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Full-Text Articles in Pharmacy and Pharmaceutical Sciences
Synthases, Joseph Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Synthases, Joseph Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Pharmaceutical Sciences Faculty Patents
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.
Synthases, Joseph Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Synthases, Joseph Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Pharmaceutical Sciences Faculty Patents
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.
Synthases, Joe Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Synthases, Joe Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Pharmaceutical Sciences Faculty Patents
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.
Synthases, Joe Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Synthases, Joe Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Pharmaceutical Sciences Faculty Patents
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.
Synthases, Joseph Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Synthases, Joseph Chappell, Kathleen R. Manna, Joseph P. Noel, Courtney M. Starks
Pharmaceutical Sciences Faculty Patents
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.
Chemical Isoprenoid Synthases And Uses Thereof, Joseph Chappell, Kyoungwhan Back
Chemical Isoprenoid Synthases And Uses Thereof, Joseph Chappell, Kyoungwhan Back
Pharmaceutical Sciences Faculty Patents
Disclosed is a chimeric isoprenoid synthase polypeptide including a first domain from a first isoprenoid synthase joined to a second domain from a second, heterologous isoprenoid synthase, whereby the chimeric isoprenoid synthase is capable of catalyzing the production of isoprenoid reaction products that are not produced in the absence of the second domain of the second, heterologous isoprenoid synthase. Also disclosed is a chimeric isoprenoid synthase polypeptide including an asymmetrically positioned homologous domain, whereby the chimeric isoprenoid synthase is capable of catalyzing the production of isoprenoid reaction products that are not produced when the domain is positioned at its naturally-occurring …
Chimeric Isoprenoid Synthases And Uses Thereof, Joseph Chappell, Kyoungwhan Back
Chimeric Isoprenoid Synthases And Uses Thereof, Joseph Chappell, Kyoungwhan Back
Pharmaceutical Sciences Faculty Patents
Disclosed is a chimeric isoprenoid synthase polypeptide including a first domain from a first isoprenoid synthase joined to a second domain from a second, heterologous isoprenoid synthase, whereby the chimeric isoprenoid synthase is capable of catalyzing the production of isoprenoid reaction products that are not produced in the absence of the second domain of the second, heterologous isoprenoid synthase. Also disclosed is a chimeric isoprenoid synthase polypeptide including an assymetrically positioned homologous domain, whereby the chimeric isoprenoid synthase is capable of catalyzing the production of isoprenoid reaction products that are not produced when the domain is positioned at its naturally-occurring …