Application | Comment | Organism |
---|---|---|
pharmacology | the enzyme has a considerable potential in biocatalysis for the stereospecific synthesis of various beta-hydroxy amino acids, which are valuable building blocks for the production of pharmaceuticals | Achromobacter xylosoxidans |
synthesis | the enzyme has a considerable potential in biocatalysis for the stereospecific synthesis of various beta-hydroxy amino acids, which are valuable building blocks for the production of pharmaceuticals | Achromobacter xylosoxidans |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli BL21 Star (DE3) cells | Achromobacter xylosoxidans |
Crystallization (Comment) | Organism |
---|---|
determination of the crystal structure at 1.5 A resolution | Achromobacter xylosoxidans |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | the role of the essential metal (manganese) ion is most likely to activate the beta-hydroxy group of the substrate for deprotonation by His193 | Achromobacter xylosoxidans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Achromobacter xylosoxidans | A0A0J9X243 | IFO 12669 | - |
Purification (Comment) | Organism |
---|---|
- |
Achromobacter xylosoxidans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-threonine | - |
Achromobacter xylosoxidans | glycine + acetaldehyde | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | pyridoxal 5'-phosphate dependent enzyme. The metal binding siteis close to the pyridoxal 5'-phosphate cofactor in the active site of the enzyme. Metal ion assisted pyridoxal 5'-phosphate-dependent mechanism | Achromobacter xylosoxidans |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme plays a major role in degradation of D-threonine | Achromobacter xylosoxidans |