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 methods 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.

Inventors:
 [1];  [1];  [2];  [2]
  1. Shoreham, NY
  2. Jarfalla, SE
Issue Date:
Research Org.:
Associated Universities, Inc., Upton, NY (United States)
OSTI Identifier:
871309
Patent Number(s):
5705391
Application Number:
08/689,823
Assignee:
Associated Universities, Inc. (Washington, DC)
Patent Classifications (CPCs):
C - CHEMISTRY C07 - ORGANIC CHEMISTRY C07K - PEPTIDES
C - CHEMISTRY C12 - BIOCHEMISTRY C12N - MICROORGANISMS OR ENZYMES
DOE Contract Number:  
AC02-76CH00016
Resource Type:
Patent
Country of Publication:
United States
Language:
English
Subject:
modified; acyl-acp; desaturase; disclosed; methods; modifying; chain; length; double; bond; positional; specificities; soluble; plant; fatty; acid; specifically; method; involves; amino; contact; residues; substrate; binding; channel; modification; lie; identified; subsequently; replaced; effect; activity; plant fatty; acid contact; specifically disclosed; method involves; amino acid; fatty acid; chain length; contact residues; acid desaturase; acyl-acp desaturase; modified acyl-acp; method involve; modifying amino; involves modifying; soluble plant; positional specificities; bond positional; double bond; /435/999/

Citation Formats

Cahoon, Edgar B, Shanklin, John, Lindgvist, Ylva, and Schneider, Gunter. Modified acyl-ACP desaturase. United States: N. p., 1998. Web.
Cahoon, Edgar B, Shanklin, John, Lindgvist, Ylva, & Schneider, Gunter. Modified acyl-ACP desaturase. United States.
Cahoon, Edgar B, Shanklin, John, Lindgvist, Ylva, and Schneider, Gunter. Tue . "Modified acyl-ACP desaturase". United States. https://www.osti.gov/servlets/purl/871309.
@article{osti_871309,
title = {Modified acyl-ACP desaturase},
author = {Cahoon, Edgar B and Shanklin, John and Lindgvist, Ylva and Schneider, Gunter},
abstractNote = {Disclosed is a methods 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.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1998},
month = {1}
}

Patent:

Save / Share:

Works referenced in this record:

Di-iron—carboxylate proteins
journal, December 1995


Structure and Function of the Escherichia coli Ribonucleotide Reductase Protein R2
journal, July 1993


Stearoyl-acyl carrier protein delta 9 desaturase from Ricinus communis is a diiron-oxo protein.
journal, March 1993


Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane
journal, December 1993


Expression of a coriander desaturase results in petroselinic acid production in transgenic tobacco.
journal, December 1992