Abstract: Nucleic acid sequences, vectors, recombinant host cells, transgenic plants, and methods for their preparation are disclosed. The nucleic acid sequences encode threonine deaminase proteins that catalyze the conversion of threonine to ?-ketobutyrate. One or both of the amino acids at positions 447 and 481 of the encoded proteins can be selected from groups of particular amino acids. For example, the amino acid at position 447 can be alanine, isoleucine, valine, phenylalanine, tryptophan, or methionine. The amino acid at position 481 can be alanine, isoleucine, proline, phenylalanine, tryptophan, or methionine.

Abstract: Nucleic acid sequences, vectors, recombinant host cells, transgenic plants, and methods for their preparation are disclosed. The nucleic acid sequences encode threonine deaminase proteins that catalyze the conversion of threonine to ?-ketobutyrate. One or both of the amino acids at positions 447 and 481 of the encoded proteins can be selected from groups of particular amino acids. For example, the amino acid at position 447 can be alanine, isoleucine, valine, phenylalanine, tryptophan, or methionine. The amino acid at position 481 can be alanine, isoleucine, proline, phenylalanine, tryptophan, or methionine.

Abstract: Genes and methods for optimizing levels of substrates employed in the biosynthesis of copolymers of 3-hydroxybutyrate (3HB) and 3-hydroxyvalerate (3HV) in plants and bacteria via manipulation of normal metabolic pathways using recombinant DNA techniques are provided. This is achieved through the use of a variety of wild-type and/or deregulated enzymes involved in the biosynthesis of aspartate family amino acids, and wild-type or deregulated forms of enzymes, such as threonine deaminase, involved in the conversion of threonine to P(3HB-co-3HV) copolymer endproduct. By these methods, enhanced levels of threonine, &agr;-ketobutyrate, propionate, propionyl-CoA, &bgr;-ketovaleryl-CoA, and &bgr;-hydroxyvaleryl-CoA are produced. Also provided are methods for the biological production of P(3HB-co-3HV) copolymers in plants and bacteria utilizing propionyl-CoA produced through a variety of engineered metabolic pathways.

Abstract: Genes encoding Class II EPSPS enzymes are disclosed. The genes are useful in producing transformed bacteria and plants which are tolerant to glyphosate herbicide. Class II EPSPS genes share little homology with known, Class I EPSPS genes, and do not hybridize to probes from Class I EPSPS's. The Class II EPSPS enzymes are characterized by being more kinetically efficient than Class I EPSPS's in the presence of glyphosate. Plants transformed with Class II EPSPS genes are also disclosed as well as a method for selectively controlling weeds in a planted transgenic crop field.

Abstract: Genes encoding Class II EPSPS enzymes are disclosed. The genes are useful in producing transformed bacteria and plants which are tolerant to glyphosate herbicide. Class II EPSPS genes share little homology with known, Class I EPSPS genes, and do not hybridize to probes from Class I EPSPS's. The Class II EPSPS enzymes are characterized by being more kinetically efficient than Class I EPSPS's in the presence of glyphosate. Plants transformed with Class II EPSPS genes are also disclosed as well as a method for selectively controlling weeds in a planted transgenic crop field.

Abstract: Genes encoding Class II EPSPS enzymes are disclosed. The genes are useful in producing transformed bacteria and plants which are tolerant to glyphosate herbicide. Class II EPSPS genes share little homology with known, Class I EPSPS genes, and do not hybridize to probes from Class I EPSPS's. The Class II EPSPS enzymes are characterized by being more kinetically efficient than Class I EPSPS's in the presence of glyphosate. Plants transformed with Class II EPSPS genes are also disclosed as well as a method for selectively controlling weeds in a planted transgenic crop field.