Abstract: Alanine 2,3-aminomutase sequences are disclosed, as are cells having alanine 2,3-aminomutase activity and methods of selecting for such cells. Methods for producing beta-alanine, pantothenate, 3-hydroxypropionic acid, as well as other organic compounds, are disclosed.

Abstract: Methods of using beta-alanine/pyruvate aminotransferase to produce 3-hydroxypropionic acid and derivatives thereof, from beta-alanine, are disclosed. Cells and recombinant nucleic acids that can be used to practice the methods are also disclosed.

Abstract: Methods of using beta-alanine/pyruvate aminotransferase to produce 3-hydroxypropionic acid and derivatives thereof, from beta-alanine, are disclosed. Cells and recombinant nucleic acids that can be used to practice the methods are also disclosed.

Abstract: Methods of using beta-alanine/pyruvate aminotransferase to produce 3-hydroxypropionic acid and derivatives thereof, from beta-alanine, are disclosed. Cells and recombinant nucleic acids that can be used to practice the methods are also disclosed.

Abstract: Alanine 2,3-aminomutase sequences are disclosed, as are cells having alanine 2,3-aminomutase activity and methods of selecting for such cells. Methods for producing beta-alanine, pantothenate, 3-hydroxypropionic acid, as well as other organic compounds, are disclosed.

Abstract: Methods of using beta-alanine/pyruvate aminotransferase to produce 3-hydroxypropionic acid and derivatives thereof, from beta-alanine, are disclosed. Cells and recombinant nucleic acids that can be used to practice the methods are also disclosed.

Abstract: Alanine 2,3-aminomutase sequences are disclosed, as are cells having alanine 2,3-aminomutase activity and methods of selecting for such cells. Methods for producing beta-alanine, pantothenate, 3-hydroxypropionic acid, as well as other organic compounds, are disclosed.

Abstract: The present disclosure provides novel beta-alanine/alpha ketoglutarate aminotransferase nucleic acid and protein sequences having increased biological activity. Also provided are cells containing such enzymes, as well as methods of their use, for example to produce malonyl semialdehyde and downstream products thereof, such as 3-hydroxypropionic acid and derivatives thereof.

Abstract: Alanine 2,3-aminomutase sequences are disclosed, as are cells having alanine 2,3-aminomutase activity and methods of selecting for such cells. Methods for producing beta-alanine, pantothenate, 3-hydroxypropionic acid, as well as other organic compounds, are disclosed.

Abstract: Alanine 2,3-aminomutase sequences are disclosed, as are cells having alanine 2,3-aminomutase activity and methods of selecting for such cells. Methods for producing beta-alanine, pantothenate, 3-hydroxypropionic acid, as well as other organic compounds, are disclosed.

Abstract: Alanine 2,3-aminomutase sequences are disclosed, as are cells having alanine 2,3-aminomutase activity and methods of selecting for such cells. Methods for producing beta-alanine, pantothenate, 3-hydroxypropionic acid, as well as other organic compounds, are disclosed.

Abstract: Engineered microorganisms that produce at least 200 &mgr;g alpha-lipoic acid (ALA) per g dry cell weight and engineered microorganisms that secrete at least a 2-fold greater amount of ALA than an amount of ALA found intracellularly, are described.

Abstract: The invention provides a mutant protein which has the same amino acid sequence as an unmutated C-reactive protein (CRP) subunit or an unmutated preCRP, except that at least one amino acid of the unmutated CRP subunit or unmutated preCRP has been deleted, at least one amino acid of the unmutated CRP subunit or unmutated preCRP has been replaced by another amino acid, at least one amino acid has been added to the unmutated CRP subunit or preCRP, or a combination of such changes has been made. The amino acid(s) added, deleted and/or replaced are chosen so that the mutant protein is less likely to form covalently cross-linked aggregates than the unmutated CRP subunit or unmutated preCRP. The mutant protein also exhibits at least one of the biological activities of modified-CRP.

Abstract: The invention provides a mutant protein which has the same amino acid sequence as an unmutated C-reactive protein (CRP) subunit or an unmutated preCRP, except that at least one amino acid of the unmutated CRP subunit or unmutated preCRP has been deleted, at least one amino acid of the unmutated CRP subunit or unmutated preCRP has been replaced by another amino acid, at least one amino acid has been added to the unmutated CRP subunit or preCRP, or a combination of such changes has been made. The amino acid(s) added, deleted and/or replaced are chosen so that the mutant protein is less likely to form covalently cross-linked aggregates than the unmutated CRP subunit or unmutated preCRP. The mutant protein also exhibits at least one of the biological activities of modified-CRP.

Abstract: A culture for the production of xanthophylls comprising Nospongiococcum excentricum ATCC 40335 and mutants thereof. The culture having a dry cell weight xanthophyll content of at least about 0.65% and being capable of growing to a cell density of greater than about 40 grams per liter. The culture also comprising: carbon, phosphate, sulfate, iron, magnesium, and nitrogen.