EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.11 | panD gene, overexpression in Corynebacterium glutamicum with 4fold increased enzyme activity and in Escherichia coli with 3fold increased enzyme activity | Escherichia coli |
4.1.1.11 | panD gene, sequencing, overexpression in Corynebacterium glutamicum with 288fold increased enzyme activity and in Escherichia coli with 41fold increased enzyme activity | Corynebacterium glutamicum |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.1.11 | - |
Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.11 | additional information | panD insertion mutant ND2 completely lacks enzyme activity and exhibits beta-alanine auxotrophy | Corynebacterium glutamicum |
4.1.1.11 | additional information | panD mutants | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.1.1.11 | 14100 | - |
x * 14100, pi-protein, calculated from the amino acid sequence | Corynebacterium glutamicum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.11 | L-aspartate | Corynebacterium glutamicum | essential for beta-alanine synthesis, involved in pantothenate biosynthesis | beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | Escherichia coli | involved in pantothenate biosynthesis | beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | Escherichia coli MG1655 | involved in pantothenate biosynthesis | beta-alanine + CO2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.11 | Corynebacterium glutamicum | Q9X4N0 | strain ATCC 13032 | - |
4.1.1.11 | Escherichia coli | P0A790 | - |
- |
4.1.1.11 | Escherichia coli MG1655 | P0A790 | - |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
4.1.1.11 | proteolytic modification | panD is initially translated as inactive precursor pi-protein which is slowly proteolytically cleaved at a specific Gly-Ser bond producing two dissimilar subunits, autocatalytic mechanism | Escherichia coli |
4.1.1.11 | proteolytic modification | the panD gene product is efficiently proteolytically processed into two subunits, an 11 kDa alpha-subunit and a 2.7 kDa beta-subunit, Gly-24/Ser-25 may be the processing site of the initially translated pi-protein | Corynebacterium glutamicum |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.1.1.11 | additional information | - |
- |
Corynebacterium glutamicum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.11 | L-aspartate | - |
Corynebacterium glutamicum | beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | alpha-decarboxylation | Escherichia coli | beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | essential for beta-alanine synthesis, involved in pantothenate biosynthesis | Corynebacterium glutamicum | beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | involved in pantothenate biosynthesis | Escherichia coli | beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | alpha-decarboxylation | Escherichia coli MG1655 | beta-alanine + CO2 | - |
? | |
4.1.1.11 | L-aspartate | involved in pantothenate biosynthesis | Escherichia coli MG1655 | beta-alanine + CO2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.11 | ? | x * 14100, pi-protein, calculated from the amino acid sequence | Corynebacterium glutamicum |
4.1.1.11 | tetramer | active enzyme is a tetramer composed of three alpha- and beta-subunits and an incompletely processed pi-protein | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.11 | PanD | - |
Corynebacterium glutamicum |
4.1.1.11 | PanD | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
4.1.1.11 | 37 | - |
assay at | Corynebacterium glutamicum |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.11 | additional information | requires pyruvate as a covalently bound, catalytically active prosthetic group, pyruvoyl-dependent enzyme, the pyruvoyl group is generated at a specific internal serine residue of the inactive pi-protein with the coincident cleavage of the Gly-Ser bond | Escherichia coli |