Abstract: Provided herein are microorganisms that include one or more heterologous nucleic acid selected from the group of a sequence encoding a 7-methylxanthosine synthase, a sequence encoding a theobromine synthase; and a sequence encoding a caffeine synthase, where the microorganism is capable of producing one or more purine alkaloid in a culture medium, when the microorganism is cultured under conditions sufficient to produce the one or more purine alkaloid. Also provided compositions and kits that include at least one of these microorganisms, and methods of producing one or more purine alkaloid that include culturing one of these microorganisms under conditions sufficient to produce the one or more purine alkaloid.

Abstract: Modified or recombinant microorganisms are provided herein that can be used to produce one or more amino acids, including, for example, methionine or one or more methionine biosynthetic pathway-derived intermediates or one or more methionine-based products.

Abstract: Provided herein are microorganisms that include one or more heterologous nucleic acid selected from the group of a sequence encoding a 7-methylxanthosine synthase, a sequence encoding a theobromine synthase; and a sequence encoding a caffeine synthase, where the microorganism is capable of producing one or more purine alkaloid in a culture medium, when the microorganism is cultured under conditions sufficient to produce the one or more purine alkaloid. Also provided compositions and kits that include at least one of these microorganisms, and methods of producing one or more purine alkaloid that include culturing one of these microorganisms under conditions sufficient to produce the one or more purine alkaloid.

Abstract: Modified or recombinant microorganisms are provided herein that can be used to produce one or more amino acids, including, for example, methionine or one or more methionine biosynthetic pathway-derived intermediates or one or more methionine-based products.

Abstract: Transformed plants which have increased or decreased linolenic acid content are disclosed. Also disclosed are plants which express a linoleic acid desaturase gene.

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: Transformed plants which have increased or decreased linolenic acid content are disclosed. Also disclosed are plants which express a linoleic acid desaturase gene.

Abstract: Methods of altering the linolenic and oleic acid content in plants are disclosed. Also disclosed are transformed plants which have altered linolenic and oleic acid content, and the DNA molecules used to produce them.

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: 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: Promoters for enhanced expression of ADPglucose pyrophosphorylase in potato tubers and fruits such as tomato; methods of using them; DNA molecules, plant cells and plants containing them. A method of decreasing the oil content of seeds by expression of ADPglucose pyrophosphorylase.

Abstract: Transformed plant cells which have increased'starch content are disclosed. Also disclosed are whole plants comprising plant cells which express CTP/ADPglucose pyrophosphorylase genes.

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 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 weU as a method for selectively controlling weeds in a planted transgenic crop field.

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 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: 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. Sucrose phosphorylase genes from Streptococcus mutans and Leuconostoc mesenteroides have been found particularly advantageous for use in the present invention. Surprisingly, in potatoes transformed to express these genes in tubers, reduced bruise discoloration susceptibility and increased uniformity of starch deposition throughout the tuber are achieved.

Abstract: DNA encoding glyphosate-tolerant 5-enolpyruvyl-3-phosphoshikimate (EPSP) synthases, plant genes encoding the glyphosate-tolerant enzymes, and plant transformation vectors containing the genes are disclosed. The DNA encodes glyphosate-tolerant EPSP synthases modified by substitution of 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: 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. Sucrose phosphorylase genes from Streptococcus mutans and Leuconostoc mesenteroides have been found particularly advantageous for use in the present invention. Surprisingly, in potatoes transformed to express these genes in tubers, reduced bruise discoloration susceptibility and increased uniformity of starch deposition throughout the tuber are achieved.