University of Iowa Research Foundation

Cargill Inc.

Merck + Co., Inc.

John P Rosazza

Timothy Walter Abraham

Douglas Conrad Cameron, Jr

Paula M Hicks

Sara C McFarlan

David Paul Weiner

Lishan Zhao

Tao Li

Yijun Chen

Lacy Daniels

Aimin He

Steven John Gort

Michel M Chartrain

Fernando A Sanchez-Riera

Chris H Senanayake

Ian Fotheringham

Mervyn L deSouza

Jinyou Zhang

Mary Jo Zidwick

Ian Fotherington

Methods and compositions that can be used to make monatin from glucose, tryptophan, indole-3-lactic acid, indole-3-pyruvate, and 2-hydroxy 2-(indol-3-ylmethyl)-4-keto glutaric acid, are provided. Methods are also disclosed for producing the indole-3-pyruvate and 2-hydroxy 2-(indol-3-ylmethyl)-4-keto glutaric acid intermediates. Compositions provided include nucleic acid molecules, polypeptides, chemical structures, and cells. Methods include in vitro and in vivo processes, and the in vitro methods include chemical reactions.

Polypeptides and biosynthetic pathways for the production of monatin and its precursors

Methods and compositions that can be used to make monatin or salt thereof from glucose, tryptophan, indole-3-lactic acid, indole-3-pyruvate, and 2-hydroxy 2-(indol-3-ylmethyl)-4-keto glutaric acid, are provided. Methods are also disclosed for producing the indole-3-pyruvate and 2-hydroxy 2-(indol-3-ylmethyl)-4-keto glutaric acid intermediates. Compositions provided include nucleic acid molecules, polypeptides, chemical structures, and cells. Methods include in vitro and in vivo processes, and the in vitro methods include chemical reactions.

Production of monatin and monatin precursors

The invention provides the nucleotide sequence and amino acid sequence for the enzyme carboxylic acid reductase isolated from bacteria. Expression cassettes, vectors, transformed cells, and variants are also provided as methods for use of recombinant biocatalytic reagents in production of synthetic, aromatic, aliphatic and alicyclic aldehydes and alcohols.

Carboxylic acid reductase polypeptide, nucleotide sequence encoding same and methods of use

A nitric oxide synthase (NOS) protein is obtained from rat brain and purified to a specific activity at least 6,360-fold that of a crude tissue preparation. The NOS protein has a denatured MW of 105 kD determined by SDS-PAGE, a dimeric MW of 230 kD determined by gel filtration and requires FAD, FMN, Ca.sup.2+ and tetrahydropterin for the production of nitric oxide from L-arginine or an arginine-rich peptide, oligopeptide or protein substrate.

Purified nitric oxide synthase from rat brain

A process is disclosed that hydrolyzes, by the action of an epoxide hydrolase of Diplodia gossipina (alternatively named Diplodia gossypina) ATCC 16391 or ATCC 10936, the undesired enantiomer of racemic indene oxide, an epoxide of indan.

Resolution of racemic indene oxide to yield (1S,2R)-indene oxide using

The present invention is directed to a novel, biologically-derived carboxylic acid reductase, also referred to herein as an aryl-aldehyde oxidoreductase, that has been isolated and purified from Nocardia sp. strain NRRL 5646, and to methods of using the carboxylic acid reductase as a biocatalyst for the reduction of carboxylic acids or their derivatives to the corresponding useful product(s). In a preferred embodiment, the invention is directed to biochemically-produced vanillin, and to the methods of its production by the biocatalytic reduction of vanillic acid, or a precursor or derivative thereof, in a reaction comprising the substantially purified, biologically-derived carboxylic acid reductase.

Carboxylic acid reductase, and methods of using same

Nitric oxide synthase has been discovered to exist in bacteria. The bacterial nitric oxide synthase was purified as much as 1,362-fold by a combination of 2', 5'-ADP-agarose affinity chromatography, and hydroxylapatite chromatography and its unique N-terminal amino acid sequence was identified.

Bacterial nitric oxide synthase

Growing community of inventors

Iowa City, IA, United States of America

John P Rosazza