Engineering a monolignol 4-O-methyltransferase with high selectivity for the condensed lignin precursor coniferyl alcohol.
Identifieur interne : 001D92 ( Main/Exploration ); précédent : 001D91; suivant : 001D93Engineering a monolignol 4-O-methyltransferase with high selectivity for the condensed lignin precursor coniferyl alcohol.
Auteurs : Yuanheng Cai [États-Unis] ; Mohammad-Wadud Bhuiya [États-Unis] ; John Shanklin [États-Unis] ; Chang-Jun Liu [États-Unis]Source :
- The Journal of biological chemistry [ 1083-351X ] ; 2015.
Descripteurs français
- KwdFr :
- Banque de gènes (MeSH), Clonage moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Escherichia coli (génétique), Escherichia coli (métabolisme), Expression des gènes (MeSH), Ingénierie des protéines (MeSH), Lignine (composition chimique), Lignine (métabolisme), Methyltransferases (composition chimique), Methyltransferases (génétique), Methyltransferases (métabolisme), Mutation (MeSH), Paroi cellulaire (composition chimique), Paroi cellulaire (enzymologie), Paroi cellulaire (génétique), Phénols (composition chimique), Phénols (métabolisme), Phénylpropionates (composition chimique), Phénylpropionates (métabolisme), Plasmides (composition chimique), Plasmides (métabolisme), Populus (composition chimique), Populus (enzymologie), Populus (génétique), Propionates (composition chimique), Propionates (métabolisme), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (génétique), Protéines végétales (métabolisme), Similitude structurale de protéines (MeSH), Spécificité du substrat (MeSH), Substitution d'acide aminé (MeSH).
- MESH :
- composition chimique : Lignine, Methyltransferases, Paroi cellulaire, Phénols, Phénylpropionates, Plasmides, Populus, Propionates, Protéines recombinantes, Protéines végétales.
- enzymologie : Paroi cellulaire, Populus.
- génétique : Escherichia coli, Methyltransferases, Paroi cellulaire, Populus, Protéines recombinantes, Protéines végétales.
- métabolisme : Escherichia coli, Lignine, Methyltransferases, Phénols, Phénylpropionates, Plasmides, Propionates, Protéines recombinantes, Protéines végétales.
- Banque de gènes, Clonage moléculaire, Cristallographie aux rayons X, Expression des gènes, Ingénierie des protéines, Mutation, Similitude structurale de protéines, Spécificité du substrat, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution (MeSH), Cell Wall (chemistry), Cell Wall (enzymology), Cell Wall (genetics), Cloning, Molecular (MeSH), Crystallography, X-Ray (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression (MeSH), Gene Library (MeSH), Lignin (chemistry), Lignin (metabolism), Methyltransferases (chemistry), Methyltransferases (genetics), Methyltransferases (metabolism), Mutation (MeSH), Phenols (chemistry), Phenols (metabolism), Phenylpropionates (chemistry), Phenylpropionates (metabolism), Plant Proteins (chemistry), Plant Proteins (genetics), Plant Proteins (metabolism), Plasmids (chemistry), Plasmids (metabolism), Populus (chemistry), Populus (enzymology), Populus (genetics), Propionates (chemistry), Propionates (metabolism), Protein Engineering (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Structural Homology, Protein (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Lignin, Methyltransferases, Phenols, Phenylpropionates, Plant Proteins, Propionates, Recombinant Proteins.
- chemistry : Cell Wall, Plasmids, Populus.
- enzymology : Cell Wall, Populus.
- genetics : Cell Wall, Escherichia coli, Methyltransferases, Plant Proteins, Populus, Recombinant Proteins.
- metabolism : Escherichia coli, Lignin, Methyltransferases, Phenols, Phenylpropionates, Plant Proteins, Plasmids, Propionates, Recombinant Proteins.
- Amino Acid Substitution, Cloning, Molecular, Crystallography, X-Ray, Gene Expression, Gene Library, Mutation, Protein Engineering, Structural Homology, Protein, Substrate Specificity.
Abstract
Lignin, a rigid biopolymer in plant cell walls, is derived from the oxidative polymerization of three monolignols. The composition of monolignol monomers dictates the degree of lignin condensation, reactivity, and thus the degradability of plant cell walls. Guaiacyl lignin is regarded as the condensed structural unit. Polymerization of lignin is initiated through the deprotonation of the para-hydroxyl group of monolignols. Therefore, preferentially modifying the para-hydroxyl of a specific monolignol to deprive its dehydrogenation propensity would disturb the formation of particular lignin subunits. Here, we test the hypothesis that specific remodeling the active site of a monolignol 4-O-methyltransferase would create an enzyme that specifically methylates the condensed guaiacyl lignin precursor coniferyl alcohol. Combining crystal structural information with combinatorial active site saturation mutagenesis and starting with the engineered promiscuous enzyme, MOMT5 (T133L/E165I/F175I/F166W/H169F), we incrementally remodeled its substrate binding pocket by the addition of four substitutions, i.e. M26H, S30R, V33S, and T319M, yielding a mutant enzyme capable of discriminately etherifying the para-hydroxyl of coniferyl alcohol even in the presence of excess sinapyl alcohol. The engineered enzyme variant has a substantially reduced substrate binding pocket that imposes a clear steric hindrance thereby excluding bulkier lignin precursors. The resulting enzyme variant represents an excellent candidate for modulating lignin composition and/or structure in planta.
DOI: 10.1074/jbc.M115.684217
PubMed: 26378240
PubMed Central: PMC4646325
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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chimique)</term><term>Methyltransferases (génétique)</term><term>Methyltransferases (métabolisme)</term><term>Mutation (MeSH)</term><term>Paroi cellulaire (composition chimique)</term><term>Paroi cellulaire (enzymologie)</term><term>Paroi cellulaire (génétique)</term><term>Phénols (composition chimique)</term><term>Phénols (métabolisme)</term><term>Phénylpropionates (composition chimique)</term><term>Phénylpropionates (métabolisme)</term><term>Plasmides (composition chimique)</term><term>Plasmides (métabolisme)</term><term>Populus (composition chimique)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Propionates (composition chimique)</term><term>Propionates (métabolisme)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (métabolisme)</term><term>Similitude structurale de protéines (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Substitution d'acide aminé (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lignin</term><term>Methyltransferases</term><term>Phenols</term><term>Phenylpropionates</term><term>Plant Proteins</term><term>Propionates</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Wall</term><term>Plasmids</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Lignine</term><term>Methyltransferases</term><term>Paroi cellulaire</term><term>Phénols</term><term>Phénylpropionates</term><term>Plasmides</term><term>Populus</term><term>Propionates</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Paroi 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xml:lang="fr"><term>Escherichia coli</term><term>Lignine</term><term>Methyltransferases</term><term>Phénols</term><term>Phénylpropionates</term><term>Plasmides</term><term>Propionates</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Cloning, Molecular</term><term>Crystallography, X-Ray</term><term>Gene Expression</term><term>Gene Library</term><term>Mutation</term><term>Protein Engineering</term><term>Structural Homology, Protein</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Banque de gènes</term><term>Clonage moléculaire</term><term>Cristallographie aux rayons X</term><term>Expression des gènes</term><term>Ingénierie des protéines</term><term>Mutation</term><term>Similitude structurale de protéines</term><term>Spécificité du substrat</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin, a rigid biopolymer in plant cell walls, is derived from the oxidative polymerization of three monolignols. The composition of monolignol monomers dictates the degree of lignin condensation, reactivity, and thus the degradability of plant cell walls. Guaiacyl lignin is regarded as the condensed structural unit. Polymerization of lignin is initiated through the deprotonation of the para-hydroxyl group of monolignols. Therefore, preferentially modifying the para-hydroxyl of a specific monolignol to deprive its dehydrogenation propensity would disturb the formation of particular lignin subunits. Here, we test the hypothesis that specific remodeling the active site of a monolignol 4-O-methyltransferase would create an enzyme that specifically methylates the condensed guaiacyl lignin precursor coniferyl alcohol. Combining crystal structural information with combinatorial active site saturation mutagenesis and starting with the engineered promiscuous enzyme, MOMT5 (T133L/E165I/F175I/F166W/H169F), we incrementally remodeled its substrate binding pocket by the addition of four substitutions, i.e. M26H, S30R, V33S, and T319M, yielding a mutant enzyme capable of discriminately etherifying the para-hydroxyl of coniferyl alcohol even in the presence of excess sinapyl alcohol. The engineered enzyme variant has a substantially reduced substrate binding pocket that imposes a clear steric hindrance thereby excluding bulkier lignin precursors. The resulting enzyme variant represents an excellent candidate for modulating lignin composition and/or structure in planta. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26378240</PMID><DateCompleted><Year>2016</Year><Month>02</Month><Day>02</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>290</Volume><Issue>44</Issue><PubDate><Year>2015</Year><Month>Oct</Month><Day>30</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Engineering a monolignol 4-O-methyltransferase with high selectivity for the condensed lignin precursor coniferyl alcohol.</ArticleTitle><Pagination><MedlinePgn>26715-24</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M115.684217</ELocationID><Abstract><AbstractText>Lignin, a rigid biopolymer in plant cell walls, is derived from the oxidative polymerization of three monolignols. The composition of monolignol monomers dictates the degree of lignin condensation, reactivity, and thus the degradability of plant cell walls. Guaiacyl lignin is regarded as the condensed structural unit. Polymerization of lignin is initiated through the deprotonation of the para-hydroxyl group of monolignols. Therefore, preferentially modifying the para-hydroxyl of a specific monolignol to deprive its dehydrogenation propensity would disturb the formation of particular lignin subunits. Here, we test the hypothesis that specific remodeling the active site of a monolignol 4-O-methyltransferase would create an enzyme that specifically methylates the condensed guaiacyl lignin precursor coniferyl alcohol. Combining crystal structural information with combinatorial active site saturation mutagenesis and starting with the engineered promiscuous enzyme, MOMT5 (T133L/E165I/F175I/F166W/H169F), we incrementally remodeled its substrate binding pocket by the addition of four substitutions, i.e. M26H, S30R, V33S, and T319M, yielding a mutant enzyme capable of discriminately etherifying the para-hydroxyl of coniferyl alcohol even in the presence of excess sinapyl alcohol. The engineered enzyme variant has a substantially reduced substrate binding pocket that imposes a clear steric hindrance thereby excluding bulkier lignin precursors. The resulting enzyme variant represents an excellent candidate for modulating lignin composition and/or structure in planta. </AbstractText><CopyrightInformation>© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cai</LastName><ForeName>Yuanheng</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>From the Biological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York 11973.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhuiya</LastName><ForeName>Mohammad-Wadud</ForeName><Initials>MW</Initials><AffiliationInfo><Affiliation>From the Biological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York 11973.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shanklin</LastName><ForeName>John</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>From the Biological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York 11973.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Chang-Jun</ForeName><Initials>CJ</Initials><AffiliationInfo><Affiliation>From the Biological, Environmental, and Climate Sciences Department, Brookhaven National Laboratory, Upton, New York 11973 cliu@bnl.gov.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>3P9I</AccessionNumber><AccessionNumber>3TKY</AccessionNumber><AccessionNumber>5CVJ</AccessionNumber><AccessionNumber>5CVU</AccessionNumber><AccessionNumber>5CVV</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>09</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010636">Phenols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010666">Phenylpropionates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011422">Propionates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>8O6NO04SMV</RegistryNumber><NameOfSubstance UI="C496130">sinapyl alcohol</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>E7SM92591P</RegistryNumber><NameOfSubstance UI="C010559">coniferyl alcohol</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>IBS9D1EU3J</RegistryNumber><NameOfSubstance UI="C495469">trans-3-(4'-hydroxyphenyl)-2-propenoic acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName><QualifierName UI="Q000737" 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IdType="pii">M115.684217</ArticleId><ArticleId IdType="doi">10.1074/jbc.M115.684217</ArticleId><ArticleId IdType="pmc">PMC4646325</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Nucleic Acids Res. 2010 Jul;38(Web Server issue):W555-62</Citation><ArticleIdList><ArticleId IdType="pubmed">20478824</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Chem Biol. 2011 Apr;15(2):194-200</Citation><ArticleIdList><ArticleId IdType="pubmed">21115265</ArticleId></ArticleIdList></Reference><Reference><Citation>Nucleic Acids Res. 2009 Jan;37(Database issue):D387-92</Citation><ArticleIdList><ArticleId IdType="pubmed">18931379</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Chem. 2011 Sep;3(9):738-43</Citation><ArticleIdList><ArticleId IdType="pubmed">21860465</ArticleId></ArticleIdList></Reference><Reference><Citation>J Agric Food Chem. 2003 Oct 8;51(21):6178-83</Citation><ArticleIdList><ArticleId IdType="pubmed">14518941</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods Mol Biol. 2014;1179:103-28</Citation><ArticleIdList><ArticleId IdType="pubmed">25055773</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501</Citation><ArticleIdList><ArticleId IdType="pubmed">20383002</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioinformatics. 2006 Jan 15;22(2):195-201</Citation><ArticleIdList><ArticleId IdType="pubmed">16301204</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Plant Biol. 2008 Jun;11(3):278-85</Citation><ArticleIdList><ArticleId IdType="pubmed">18434238</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Biol. 2007 Feb 20;17(4):R115-9</Citation><ArticleIdList><ArticleId IdType="pubmed">17307040</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Biotechnol. 2013 Apr;24(2):336-43</Citation><ArticleIdList><ArticleId IdType="pubmed">23228388</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 2010 Dec;22(12):4114-27</Citation><ArticleIdList><ArticleId IdType="pubmed">21177481</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2010 Jan 1;285(1):277-85</Citation><ArticleIdList><ArticleId IdType="pubmed">19875443</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2011 Apr 12;108(15):6300-5</Citation><ArticleIdList><ArticleId IdType="pubmed">21444820</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 2004 Feb;134(2):586-94</Citation><ArticleIdList><ArticleId IdType="pubmed">14730080</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Plant Biol. 2003;54:519-46</Citation><ArticleIdList><ArticleId IdType="pubmed">14503002</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 2002 Jun;14(6):1265-77</Citation><ArticleIdList><ArticleId IdType="pubmed">12084826</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1999 Aug 1;368(1):172-80</Citation><ArticleIdList><ArticleId IdType="pubmed">10415125</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 2006 Dec;18(12):3656-69</Citation><ArticleIdList><ArticleId IdType="pubmed">17172354</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 2012 Jul;24(7):3135-52</Citation><ArticleIdList><ArticleId IdType="pubmed">22851762</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1131-7</Citation><ArticleIdList><ArticleId IdType="pubmed">12832755</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1999 Jan;119(1):153-64</Citation><ArticleIdList><ArticleId IdType="pubmed">9880356</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Chem Biol. 2009 Feb;13(1):3-9</Citation><ArticleIdList><ArticleId IdType="pubmed">19249235</ArticleId></ArticleIdList></Reference><Reference><Citation>Angew Chem Int Ed Engl. 2005 Jul 4;44(27):4192-6</Citation><ArticleIdList><ArticleId IdType="pubmed">15929154</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant J. 2009 May;58(4):706-14</Citation><ArticleIdList><ArticleId IdType="pubmed">19175772</ArticleId></ArticleIdList></Reference><Reference><Citation>Methods. 2013 Mar 15;60(1):81-90</Citation><ArticleIdList><ArticleId IdType="pubmed">22465795</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Sci. 2011 Oct;181(4):379-86</Citation><ArticleIdList><ArticleId IdType="pubmed">21889043</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Chem Biol. 2006 Oct;10(5):498-508</Citation><ArticleIdList><ArticleId IdType="pubmed">16939713</ArticleId></ArticleIdList></Reference><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):355-67</Citation><ArticleIdList><ArticleId IdType="pubmed">21460454</ArticleId></ArticleIdList></Reference><Reference><Citation>World J Microbiol Biotechnol. 2013 Apr;29(4):667-72</Citation><ArticleIdList><ArticleId IdType="pubmed">23225176</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 2010 May;22(5):1620-32</Citation><ArticleIdList><ArticleId IdType="pubmed">20511296</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Protoc. 2007;2(4):891-903</Citation><ArticleIdList><ArticleId IdType="pubmed">17446890</ArticleId></ArticleIdList></Reference><Reference><Citation>Chemistry. 2006 Aug 7;12(23):6031-8</Citation><ArticleIdList><ArticleId IdType="pubmed">16789057</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Biotechnol J. 2014 Dec;12(9):1154-62</Citation><ArticleIdList><ArticleId IdType="pubmed">25209835</ArticleId></ArticleIdList></Reference><Reference><Citation>Chembiochem. 2008 Jul 21;9(11):1797-804</Citation><ArticleIdList><ArticleId IdType="pubmed">18567049</ArticleId></ArticleIdList></Reference><Reference><Citation>Electrophoresis. 2009 Jun;30 Suppl 1:S162-73</Citation><ArticleIdList><ArticleId IdType="pubmed">19517507</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1998 Jan 1;349(1):153-60</Citation><ArticleIdList><ArticleId IdType="pubmed">9439593</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="Cai, Yuanheng" sort="Cai, Yuanheng" uniqKey="Cai Y" first="Yuanheng" last="Cai">Yuanheng Cai</name></region><name sortKey="Bhuiya, Mohammad Wadud" sort="Bhuiya, Mohammad Wadud" uniqKey="Bhuiya M" first="Mohammad-Wadud" last="Bhuiya">Mohammad-Wadud Bhuiya</name><name sortKey="Liu, Chang Jun" sort="Liu, Chang Jun" uniqKey="Liu C" first="Chang-Jun" last="Liu">Chang-Jun 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