Monsanto Technology LLC

Reg Life Sciences, LLC

Ls9, Inc.

Genomatica, Inc.

Murtaza F Alibhai

Zhihao Hu

Hugh A Sampson

Louis G Hom

Vikranth Arlagadda

Eli S Groban

Elizabeth J Clarke

Na Trinh

James D Astwood

Charles A McWherter

Timothy J Rydel

Stanislaw Flasinski

Andreas W Schirmer

Paul C C Feng

Gregory R Heck

Mathew A Rude

Youlin Qi

William Carlton Stallings

Claire Cajacob

Paul C Feng

The present invention relates to novel mutant thioesterase enzymes and naturally-occurring equivalents thereof, compositions made from such enzymes and uses of thioesterase enzymes. In particular, the present invention provides mutant thioesterase enzymes that have altered properties, for example, altered substrate specificity, altered activity, altered selectivity, and/or altered proportional yields in the product mixtures. The present invention also provides polynucleotides encoding such mutant thioesterase enzymes, and vectors and host cells comprising such polynucleotides. The invention further provides for novel uses of thioesterases in the production of various fatty acid derivatives, which are useful as, or as components of, industrial chemicals and fuels.

Methods and compositions related to thioesterase enzymes

Compositions and methods for producing olefins are described herein. The olefins can be used to produced biofuels.

Methods and compositions for producing olefins

The compositions and methods disclosed herein provide novel DNA molecules that encode glyphosate resistant EPSPS proteins and plants containing these new proteins. The plants that express the new EPSPS proteins are themselves tolerant to the herbicidal effects of glyphosate.

Glyphosate resistant class I 5-endolpyruvylshikimate-3-phosphate synthase (EPSPS)

Methods and compositions, including nucleotide sequences, amino acid sequences, and host cells, for producing fatty aldehydes are described.

Methods and compositions for producing fatty aldehydes

Glyphosate resistant class I 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS)

The present invention discloses DNA sequences encoding plant and novel lipid acyl hydrolase proteins having coleopteran specific insect inhibitory activity, as well as variants and permuteins having enhanced levels of activity directed to controlling coleopteran insect infestation and enhanced levels of expression in planta. Additionally, catalytic dyad active site conformation is disclosed for both dicot and monocot plant derived non-specific lipid acyl hydrolases having coleopteran insect inhibitory properties.

Insect inhibitory lipid acyl hydrolases

Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of patatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding. Permuteins are also disclosed which have a rearranged amino acid sequence while retaining enzymatic activity. Deallergenized proteins and permuteins can be used as insecticidal materials, as nutritional supplements, and as immunotherapeutic agents.

Nucleic acids encoding deallergenized proteins and permuteins

Preparation of deallergenized proteins and permuteins

The present invention discloses DNA sequences encoding plant and novel lipid acyl hydrolase proteins having coleopteran specific insect inhibitory activity, as well as variants and permuteins having enhanced levels of activity directed to controlling coleotperan insect infestation and enhanced levels of expression in planta. Additionally, catalytic dyad active site conformation is disclosed for both dicot and monocot plant derived non-specific lipid acyl hydrolases having coleopteran insect inhibitory properties.

Modified proteins are disclosed that maintain enzymatic and insecticidal activity while displaying reduced or eliminated allergenicity. Epitopes which bind to anti-patatin antibodies were identified, and removed via site directed mutagenesis. Tyrosines were observed to generally contribute to the allergenic properties of palatin proteins. Removal of glycosylation sites was observed to reduce or eliminate antibody binding. Permuteins are also disclosed which have a rearranged amino acid sequence while retaining enzymatic activity. Deallergenized proteins and permuteins can be used as insecticidal materials, as nutritional supplements, and as immunotherapeutic agents.

Growing community of inventors

Chesterfield, MO, United States of America

Murtaza F Alibhai