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Literature summary for 4.1.1.11 extracted from

  • 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 (2010), Chemistry, 16, 10030-10041.
    View publication on PubMed
Search for more literature for 4.1.1.11

Activating Compound

Activating Compound Comment Organism Structure
Pyruvoyl group
-
 Escherichia coli
Pyruvoyl group
-
 Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
2-(difluoromethyl)-L-aspartic acid
-
 Escherichia coli
2-(difluoromethyl)-L-aspartic acid
-
 Mycobacterium tuberculosis
additional information not inhibited by (2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid Escherichia coli
additional information not inhibited by (2R,3R)-3-fluoroaspartic acid and (2R,3S)-3-fluoroaspartic acid Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate
-
 Escherichia coli beta-alanine + CO2
-
 ?
L-aspartate
-
 Mycobacterium tuberculosis beta-alanine + CO2
-
 ?
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 Escherichia coli ?
-
 ?
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 Mycobacterium tuberculosis ?
-
 ?

Synonyms

Synonyms Comment Organism
ACD
-
 Escherichia coli
ACD
-
 Mycobacterium tuberculosis