EC Number | Cloned (Comment) | Organism |
---|---|---|
4.1.1.12 | expressed in Escherichia coli BL21(DE3) cells | Pseudomonas sp. |
4.1.1.12 | expressed in Escherichia coli BL21(DE3) cells | Comamonas testosteroni |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.1.12 | hanging drop vapor diffusion method, using 15% (w/v) PEG4000 and 0.1 M lithium sulfate in 0.1 M Tris-HCl buffer (pH 7.4-8.5) | Comamonas testosteroni |
4.1.1.12 | hanging drop vapor diffusion method, using 40% (w/v) PEG400 and 0.1 M lithium sulfate in 0.1 M Tris-HCl buffer (pH 8.4) | Pseudomonas sp. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.1.12 | E84K/E88K | the mutant retains 13% activity compared to the wild type enzyme | Comamonas testosteroni |
4.1.1.12 | K17A | the mutant shows 131.2% activity compared to the wild type enzyme | Comamonas testosteroni |
4.1.1.12 | K315A | the mutant shows 36.7% activity compared to the wild type enzyme | Comamonas testosteroni |
4.1.1.12 | R37A | the mutant shows 10.4% activity compared to the wild type enzyme | Comamonas testosteroni |
4.1.1.12 | R425A | the mutant retains 2.5% activity compared to the wild type enzyme | Comamonas testosteroni |
4.1.1.12 | R487A | completely inactive mutant | Comamonas testosteroni |
4.1.1.12 | S67A/Y68A/M69A | the mutant retains less than 1% activity compared to the wild type enzyme | Comamonas testosteroni |
4.1.1.12 | S67E/Y68E/M69E | the mutations produce an inactive dimer | Comamonas testosteroni |
4.1.1.12 | S67R/Y68R/M69R | the mutations produce an inactive dimer | Comamonas testosteroni |
4.1.1.12 | Y134F | the mutant shows 40.3% activity compared to the wild type enzyme | Comamonas testosteroni |
4.1.1.12 | Y207F | the mutant shows 10.7% activity compared to the wild type enzyme | Comamonas testosteroni |
4.1.1.12 | Y441F | the mutant shows 40.8% activity compared to the wild type enzyme | Comamonas testosteroni |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.1.12 | Comamonas testosteroni | Q93QX0 | - |
- |
4.1.1.12 | Comamonas testosteroni CCRC 11585 | Q93QX0 | - |
- |
4.1.1.12 | Pseudomonas sp. | - |
strain ATCC 19121 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.1.12 | Ni-NTA column chromatography and HPLC gel filtration | Pseudomonas sp. |
4.1.1.12 | Ni-NTA column chromatography and HPLC gel filtration | Comamonas testosteroni |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.1.12 | L-Asp | - |
Pseudomonas sp. | L-Ala + CO2 | - |
? | |
4.1.1.12 | L-Asp | - |
Comamonas testosteroni | L-Ala + CO2 | - |
? | |
4.1.1.12 | L-Asp | - |
Comamonas testosteroni CCRC 11585 | L-Ala + CO2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.1.1.12 | homododecamer | x-ray crystallography | Pseudomonas sp. |
4.1.1.12 | homododecamer | x-ray crystallography | Comamonas testosteroni |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.1.1.12 | Asd | - |
Pseudomonas sp. |
4.1.1.12 | Asd | - |
Comamonas testosteroni |
4.1.1.12 | L-Aspartate beta-decarboxylase | - |
Pseudomonas sp. |
4.1.1.12 | L-Aspartate beta-decarboxylase | - |
Comamonas testosteroni |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.1.12 | 259 | - |
L-Asp | mutant enzyme Y134F, at pH 5.0 and 37°C | Comamonas testosteroni | |
4.1.1.12 | 270 | - |
L-Asp | mutant enzyme R37A, at pH 5.0 and 37°C | Comamonas testosteroni | |
4.1.1.12 | 273 | - |
L-Asp | mutant enzyme Y441F, at pH 5.0 and 37°C | Comamonas testosteroni | |
4.1.1.12 | 279 | - |
L-Asp | mutant enzyme K315A, at pH 5.0 and 37°C | Comamonas testosteroni | |
4.1.1.12 | 294 | - |
L-Asp | mutant enzyme Y207F, at pH 5.0 and 37°C | Comamonas testosteroni | |
4.1.1.12 | 311 | - |
L-Asp | mutant enzyme K17A, at pH 5.0 and 37°C | Comamonas testosteroni | |
4.1.1.12 | 442 | - |
L-Asp | wild type enzyme, at pH 5.0 and 37°C | Comamonas testosteroni |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
4.1.1.12 | pyridoxal 5'-phosphate | dependent on, pyridoxal 5'-phosphate is bound covalently to Lys315 in the active site | Pseudomonas sp. | |
4.1.1.12 | pyridoxal 5'-phosphate | dependent on, pyridoxal 5'-phosphate is bound covalently to Lys315 in the active site | Comamonas testosteroni |