Alkaline phosphatases (EC 126.96.36.199) occur widely in nature and are found in all three domains of life . The Escherichia coli PhoA enzyme has been extensively studied whereas PhoX family of alkaline phosphatases are only minimally characterised and show no sequence similarity to other phosphotransfer enzymes. Yong et al.  determined high-resolution crystal structures for native PhoX from Pseudomonas fluorescens  and for its complexes with phosphate , a nonhydrolysable ATP analogue adenosine-5′-[β,γ-methylene]triphosphate (AMP-PCP) , and the putative transition-state mimic vanadate . The active site contains two antiferromagnetically coupled ferric ions (Fe3+), three calcium ions (Ca2+), and an oxo group bridging one Ca2+ and two Fe3+ ions.
|Cartoon representation of P. fluorescens PhoX crystal structure.|
|The PhoX active site containing bound phosphate [1, Fig. 2c].|
|A model for the catalytic mechanism of PhoX [1, Fig. 3d].|
The transition state is indicated with the double dagger (‡) symbol.
- Millán, J.L. (2006) Alkaline Phosphatases: Structure, substrate specificity and functional relatedness to other members of a large superfamily of enzymes. Purinergic Signalling 2, 335–341.
- Yong, S.C., Roversi, P., Lillington, J., Rodriguez, F., Krehenbrink, M., Zeldin, O.B., Garman, E.F., Lea, S.M. and Berks, B.C. (2014) A complex iron-calcium cofactor catalyzing phosphotransfer chemistry. Science 345, 1170—1173.