Active site and laminarin binding in glycoside hydrolase family 55.
Identifieur interne : 000284 ( Main/Exploration ); précédent : 000283; suivant : 000285Active site and laminarin binding in glycoside hydrolase family 55.
Auteurs : Christopher M. Bianchetti [États-Unis] ; Taichi E. Takasuka [Japon] ; Sam Deutsch ; Hannah S. Udell [États-Unis] ; Eric J. Yik [États-Unis] ; Lai F. Bergeman [États-Unis] ; Brian G. Fox [États-Unis]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2015.
Descripteurs français
- KwdFr :
- Biologie informatique (MeSH), Catalyse (MeSH), Concentration en ions d'hydrogène (MeSH), Cristallographie aux rayons X (MeSH), Domaine catalytique (MeSH), Eau (composition chimique), Escherichia coli (métabolisme), Glucanes (composition chimique), Glycosidases (composition chimique), Hydrolyse (MeSH), Liaison aux protéines (MeSH), Modèles moléculaires (MeSH), Mutagenèse (MeSH), Mutation (MeSH), Phanerochaete (enzymologie), Phylogenèse (MeSH), Polyosides (composition chimique), Protéines bactériennes (composition chimique), Streptomyces (enzymologie).
- MESH :
- composition chimique : Eau, Glucanes, Glycosidases, Polyosides, Protéines bactériennes.
- enzymologie : Phanerochaete, Streptomyces.
- métabolisme : Escherichia coli.
- Biologie informatique, Catalyse, Concentration en ions d'hydrogène, Cristallographie aux rayons X, Domaine catalytique, Hydrolyse, Liaison aux protéines, Modèles moléculaires, Mutagenèse, Mutation, Phylogenèse.
English descriptors
- KwdEn :
- Bacterial Proteins (chemistry), Catalysis (MeSH), Catalytic Domain (MeSH), Computational Biology (MeSH), Crystallography, X-Ray (MeSH), Escherichia coli (metabolism), Glucans (chemistry), Glycoside Hydrolases (chemistry), Hydrogen-Ion Concentration (MeSH), Hydrolysis (MeSH), Models, Molecular (MeSH), Mutagenesis (MeSH), Mutation (MeSH), Phanerochaete (enzymology), Phylogeny (MeSH), Polysaccharides (chemistry), Protein Binding (MeSH), Streptomyces (enzymology), Water (chemistry).
- MESH :
- chemical , chemistry : Bacterial Proteins, Glucans, Glycoside Hydrolases, Polysaccharides, Water.
- enzymology : Phanerochaete, Streptomyces.
- metabolism : Escherichia coli.
- Catalysis, Catalytic Domain, Computational Biology, Crystallography, X-Ray, Hydrogen-Ion Concentration, Hydrolysis, Models, Molecular, Mutagenesis, Mutation, Phylogeny, Protein Binding.
Abstract
The Carbohydrate Active Enzyme (CAZy) database indicates that glycoside hydrolase family 55 (GH55) contains both endo- and exo-β-1,3-glucanases. The founding structure in the GH55 is PcLam55A from the white rot fungus Phanerochaete chrysosporium (Ishida, T., Fushinobu, S., Kawai, R., Kitaoka, M., Igarashi, K., and Samejima, M. (2009) Crystal structure of glycoside hydrolase family 55 β-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium. J. Biol. Chem. 284, 10100-10109). Here, we present high resolution crystal structures of bacterial SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E with bound substrates and product. These structures, along with mutagenesis and kinetic studies, implicate Glu-502 as the catalytic acid (as proposed earlier for Glu-663 in PcLam55A) and a proton relay network of four residues in activating water as the nucleophile. Further, a set of conserved aromatic residues that define the active site apparently enforce an exo-glucanase reactivity as demonstrated by exhaustive hydrolysis reactions with purified laminarioligosaccharides. Two additional aromatic residues that line the substrate-binding channel show substrate-dependent conformational flexibility that may promote processive reactivity of the bound oligosaccharide in the bacterial enzymes. Gene synthesis carried out on ∼30% of the GH55 family gave 34 active enzymes (19% functional coverage of the nonredundant members of GH55). These active enzymes reacted with only laminarin from a panel of 10 different soluble and insoluble polysaccharides and displayed a broad range of specific activities and optima for pH and temperature. Application of this experimental method provides a new, systematic way to annotate glycoside hydrolase phylogenetic space for functional properties.
DOI: 10.1074/jbc.M114.623579
PubMed: 25752603
PubMed Central: PMC4424323
Affiliations:
Links toward previous steps (curation, corpus...)
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<term>Catalytic Domain (MeSH)</term>
<term>Computational Biology (MeSH)</term>
<term>Crystallography, X-Ray (MeSH)</term>
<term>Escherichia coli (metabolism)</term>
<term>Glucans (chemistry)</term>
<term>Glycoside Hydrolases (chemistry)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Hydrolysis (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Mutagenesis (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phylogeny (MeSH)</term>
<term>Polysaccharides (chemistry)</term>
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<term>Streptomyces (enzymology)</term>
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<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Cristallographie aux rayons X (MeSH)</term>
<term>Domaine catalytique (MeSH)</term>
<term>Eau (composition chimique)</term>
<term>Escherichia coli (métabolisme)</term>
<term>Glucanes (composition chimique)</term>
<term>Glycosidases (composition chimique)</term>
<term>Hydrolyse (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mutagenèse (MeSH)</term>
<term>Mutation (MeSH)</term>
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<term>Glycoside Hydrolases</term>
<term>Polysaccharides</term>
<term>Water</term>
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<term>Glucanes</term>
<term>Glycosidases</term>
<term>Polyosides</term>
<term>Protéines bactériennes</term>
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<front><div type="abstract" xml:lang="en">The Carbohydrate Active Enzyme (CAZy) database indicates that glycoside hydrolase family 55 (GH55) contains both endo- and exo-β-1,3-glucanases. The founding structure in the GH55 is PcLam55A from the white rot fungus Phanerochaete chrysosporium (Ishida, T., Fushinobu, S., Kawai, R., Kitaoka, M., Igarashi, K., and Samejima, M. (2009) Crystal structure of glycoside hydrolase family 55 β-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium. J. Biol. Chem. 284, 10100-10109). Here, we present high resolution crystal structures of bacterial SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E with bound substrates and product. These structures, along with mutagenesis and kinetic studies, implicate Glu-502 as the catalytic acid (as proposed earlier for Glu-663 in PcLam55A) and a proton relay network of four residues in activating water as the nucleophile. Further, a set of conserved aromatic residues that define the active site apparently enforce an exo-glucanase reactivity as demonstrated by exhaustive hydrolysis reactions with purified laminarioligosaccharides. Two additional aromatic residues that line the substrate-binding channel show substrate-dependent conformational flexibility that may promote processive reactivity of the bound oligosaccharide in the bacterial enzymes. Gene synthesis carried out on ∼30% of the GH55 family gave 34 active enzymes (19% functional coverage of the nonredundant members of GH55). These active enzymes reacted with only laminarin from a panel of 10 different soluble and insoluble polysaccharides and displayed a broad range of specific activities and optima for pH and temperature. Application of this experimental method provides a new, systematic way to annotate glycoside hydrolase phylogenetic space for functional properties. </div>
</front>
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<DateCompleted><Year>2015</Year>
<Month>08</Month>
<Day>03</Day>
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<Title>The Journal of biological chemistry</Title>
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<ArticleTitle>Active site and laminarin binding in glycoside hydrolase family 55.</ArticleTitle>
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<Abstract><AbstractText>The Carbohydrate Active Enzyme (CAZy) database indicates that glycoside hydrolase family 55 (GH55) contains both endo- and exo-β-1,3-glucanases. The founding structure in the GH55 is PcLam55A from the white rot fungus Phanerochaete chrysosporium (Ishida, T., Fushinobu, S., Kawai, R., Kitaoka, M., Igarashi, K., and Samejima, M. (2009) Crystal structure of glycoside hydrolase family 55 β-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium. J. Biol. Chem. 284, 10100-10109). Here, we present high resolution crystal structures of bacterial SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E with bound substrates and product. These structures, along with mutagenesis and kinetic studies, implicate Glu-502 as the catalytic acid (as proposed earlier for Glu-663 in PcLam55A) and a proton relay network of four residues in activating water as the nucleophile. Further, a set of conserved aromatic residues that define the active site apparently enforce an exo-glucanase reactivity as demonstrated by exhaustive hydrolysis reactions with purified laminarioligosaccharides. Two additional aromatic residues that line the substrate-binding channel show substrate-dependent conformational flexibility that may promote processive reactivity of the bound oligosaccharide in the bacterial enzymes. Gene synthesis carried out on ∼30% of the GH55 family gave 34 active enzymes (19% functional coverage of the nonredundant members of GH55). These active enzymes reacted with only laminarin from a panel of 10 different soluble and insoluble polysaccharides and displayed a broad range of specific activities and optima for pH and temperature. Application of this experimental method provides a new, systematic way to annotate glycoside hydrolase phylogenetic space for functional properties. </AbstractText>
<CopyrightInformation>© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bianchetti</LastName>
<ForeName>Christopher M</ForeName>
<Initials>CM</Initials>
<AffiliationInfo><Affiliation>From the Great Lakes Bioenergy Research Center, University of Wisconsin-Madison, Madison, Wisconsin 53706, the Department of Chemistry, University of Wisconsin-Oshkosh, Oshkosh, Wisconsin 54901.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Takasuka</LastName>
<ForeName>Taichi E</ForeName>
<Initials>TE</Initials>
<AffiliationInfo><Affiliation>From the Great Lakes Bioenergy Research Center, University of Wisconsin-Madison, Madison, Wisconsin 53706, the Research Faculty of Agriculture, Hokkaido University, Sapporo, 060-8589, Japan.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Deutsch</LastName>
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<Initials>S</Initials>
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<ForeName>Eric J</ForeName>
<Initials>EJ</Initials>
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<Author ValidYN="Y"><LastName>Bergeman</LastName>
<ForeName>Lai F</ForeName>
<Initials>LF</Initials>
<AffiliationInfo><Affiliation>From the Great Lakes Bioenergy Research Center, University of Wisconsin-Madison, Madison, Wisconsin 53706.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fox</LastName>
<ForeName>Brian G</ForeName>
<Initials>BG</Initials>
<AffiliationInfo><Affiliation>From the Great Lakes Bioenergy Research Center, University of Wisconsin-Madison, Madison, Wisconsin 53706, bgfox@biochem.wisc.edu.</Affiliation>
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<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
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<ArticleIdList><ArticleId IdType="pubmed">25752603</ArticleId>
<ArticleId IdType="pii">M114.623579</ArticleId>
<ArticleId IdType="doi">10.1074/jbc.M114.623579</ArticleId>
<ArticleId IdType="pmc">PMC4424323</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Curr Opin Chem Biol. 2000 Oct;4(5):573-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11006547</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Appl Environ Microbiol. 2001 Feb;67(2):865-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11157256</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Gene. 2001 Oct 17;277(1-2):199-208</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11602357</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Prog Biophys Mol Biol. 2001 Oct;77(2):111-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11747907</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Genet. 2002 Mar;40(6):374-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11919676</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2002 Aug 28;124(34):10015-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12188666</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2003 Jul 1;31(13):3784-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12824418</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biosci Biotechnol Biochem. 2003 Jun;67(6):1349-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12843664</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2003 Nov;59(Pt 11):1966-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14573951</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2004 Sep 15;382(Pt 3):769-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15214846</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biosci Biotechnol Biochem. 2004 Oct;68(10):2111-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15502357</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15572765</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biotechnol Lett. 2006 Mar;28(6):365-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16614901</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Bioorg Med Chem Lett. 2007 Jul 1;17(13):3702-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17475486</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biotechnol Prog. 2007 May-Jun;23(3):585-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17506520</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Expr Purif. 2007 Sep;55(1):53-68</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17543538</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biosci Biotechnol Biochem. 2007 Jun;71(6):1568-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17587693</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2007 Sep 21;372(3):774-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17681537</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1983 Jun 10;220(4602):1161-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17818500</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2007 Oct 19;373(2):337-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17822716</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Structure. 2007 Sep;15(9):1040-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17850744</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Microbiol. 2007 Oct;66(2):279-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17854405</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteins. 2008 May 1;71(2):982-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18004753</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2007 Nov 22;450(7169):560-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18033299</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2008 Jan;36(Database issue):D190-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18045787</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2008 Jan;64(Pt 1):61-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18094468</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2009 Jan;37(Database issue):D233-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18838391</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2008 Dec 26;283(52):36328-37</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18981178</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Mol Biol. 2009;498:55-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18988018</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2009 Apr 10;284(15):10100-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19193645</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Int J Syst Evol Microbiol. 2009 Feb;59(Pt 2):275-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19196765</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2009 Apr 17;284(16):10610-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19244232</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Protoc Protein Sci. 2009 Apr;Chapter 5:Unit 5.23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19365792</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19461840</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):582-601</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19465773</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS J. 2009 Jul;276(14):3837-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19523117</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2009 Sep 25;284(39):26708-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19640850</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Plant Signal Behav. 2009 Jun;4(6):489-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19816126</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20057044</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20124702</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2010 May;38(8):2603-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20211837</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biotechnol Bioeng. 2010 Oct 1;107(2):195-205</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20552664</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>ISME J. 2011 Aug;5(8):1323-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21368904</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 2011;498:349-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21601685</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Methods. 2011 Sep 29;8(10):785-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21959131</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2011 Nov 25;286(47):41028-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21965672</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>ISME J. 2012 Sep;6(9):1688-701</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22378535</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Elife. 2012 Dec 18;1:e00311</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23251785</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):52-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23275163</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Sci Rep. 2013;3:1030</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23301151</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2013 May 10;288(19):13503-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23532843</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Phys Chem B. 2013 May 2;117(17):4924-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23534900</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2013 Jun 21;288(25):18574-87</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23653358</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Antibiot (Tokyo). 2014 Jan;67(1):53-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23921819</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Mol Biol. 2014;1079:105-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24170397</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2014 Jan 24;289(4):2027-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24337571</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Mol Biol. 2014;1118:71-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24395410</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2014 Apr 07;9(4):e94166</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24710170</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Appl Environ Microbiol. 2014 Aug;80(15):4692-701</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24837391</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Environ Microbiol Rep. 2014 Aug;6(4):389-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24992538</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biotechnol Biofuels. 2014 Aug 06;7:109</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25161697</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Front Plant Sci. 2014 Sep 16;5:470</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25278948</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>MBio. 2014 Nov 18;5(6):e02077</Citation>
<ArticleIdList><ArticleId IdType="pubmed">25406380</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Bacteriol. 1995 Dec;177(23):6937-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7592488</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Opin Struct Biol. 1994 Dec;4(6):885-92</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7712292</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1995 Feb 21;34(7):2220-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7857933</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Appl Environ Microbiol. 1994 Feb;60(2):594-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8135518</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Carbohydr Res. 1996 Feb 23;281(2):187-201</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8721145</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 1997 Jan 15;321 ( Pt 2):557-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9020895</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Gene. 1999 Jan 21;226(2):147-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9931476</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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