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"Newton's cradle" proton relay with amide-imidic acid tautomerization in inverting cellulase visualized by neutron crystallography.

Identifieur interne : 000286 ( Main/Exploration ); précédent : 000285; suivant : 000287

"Newton's cradle" proton relay with amide-imidic acid tautomerization in inverting cellulase visualized by neutron crystallography.

Auteurs : Akihiko Nakamura [Japon] ; Takuya Ishida [Japon] ; Katsuhiro Kusaka [Japon] ; Taro Yamada [Japon] ; Shinya Fushinobu [Japon] ; Ichiro Tanaka [Japon] ; Satoshi Kaneko [Japon] ; Kazunori Ohta [Japon] ; Hiroaki Tanaka [Japon] ; Koji Inaka [Japon] ; Yoshiki Higuchi [Japon] ; Nobuo Niimura [Japon] ; Masahiro Samejima [Japon] ; Kiyohiko Igarashi [Japon]

Source :

RBID : pubmed:26601228

Abstract

Hydrolysis of carbohydrates is a major bioreaction in nature, catalyzed by glycoside hydrolases (GHs). We used neutron diffraction and high-resolution x-ray diffraction analyses to investigate the hydrogen bond network in inverting cellulase PcCel45A, which is an endoglucanase belonging to subfamily C of GH family 45, isolated from the basidiomycete Phanerochaete chrysosporium. Examination of the enzyme and enzyme-ligand structures indicates a key role of multiple tautomerizations of asparagine residues and peptide bonds, which are finally connected to the other catalytic residue via typical side-chain hydrogen bonds, in forming the "Newton's cradle"-like proton relay pathway of the catalytic cycle. Amide-imidic acid tautomerization of asparagine has not been taken into account in recent molecular dynamics simulations of not only cellulases but also general enzyme catalysis, and it may be necessary to reconsider our interpretation of many enzymatic reactions.

DOI: 10.1126/sciadv.1500263
PubMed: 26601228
PubMed Central: PMC4643802


Affiliations:


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<div type="abstract" xml:lang="en">Hydrolysis of carbohydrates is a major bioreaction in nature, catalyzed by glycoside hydrolases (GHs). We used neutron diffraction and high-resolution x-ray diffraction analyses to investigate the hydrogen bond network in inverting cellulase PcCel45A, which is an endoglucanase belonging to subfamily C of GH family 45, isolated from the basidiomycete Phanerochaete chrysosporium. Examination of the enzyme and enzyme-ligand structures indicates a key role of multiple tautomerizations of asparagine residues and peptide bonds, which are finally connected to the other catalytic residue via typical side-chain hydrogen bonds, in forming the "Newton's cradle"-like proton relay pathway of the catalytic cycle. Amide-imidic acid tautomerization of asparagine has not been taken into account in recent molecular dynamics simulations of not only cellulases but also general enzyme catalysis, and it may be necessary to reconsider our interpretation of many enzymatic reactions. </div>
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<AbstractText>Hydrolysis of carbohydrates is a major bioreaction in nature, catalyzed by glycoside hydrolases (GHs). We used neutron diffraction and high-resolution x-ray diffraction analyses to investigate the hydrogen bond network in inverting cellulase PcCel45A, which is an endoglucanase belonging to subfamily C of GH family 45, isolated from the basidiomycete Phanerochaete chrysosporium. Examination of the enzyme and enzyme-ligand structures indicates a key role of multiple tautomerizations of asparagine residues and peptide bonds, which are finally connected to the other catalytic residue via typical side-chain hydrogen bonds, in forming the "Newton's cradle"-like proton relay pathway of the catalytic cycle. Amide-imidic acid tautomerization of asparagine has not been taken into account in recent molecular dynamics simulations of not only cellulases but also general enzyme catalysis, and it may be necessary to reconsider our interpretation of many enzymatic reactions. </AbstractText>
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<LastName>Nakamura</LastName>
<ForeName>Akihiko</ForeName>
<Initials>A</Initials>
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<Affiliation>Department of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan.</Affiliation>
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<LastName>Ishida</LastName>
<ForeName>Takuya</ForeName>
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<ForeName>Katsuhiro</ForeName>
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</AffiliationInfo>
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<ForeName>Shinya</ForeName>
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<ForeName>Nobuo</ForeName>
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<ForeName>Masahiro</ForeName>
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<ForeName>Kiyohiko</ForeName>
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<PublicationType UI="D016428">Journal Article</PublicationType>
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<ArticleDate DateType="Electronic">
<Year>2015</Year>
<Month>08</Month>
<Day>21</Day>
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<Keyword MajorTopicYN="N">Carbohydrate Active enZymes</Keyword>
<Keyword MajorTopicYN="N">Cellulase</Keyword>
<Keyword MajorTopicYN="N">Neutron crystallography</Keyword>
<Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword>
<Keyword MajorTopicYN="N">Proton relay</Keyword>
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