Literature summary extracted from
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 (2001), Chem. Commun. (Camb.), 2001, 1760-1761.
No PubMed abstract available
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.1.1.11 |
panD gene overexpression |
Escherichia coli |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.1.1.11 |
- |
Escherichia coli |
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
4.1.1.11 |
14000 |
- |
4 * 14000 |
Escherichia coli |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.1.1.11 |
L-aspartate |
Escherichia coli |
involved in the biosynthesis of pantothenate |
beta-alanine + CO2 |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.1.11 |
Escherichia coli |
- |
- |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
4.1.1.11 |
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 |
Escherichia coli |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.1.1.11 |
recombinant enzyme |
Escherichia coli |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
4.1.1.11 |
L-aspartate = beta-alanine + CO2 |
detailed catalytic mechanism |
Escherichia coli |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.1.1.11 |
L-aspartate |
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 |
Escherichia coli |
beta-alanine + CO2 |
- |
? |
|
4.1.1.11 |
L-aspartate |
involved in the biosynthesis of pantothenate |
Escherichia coli |
beta-alanine + CO2 |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.1.1.11 |
tetramer |
4 * 14000 |
Escherichia coli |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.1.1.11 |
ADC |
- |
Escherichia coli |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
4.1.1.11 |
25 |
- |
assay at |
Escherichia coli |