Cloned (Comment) | Organism |
---|---|
overexpression in Escherichia coli | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
crystal structure of an unprocessed native proenzyme and of the mutants G24S, S25A, S25C, S25T, H11A, Ala-24 and Ala-26 insertion mutants, hanging-drop vapour-diffusion method | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
G24S | study of the structure and processing activity | Escherichia coli |
H11A | study of the structure and processing activity | Escherichia coli |
additional information | inactive Ala-24 and Ala-26 insertion mutants, study of the structure and processing activity | Escherichia coli |
S25A | inactive mutant, study of the structure and processing activity | Escherichia coli |
S25C | study of the structure and processing activity | Escherichia coli |
S25T | inactive mutant, study of the structure and processing activity | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
14000 | - |
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | Escherichia coli | major route of beta-alanine production essential for the biosynthesis of pantothenate | beta-alanine + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A790 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | ADC, which is translated as inactive pro-protein, i.e. pi-protein, undergoes intramolecular self-cleavage at Gly-24/Ser-25 producing the alpha- and beta-subunit, molecular mechanism of self-processing, slow process | Escherichia coli |
Purification (Comment) | Organism |
---|---|
native pro-ADC and mutants | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | Thr-57 and a water molecule are probable catalytic residues able to support acid-base catalysis, enzyme structure | Escherichia coli | beta-alanine + CO2 | - |
? | |
L-aspartate | major route of beta-alanine production essential for the biosynthesis of pantothenate | Escherichia coli | beta-alanine + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
ADC | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the translated inactive proenzyme, pi-enzyme, self-processes to create its own covalently bound prosthetic group, a pyruvoyl cofactor, mechanism | Escherichia coli |