Cloned (Comment) | Organism |
---|---|
- |
Aeropyrum pernix |
Crystallization (Comment) | Organism |
---|---|
structures of the enzyme without acetate, the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-phosphoserine, and the complex formed by the K127A mutant with the external Schiff base of pyridoxal 5'-phosphate with O-acetylserine, to 2.1 A resolution. No significant difference is seen in the overall structure between the free and complexed forms of the enzyme. The side chains of T152, S153, and Q224 interact with the carboxylate of the substrate. The position of R297 is significantly unchanged in the complex of the K127A mutant with the external Schiff base, allowing enough space for an interaction with O-phosphoserine. The positively charged environment around the entrance of the active site including S153 and R297 is important for accepting negatively charged substrates | Aeropyrum pernix |
Protein Variants | Comment | Organism |
---|---|---|
K127A | mutant is inactive for cysteine synthesis and does not form the alpha-aminoacrylate intermediate | Aeropyrum pernix |
Q224A | 0.04% of wild-type activity | Aeropyrum pernix |
R297A | 0.3% of wild-type activity | Aeropyrum pernix |
R297E | 11% of wild-type activity | Aeropyrum pernix |
R297K | 0.2% of wild-type activity | Aeropyrum pernix |
S153A | 0.4% of wild-type activity | Aeropyrum pernix |
S153T | 0.2% of wild-type activity | Aeropyrum pernix |
T152A | 0.2% of wild-type activity | Aeropyrum pernix |
T152S | 71% of wild-type activity | Aeropyrum pernix |
T203A | 36% of wild-type activity | Aeropyrum pernix |
T203M | 0.3% of wild-type activity | Aeropyrum pernix |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | Q9YBL2 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
23 | - |
pH 7.5, 80°C | Aeropyrum pernix |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme also catalyzes the reaction of EC 2.5.1.47, cysteine synthase | Aeropyrum pernix | ? | - |
? | |
O-phospho-L-serine + hydrogen sulfide | - |
Aeropyrum pernix | L-cysteine + phosphate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
OPSS | - |
Aeropyrum pernix |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | crystallization data | Aeropyrum pernix |