EC Number |
Title |
Organism |
---|
2.6.1.52 | Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria |
Bos taurus |
2.6.1.52 | Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria |
Escherichia coli |
2.6.1.52 | Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria |
Glycine max |
2.6.1.52 | Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria |
Niallia circulans |
2.6.1.52 | Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria |
Alkalihalobacillus alcalophilus |
2.6.1.52 | Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria |
Tetradesmus obliquus |
2.6.1.52 | Comparison of kinetic and enzymatic properties of intracellular phosphoserine aminotransferases from alkaliphilic and neutralophilic bacteria |
Ovis aries |
2.6.1.52 | Engineering of phosphoserine aminotransferase increases the conversion of L-homoserine to 4-hydroxy-2-ketobutyrate in a glycerol-independent pathway of 1,3-propanediol production from glucose |
Escherichia coli |
2.6.1.52 | Engineering of phosphoserine aminotransferase increases the conversion of L-homoserine to 4-hydroxy-2-ketobutyrate in a glycerol-independent pathway of 1,3-propanediol production from glucose |
Escherichia coli MG1655 |
2.6.1.52 | Glutamine-utilizing transaminases are a metabolic vulnerability of TAZ/YAP-activated cancer cells |
Homo sapiens |