EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    4.1.1.11 | more |
(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 |
? |
- |
? |
| 4.1.1.11 | more |
(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 |
? |
- |
? |
| 4.1.1.11 | more |
large-scale enzymatic production of beta-alanine from L-aspartate by pH-stat directed, fed-batch-feeding strategy, method development and evaluation, overview |
Corynebacterium glutamicum |
? |
- |
? |
| 4.1.1.11 | more |
the enzyme also shows cysteine sulfinic acid decarboxylase activity, EC 4.1.1.29, catalyzing the decarboxylation of cysteine sulfinic acid and cysteic acid |
Drosophila melanogaster |
? |
- |
? |
| 4.1.1.11 | more |
the enzyme also shows cysteine sulfinic acid decarboxylase activity, EC 4.1.1.29, catalyzing the decarboxylation of cysteine sulfinic acid and cysteic acid. Homology modeling of AeADC and substrate docking suggest that residue Q377, localized at the active site of AeADC, could better interact with aspartate through hydrogen bonding, which may play a role in aspartate selectivity |
Aedes aegypti |
? |
- |
? |
| 4.1.1.11 | more |
the enzyme performs self-cleavage for catalytic activition |
Corynebacterium glutamicum |
? |
- |
? |
| 4.1.1.11 | more |
the enzyme is 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 |
Thermococcus kodakarensis |
? |
- |
? |
| 4.1.1.11 | more |
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection |
Corynebacterium glutamicum |
? |
- |
? |
| 4.1.1.11 | more |
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection |
Escherichia coli |
? |
- |
? |
| 4.1.1.11 | more |
fluorometric method for beta-alanine determination, development of a high-throughput screening method for beta-alanine detection |
Bacillus subtilis |
? |
- |
? |
