,4S,5S)-2,3,4,6-tetrahydroxy-5-mercaptohexanal
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ZINC03871163
(2S,3S,4R,5S)2,5bis(hydroxymethyl)tetrahydrofuran-2,3,4-triol
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ZINC03830875
(2S,3S,4S,5R)-2(hydroxymethyl) tetrahydro-2H-pyran-2,3,4,5-tetraol
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ZINC03830878
2,4-dihydroxypyrimidine-5-carboxylate
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ZINC00901606, moderate inhibition
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
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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
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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
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pentyl pantothenamide
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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
enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis
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additional information
enzyme ADC is also subject to mechanism-based inactivation, which has been reported for many other pyruvoyl-dependent. Mechanism-based inactivation only occurs during catalysis
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additional information
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not inhibited by (2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid
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additional information
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not inhibited by (2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid
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additional information
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potential inhibitor molecule docking using the enzyme's crystal structure, overview
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additional information
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no inhibition by D-serine, (4S)-1,3-thiazolidin-3-ium-4-carboxylate, alpha-D-arabinopyranose, and 1,2-dihydropyrazolo[3,4-d]pyrimidin-4-one
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