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Literature summary extracted from
- Crystal structure of the Schiff base intermediate prior to decarboxylation in the catalytic cycle of aspartate alpha-decarboxylase (2004), J. Mol. Biol., 340, 1-7.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.1.1.11 | both apo form and in complex with isoasparagine | Helicobacter pylori |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.1.11 | Helicobacter pylori | P56065 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 4.1.1.11 | 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 | Helicobacter pylori |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.1.1.11 | L-aspartate = beta-alanine + CO2 | in the apo structure, N-terminal Ser25 of alpha chain is converted to pyruvoyl group. Substrate analogue isoasparagine becomes covalently attached to the pyruvoyl group forming the Schiff base intermediate prior to decarboxylation | Helicobacter pylori |
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