Mutant organophosphorus acid anhydrolases and uses thereof
AssigneeThe United States of America as represented by the Secretary of the Army
InventorsMark A Guelta, Melissa M. Dixon, Steven P Harvey
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Abstract
Disclosed herein are non-wild-type organophosphorus acid anhydrolases having two site mutations, methods of production, and methods of use to effectively degrade toxic chemicals such as ((RS)-Propan-2-yl methylphosphonofluoridate) (Sarin) and other organophosphorus compounds.
Claims10
An isolated organophosphorous acid anhydrolase (OPAA) enzyme, wherein said anhydrolase consists of a non-wild-type amino acid at sequence positions 212 and 342 of SEQ ID NO:
- 1, and wherein Tyrosine (Y) is replaced by Phenylalanine (F) at position 212, and Valine (V) is replaced by Isoleucine (I) at position 342.
A method for degrading ((RS)-Propan-2-yl methylphosphonofluoridate) (Sarin), comprising contacting Sarin with an isolated organophosphorus acid anhydrolase enzyme, wherein said anhydrolase consists of a non-wild-type amino acid at sequence positions 212 and 342 of SEQ ID NO:
- 1, and wherein Tyrosine (Y) is replaced by Phenylalanine (F) at position 212, and Valine (V) is replaced Isoleucine (I) at position 342.
A kit for degrading ((RS)-Propan-2-yl methylphosphonofluoridate) (Sarin), consisting of an isolated organophosphorus acid anhydrolase enzyme, wherein said anhydrolase consists of a non-wild-type amino acid at sequence positions 212, and 342 of SEQ ID NO:
- 1, and wherein Tyrosine (Y) is replaced by Phenylalanine (V) at position 212, and Valine (V) is replaced by Isoleueine (I) at position 342;
- and a pharmaccuticalty-acceptable carrier.
Dependencies are inferred from the claim text.