skip to main content
DOE Patents title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Modified acyl-ACP desaturase

Abstract

Disclosed is a method for modifying the chain length and double bond positional specificities of a soluble plant fatty acid desaturase. More specifically, the method involves modifying amino acid contact residues in the substrate binding channel of the soluble fatty acid desaturase which contact the fatty acid. Specifically disclosed is the modification of an acyl-ACP desaturase. Amino acid contact residues which lie within the substrate binding channel are identified, and subsequently replaced with different residues to effect the modification of activity. 1 fig.

Inventors:
; ; ;
Issue Date:
Research Org.:
Associated Universities Inc
Sponsoring Org.:
USDOE, Washington, DC (United States)
OSTI Identifier:
563670
Patent Number(s):
5705391
Application Number:
PAN: 8-689,823
Assignee:
Associated Universities, Inc., Washington, DC (United States)
DOE Contract Number:  
AC02-76CH00016
Resource Type:
Patent
Resource Relation:
Other Information: PBD: 6 Jan 1998
Country of Publication:
United States
Language:
English
Subject:
55 BIOLOGY AND MEDICINE, BASIC STUDIES; OXYGENASES; SPECIFICITY; BIOCHEMICAL REACTION KINETICS; ENZYME ACTIVITY; CHEMICAL BONDS; CARBOXYLIC ACIDS

Citation Formats

Cahoon, E B, Shanklin, J, Lindgvist, Y, and Schneider, G. Modified acyl-ACP desaturase. United States: N. p., 1998. Web.
Cahoon, E B, Shanklin, J, Lindgvist, Y, & Schneider, G. Modified acyl-ACP desaturase. United States.
Cahoon, E B, Shanklin, J, Lindgvist, Y, and Schneider, G. Tue . "Modified acyl-ACP desaturase". United States.
@article{osti_563670,
title = {Modified acyl-ACP desaturase},
author = {Cahoon, E B and Shanklin, J and Lindgvist, Y and Schneider, G},
abstractNote = {Disclosed is a method for modifying the chain length and double bond positional specificities of a soluble plant fatty acid desaturase. More specifically, the method involves modifying amino acid contact residues in the substrate binding channel of the soluble fatty acid desaturase which contact the fatty acid. Specifically disclosed is the modification of an acyl-ACP desaturase. Amino acid contact residues which lie within the substrate binding channel are identified, and subsequently replaced with different residues to effect the modification of activity. 1 fig.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1998},
month = {1}
}