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Title: Variants of glycoside hydrolases

Abstract

The present invention relates to variants of a parent glycoside hydrolase, comprising a substitution at one or more positions corresponding to positions 21, 94, 157, 205, 206, 247, 337, 350, 373, 383, 438, 455, 467, and 486 of amino acids 1 to 513 of SEQ ID NO: 2, and optionally further comprising a substitution at one or more positions corresponding to positions 8, 22, 41, 49, 57, 113, 193, 196, 226, 227, 246, 251, 255, 259, 301, 356, 371, 411, and 462 of amino acids 1 to 513 of SEQ ID NO: 2 a substitution at one or more positions corresponding to positions 8, 22, 41, 49, 57, 113, 193, 196, 226, 227, 246, 251, 255, 259, 301, 356, 371, 411, and 462 of amino acids 1 to 513 of SEQ ID NO: 2, wherein the variants have glycoside hydrolase activity. The present invention also relates to nucleotide sequences encoding the variant glycoside hydrolases and to nucleic acid constructs, vectors, and host cells comprising the nucleotide sequences.

Inventors:
 [1];  [2];  [1];  [1];  [3];  [4]
  1. Davis, CA
  2. Hamilton, MT
  3. Carnation, WA
  4. Sacramento, CA
Issue Date:
Research Org.:
Novozymes, Inc. (Davis, CA)
Sponsoring Org.:
USDOE
OSTI Identifier:
1016673
Patent Number(s):
7,932,073
Application Number:
US Patent Application 11/891,249
Assignee:
Novozymes, Inc. (Davis, CA)
DOE Contract Number:  
AC36-98GO10337
Resource Type:
Patent
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Teter, Sarah, Ward, Connie, Cherry, Joel, Jones, Aubrey, Harris, Paul, and Yi, Jung. Variants of glycoside hydrolases. United States: N. p., 2011. Web.
Teter, Sarah, Ward, Connie, Cherry, Joel, Jones, Aubrey, Harris, Paul, & Yi, Jung. Variants of glycoside hydrolases. United States.
Teter, Sarah, Ward, Connie, Cherry, Joel, Jones, Aubrey, Harris, Paul, and Yi, Jung. Tue . "Variants of glycoside hydrolases". United States. https://www.osti.gov/servlets/purl/1016673.
@article{osti_1016673,
title = {Variants of glycoside hydrolases},
author = {Teter, Sarah and Ward, Connie and Cherry, Joel and Jones, Aubrey and Harris, Paul and Yi, Jung},
abstractNote = {The present invention relates to variants of a parent glycoside hydrolase, comprising a substitution at one or more positions corresponding to positions 21, 94, 157, 205, 206, 247, 337, 350, 373, 383, 438, 455, 467, and 486 of amino acids 1 to 513 of SEQ ID NO: 2, and optionally further comprising a substitution at one or more positions corresponding to positions 8, 22, 41, 49, 57, 113, 193, 196, 226, 227, 246, 251, 255, 259, 301, 356, 371, 411, and 462 of amino acids 1 to 513 of SEQ ID NO: 2 a substitution at one or more positions corresponding to positions 8, 22, 41, 49, 57, 113, 193, 196, 226, 227, 246, 251, 255, 259, 301, 356, 371, 411, and 462 of amino acids 1 to 513 of SEQ ID NO: 2, wherein the variants have glycoside hydrolase activity. The present invention also relates to nucleotide sequences encoding the variant glycoside hydrolases and to nucleic acid constructs, vectors, and host cells comprising the nucleotide sequences.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {2011},
month = {4}
}

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Works referenced in this record:

Activity Studies and Crystal Structures of Catalytically Deficient Mutants of Cellobiohydrolase I fromTrichoderma reesei
journal, November 1996

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Structural basis for enantiomer binding and separation of a common β-blocker: crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 Å resolution
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Molecular cloning and sequence analysis of the cellobiohydrolase i gene fromTrichoderma koningii G-39
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