Novel polypeptides and the corresponding nucleic acids encoding such polypeptides are disclosed herein. The invention provides methods of making modified polypeptides by altering one or more amino acid residues involved in the active site of a preselected polypeptide.
Novel synthases and the corresponding nucleic acids encoding such synthases are disclosed herein. Such synthases possess an active site pocket that includes key amino acid residues that are modified to generate desired terpenoid reaction intermediates and products. Synthase modifications are designed based on, e. g. , the three-dimensional coordinates of tobacco 5-epi-aristolochene synthase with or without a substrate bound in the active site.
Novel synthases and the corresponding nucleic acids encoding such synthases are disclosed herein. Such synthases possess an active site pocket that includes key amino acid residues that are modified to generate desired terpenoid reaction intermediates and products. Synthase modifications are designed based on, e. g. , the three-dimensional coordinates of tobacco 5-epi-aristolochene synthase, with or without a substrate bound in the active site.
Novel synthases and the corresponding nucleic acids encoding such synthases are disclosed herein. Such synthases possess an active site pocket that includes key amino acid residues that are modified to generate desired terpenoid reaction intermediates and products. Synthase modifications are designed based on, e. g. , the three-dimensional coordinates of tobacco 5-epi-aristolochene synthase, with or without a substrate bound in the active site.
Pathogen- Or Elicitor-Inducible Transcription Regulatory Element From The Tobacco 5-Epi-Aristolochene Synthase Gene And Plants Transformed Therewith
Joseph Chappell - Lexington KY Shaohui Yin - Ardmore OK Catherine Cornett - Florence KY
Assignee:
University of Kentucky Research Foundation - Lexington KY
International Classification:
A01H 500
US Classification:
8003173, 435419, 800298, 800317
Abstract:
A tobacco epi-5-aristolochene synthase transcriptional regulatory element functional in plants, plant tissue and in plant cells for pathogen inducible gene expression and a method for increasing the transcriptional expression of downstream genetic information in plants, plant tissue and plant cells are disclosed.
Joseph Chappell - Lexington KY Kathleen R. Manna - Georgetown IN Joseph P. Noel - San Diego CA Courtney M. Starks - La Jolla CA
Assignee:
The Salk Institute for Biological Studies - La Jolla CA The University of Kentucky Research Foundation - Lexington KY
International Classification:
C12N 500
US Classification:
435325, 435183, 435193, 435410, 435468, 800278
Abstract:
Novel synthases and the corresponding nucleic acids encoding such synthases are disclosed herein. Such synthases possess an active site pocket that includes key amino acid residues that are modified to generate desired terpenoid reaction intermediates and products. Synthase modifications are designed based on, e. g. , the three-dimensional coordinates of tobacco 5-epi-aristolochene synthase, with or without a substrate bound in the active site.
Joseph Chappell - Lexington KY, US Kathleen R. Manna - Georgetown IN, US Joseph P. Noel - San Diego CA, US Courtney M. Starks - La Jolla CA, US
Assignee:
The University of Kentucky Research Foundation - Lexington KY The Salk Institute for Biological Studies - San Diego CA
International Classification:
C12N005/00 C12N009/00 C12N009/10
US Classification:
435325, 435183, 435193, 435410, 435468, 800278
Abstract:
Novel synthases and the corresponding nucleic acids encoding such synthases are disclosed herein. Such synthases possess an active site pocket that includes key amino acid residues that are modified to generate desired terpenoid reaction intermediates and products. Synthase modifications are designed based on, e. g. , the three-dimensional coordinates of tobacco 5-epi-aristolochene synthase. with or without a substrate bound in the active site.
Plant Cells And Plants Expressing Chimeric Isoprenoid Synthases
Joseph Chappell - Lexington KY, US Kyoungwhan Back - Kwangju, KR
Assignee:
University of Kentucky, Research Foundation - Lexington KY
International Classification:
A01H 5/00 C12N 15/82
US Classification:
800298, 435419
Abstract:
The invention features plant cells and plants that include a nucleic acid molecule encoding a chimeric isoprenoid synthase polypeptide including an asymmetrically positioned homologous domain. The chimeric isoprenoid synthases of the invention catalyze the production of isoprenoid reaction products that are not produced when the asymmetrically positioned homologous domain is positioned at its naturally-occurring site in an isoprenoid synthase polypeptide.
Dr. Chappell graduated from the Emory University School of Medicine in 1973. He works in Tupelo, MS and specializes in Ophthalmology. Dr. Chappell is affiliated with North Mississippi Medical Center.
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