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Overexpression of Phosphotriesterase, a Metallo-Organophosphorous Hydrolase by a Novel and Versatile Protein Expression System

Award Information
Agency: Department of Defense
Branch: Army
Contract: DAAD19-02-C-0022
Agency Tracking Number: A013-0034
Amount: $100,000.00
Phase: Phase I
Program: STTR
Solicitation Topic Code: N/A
Solicitation Number: N/A
Solicitation Year: N/A
Award Year: 2001
Award Start Date (Proposal Award Date): N/A
Award End Date (Contract End Date): N/A
Small Business Information
255 Robinson Road
Pasadena, CA 91104
United States
DUNS: 011114167
HUBZone Owned: No
Woman Owned: No
Socially and Economically Disadvantaged: No
Principal Investigator
 Sunney Chan
 George G. Hoag Profesor
 (626) 395-6524
Business Contact
 Philip Koebel
Title: Chief Operating Officer
Phone: (626) 797-6342
Research Institution
 Richard P Seligman
Division of Chem./Chem. Eng.
Pasadena, CA 91125
United States

 (626) 395-6357
 Nonprofit College or University

A unique recombinant protein overexpression system will be investigated for the production of phosphotriesterase, an organophosphate hydrolase from Pseudomonas diminuta MG and Flavobacterium sp. ATCC 27551. This enzyme is a leading bioremediationcandidate for large-scale detoxification of insecticides and chemical warfare agents. The hydrolase will be prepared in three different versions using this novel system. A soluble form, a membrane-bound version and a fusion protein suitable for biosensorapplications will be attempted. This versatile expression vehicle could be very effective for membrane protein applications, an important niche where systems currently available have been shown to be inadequate. Furthermore, the low-cost nature of thissystem is very attractive for large-scale protein production purposes.This system will occupy an important niche market where expression systems currently available commercially are not effective. This system can be used for the mass production ofmedicinally important membrane proteins and in structural genomics efforts of membrane proteins. The recombinant membrane proteins can be marketed for use in high-throughput screening, in structural biology efforts of medicinally important membraneproteins hence crucil in structure-based drug design endeavors.

* Information listed above is at the time of submission. *

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