Abstract
Abstract Bacillus subtilis PhoD is an extracytoplasmic alkaline phosphodiesterase that liberates phosphate from organic compounds. PhoD active site contains one Fe 3+ ion and two Ca 2+ ions. Structurally, PhoD is similar to the metallophosphatase family of eukaryotic purple acid phosphatases (PAPs). PAPs have two metal ions at their active site, Fe 3+ and M 2 + of variable identity. M 2 + is frequently an Fe or Zn. As in the PAPs, the Fe 3+ ion in PhoD is coordinated to a tyrosine. However, PhoD has a Ca 2+ at the M 2 + site, and a second supporting Ca 2+ . PhoD also exhibits a C‐terminal α‐helix, which buries the active site. It is probable that the C‐terminal α‐helix has a regulatory role in PhoD activity.
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