Accession Number : ADA182210

Title :   Mutant Proteins--Enzymes to Hydrolyze Toxic Organophosphates.

Descriptive Note : Annual rept. 15 Jun 86-14 Jun 87,

Corporate Author : CALIFORNIA INST OF TECH PASADENA DIV OF CHEMISTRY AND CHEMICAL ENGINEERING

Personal Author(s) : Richards,John H

PDF Url : ADA182210

Report Date : 15 Jun 1987

Pagination or Media Count : 8

Abstract : This report discusses how the function of a protein is related to its three-dimensional structure and in turn to its sequence of amino acids, and how the various elements of a protein contribute to its structure stability. To gain the appropriated insights into the general rules that govern these relationships, we are developing and using various techniques of mutagenesis to alter the amino acid sequence in enzymes such as Beta-lactamase (responsible for resistance to penicillin therapy in many strains of infectious bacteria) and the serine protease alpha-lytic protease. We also employ novel chemical modifications of mutant proteins to achieve structures that cannot be obtained by purely biochemical approaches. The eventual objective is to be able to develop new enzymatic catalysts that, for example, will accelerate the hydrolysis of toxic organophosphates, some of which are potent nerve bases. Keywords: Antibiotic Resistance.

Descriptors :   *AMINO ACIDS, *HYDROLYSIS, *ORGANOPHOSPHATES, *ENZYMES, *PROTEINS, *MOLECULAR STRUCTURE, ANTIBIOTICS, RESISTANCE(BIOLOGY), CATALYSIS, PEPTIDE HYDROLASES, BACTERIA, BIOCHEMISTRY, CATALYSTS, CHEMICALS, INFECTIOUS DISEASES, MODIFICATION, MUTATIONS, ORGANOPHOSPHATES, SEQUENCES, STABILITY, STRAINS(BIOLOGY), STRUCTURES, THERAPY, THREE DIMENSIONAL, TOXICITY

Subject Categories : Biochemistry
      Genetic Engineering and Molecular Biology

Distribution Statement : APPROVED FOR PUBLIC RELEASE