Mutant xylan biosynthetic enzymes capable of dominant suppression of xylan biosynthesis
Abstract
The present invention provides for a polypeptide capable of dominant suppression of a first naturally occurring IRX10, wherein the polypeptide comprises an amino acid sequence having at least 70% identity as compared to a second naturally occurring IRX10 wherein the polypeptide comprises one or more of the conserved amino acid indicated in FIG. 2 substituted with a different amino acid residue.
- Inventors:
- Issue Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1860207
- Patent Number(s):
- 11208666
- Application Number:
- 15/847,788
- Assignee:
- The Regents of the University of California (Oakland, CA)
- Patent Classifications (CPCs):
-
C - CHEMISTRY C07 - ORGANIC CHEMISTRY C07K - PEPTIDES
C - CHEMISTRY C12 - BIOCHEMISTRY C12N - MICROORGANISMS OR ENZYMES
- DOE Contract Number:
- AC02-05CH11231
- Resource Type:
- Patent
- Resource Relation:
- Patent File Date: 12/19/2017
- Country of Publication:
- United States
- Language:
- English
Citation Formats
Brandon, Andrew, Scheller, Henrik Vibe, and Loque, Dominique. Mutant xylan biosynthetic enzymes capable of dominant suppression of xylan biosynthesis. United States: N. p., 2021.
Web.
Brandon, Andrew, Scheller, Henrik Vibe, & Loque, Dominique. Mutant xylan biosynthetic enzymes capable of dominant suppression of xylan biosynthesis. United States.
Brandon, Andrew, Scheller, Henrik Vibe, and Loque, Dominique. Tue .
"Mutant xylan biosynthetic enzymes capable of dominant suppression of xylan biosynthesis". United States. https://www.osti.gov/servlets/purl/1860207.
@article{osti_1860207,
title = {Mutant xylan biosynthetic enzymes capable of dominant suppression of xylan biosynthesis},
author = {Brandon, Andrew and Scheller, Henrik Vibe and Loque, Dominique},
abstractNote = {The present invention provides for a polypeptide capable of dominant suppression of a first naturally occurring IRX10, wherein the polypeptide comprises an amino acid sequence having at least 70% identity as compared to a second naturally occurring IRX10 wherein the polypeptide comprises one or more of the conserved amino acid indicated in FIG. 2 substituted with a different amino acid residue.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2021},
month = {12}
}
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