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Title: Cellobiohydrolase I enzymes

Abstract

Provided herein is an isolated Cel7A polypeptide comprising mutations in the catalytic domain of the polypeptide relative to the catalytic domain of a wild type Cel7A polypeptide, wherein the mutations reduce N-linked glycosylation of the isolated polypeptide relative to the wild type polypeptide. Also provided herein is an isolated Cel7A polypeptide comprising increased O-linked glycosylation of the linker domain relative to a linker domain of a wild type Cel7A polypeptide. The increased O-linked glycosylation is a result of the addition of and/or substitution of one or more serine and/or threonine residues to the linker domain relative to the linker domain of the wild type polypeptide. In some embodiments, the isolated Cel7A polypeptide comprising mutations in the catalytic domain of the polypeptide relative to the catalytic domain of a wild type Cel7A polypeptide further comprises increased O-linked glycosylation of the linker domain relative to a linker domain of a wild type Cel7A polypeptide. The mutations in the catalytic domain reduce N-linked glycosylation of the isolated polypeptide relative to the wild type polypeptide. The addition of and/or substitution of one or more serine and/or threonine residues to the linker domain relative to the linker domain of the wild type polypeptide increases O-linkedmore » glycosylation of the isolated polypeptide. Further provided are compositions comprising such polypeptides and nucleic acids encoding such polypeptides. Still further provided are methods for making such polypeptides.« less

Inventors:
; ; ; ; ; ;
Issue Date:
Research Org.:
National Energy Technology Laboratory (NETL), Pittsburgh, PA, Morgantown, WV (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1117875
Patent Number(s):
8637293
Application Number:
12/123,352
Assignee:
Alliance for Sustainable Energy, LLC (Golden, CO)
Patent Classifications (CPCs):
C - CHEMISTRY C12 - BIOCHEMISTRY C12N - MICROORGANISMS OR ENZYMES
C - CHEMISTRY C12 - BIOCHEMISTRY C12Y - ENZYMES
DOE Contract Number:  
AC36-99GO10337
Resource Type:
Patent
Resource Relation:
Patent File Date: 2008 May 19
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Adney, William S, Himmel, Michael E, Decker, Stephen R, Knoshaug, Eric P, Nimlos, Mark R, Crowley, Michael F, and Jeoh, Tina. Cellobiohydrolase I enzymes. United States: N. p., 2014. Web.
Adney, William S, Himmel, Michael E, Decker, Stephen R, Knoshaug, Eric P, Nimlos, Mark R, Crowley, Michael F, & Jeoh, Tina. Cellobiohydrolase I enzymes. United States.
Adney, William S, Himmel, Michael E, Decker, Stephen R, Knoshaug, Eric P, Nimlos, Mark R, Crowley, Michael F, and Jeoh, Tina. Tue . "Cellobiohydrolase I enzymes". United States. https://www.osti.gov/servlets/purl/1117875.
@article{osti_1117875,
title = {Cellobiohydrolase I enzymes},
author = {Adney, William S and Himmel, Michael E and Decker, Stephen R and Knoshaug, Eric P and Nimlos, Mark R and Crowley, Michael F and Jeoh, Tina},
abstractNote = {Provided herein is an isolated Cel7A polypeptide comprising mutations in the catalytic domain of the polypeptide relative to the catalytic domain of a wild type Cel7A polypeptide, wherein the mutations reduce N-linked glycosylation of the isolated polypeptide relative to the wild type polypeptide. Also provided herein is an isolated Cel7A polypeptide comprising increased O-linked glycosylation of the linker domain relative to a linker domain of a wild type Cel7A polypeptide. The increased O-linked glycosylation is a result of the addition of and/or substitution of one or more serine and/or threonine residues to the linker domain relative to the linker domain of the wild type polypeptide. In some embodiments, the isolated Cel7A polypeptide comprising mutations in the catalytic domain of the polypeptide relative to the catalytic domain of a wild type Cel7A polypeptide further comprises increased O-linked glycosylation of the linker domain relative to a linker domain of a wild type Cel7A polypeptide. The mutations in the catalytic domain reduce N-linked glycosylation of the isolated polypeptide relative to the wild type polypeptide. The addition of and/or substitution of one or more serine and/or threonine residues to the linker domain relative to the linker domain of the wild type polypeptide increases O-linked glycosylation of the isolated polypeptide. Further provided are compositions comprising such polypeptides and nucleic acids encoding such polypeptides. Still further provided are methods for making such polypeptides.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2014},
month = {1}
}

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