Structural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes.

The crystallographic structures of both the vanadium chloroperoxidase and bromoperoxidase enzymes have been determined with either vanadium or phosphate bound at their active site. The amino acids that are involved in phosphate binding in the acid phosphatase enzymes and those that are coordinated to vanadium in the haloperoxidases appear to be conserved between the two classes of enzyme. The detailed active site architecture for enzymes that recognize and use either vanadium or phosphate will be discussed in relation to their proposed enzymatic mechanism. Copyright 2002 John Wiley & Sons, Ltd.