Mutant OPAA enzymes with increased catalytic efficiency on cyclosarin
AssigneeThe United States of America as represented by the Secretary of the Army
InventorsSteven P Harvey, Melissa M Dixon, Mark A Guelta
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Abstract
The invention comprises isolated, mutant, non-wild-type organophosphorus acid anhydrolase (OPAA) enzymes having two site mutations, methods of production, and methods of use to effectively degrade cylcosarin (GF) (cyclohexyl methylphosphonofluoridate) with greater catalytic efficiency than the wild-type OPAA.
Claims11
An isolated, mutant organophosphorus acid anhydrolase (OPAA) enzyme, wherein said mutant anhydrolase comprises a non-wild-type amino acid at each of sequence positions 212 and 342 of SEQ ID NO:
- 1, and wherein said mutant anhydrolase comprises Phenylalanine (F) at sequence position 212 and Tyrosine (Y) at sequence position 342 of SEQ ID NO:
- 1.
A method for degrading GF (cyclohexyl methylphosphonofluoridate), comprising contacting GF with a mutant organophosphorus acid anhydrolase, wherein said mutant anhydrolase comprises a non-wild-type amino acid at sequence positions 212 and 342 of SEQ ID NO:
- 1, and wherein said mutant anhydrolase comprises Phenylalanine (F) at sequence position 212 and Tyrosine (Y) at sequence position 342 of SEQ ID NO:
- 1.
A kit for degrading GF, comprising:
- (a) an isolated, mutant organophosphorus acid anhydrolase, wherein said mutant anhydrolase comprises a non-wild-type amino acid at sequence positions 212 and 342 of SEQ ID NO:
- 1, and wherein said mutant anhydrolase comprises Phenylalanine (F) at sequence position 212 and Tyrosine (Y) at sequence position 342 of SEQ ID NO:
- 1;
- and
- (b) a pharmaceutically-acceptable carrier.
Dependencies are inferred from the claim text.