Abstract: Introducing sucrose phosphorylase activity into plants by transformation with a gene for the enzyme increases the rate of sucrose hydrolysis, leading to increased starch, oil, and protein levels. The preferred gene is from Streptococcus mutans. Surprisingly, in potatoes transformed to express this gene in tubers, reduced bruise discoloration susceptibility and increased uniformity of starch deposition throughout the tuber are achieved.

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, .alpha.-ketobutyrate, propionate, propionyl-CoA, .beta.-ketovaleryl-CoA, and .beta.-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. Introduction into plants and bacteria of an appropriate .beta.-ketothiolase, .beta.

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 end product. By these methods, enhanced levels of threonine, .alpha.-ketobutyrate, propionate, propionyl-CoA, .beta.-ketovaleryl-CoA, and .beta.-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. Introduction into plants and bacteria of an appropriate .beta.-ketothiolase, .beta.

Abstract: Glyphosate-tolerant 5-enolpyruvyl-3-phosphoshikimate (EPSP) synthases, DNA encoding glyphsate-tolerant EPSP synthases, plant genes encoding the glyphosate-tolerant enzymes, plant transformation vectors containing the genes, transformed plant cells and differentiated transformed plants containing the plant genes are disclosed. The glyphosate-tolerant EPSP synthases are prepared by substituting an alanine residue for a glycine residue in a first conserved sequence found between positions 80 and 120, and a threonine residue for an alanine residue in a second conserved sequence found between positions 170 and 210 in the mature wild type EPSP synthase.

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 a glyphosate oxidoreductase enzyme are disclosed. The genes are useful in producing transformed bacteria and plants which degrade glyphosate herbicide as well as crop plants which are tolerant to glyphosate herbicide.

Abstract: A method of producing plant products containing modified starch content, including higher ratios of amylose to amylopectin, increase in intermediate material, or amylopectin having fewer branches or altered branching pattern. Also provided are DNA constructs and transformed plant cells useful in that method. The preferred method uses isoamylase from a Flavobacterium sp., more preferably in combination with a gene encoding ADPglucose pyrophosphorylase. Also disclosed are the gene from Flavobacterium sp. and transformed bacterial and plant cells containing a derivative thereof.

Abstract: Introducing sucrose phosphorylase activity into plants by transformation with a gene for the enzyme increases the rate of sucrose hydrolysis, leading to increased starch, oil, and protein levels. The preferred gene is from Streptococcus mutans. Surprisingly, in potatoes transformed to express this gene in tubers, reduced bruise discoloration susceptibility and increased uniformity of starch deposition throughout the tuber are achieved.

Abstract: A method for controlling the ripening of fruits and vegetables as well as a method for controlling senescence of plant tissue is described. The method generally embraces the expression of an ACC metabolizing enzyme in the fruit or other desired plant tissue to inhibit the production of ethylene in the fruit or plant tissue. The use of the ACC metabolizing enzyme ACC deaminase is described in detail. The ripening or senescence process in the fruit or plant tissue is inhibited by the expression of the ACC deaminase gene such that the shelf-life and marketability of the fruit or plant is enhanced. The ACC metabolizing enzyme may be used in combination with other methods for reducing ethylene production in transformed plants to further reduce the production of ethylene in the fruit or plant. DNA constructs containing the ACC deaminase gene are also described.

Abstract: The invention relates to a method of improving the quality of potatoes stored at reduced temperatures and a method of prolonging dormancy of stored potato tubers, by increasing the level of ADPglucose pyrophosphorylase enzyme activity within the potato tuber during storage at ambient or reduced temperatures. Novel DNA molecules, plant cells, and potato plants are provided which contain the gene for the ADPglucose pyrophosphorylase enzyme.