WFRF:(Chaberski Evan Kirk)
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The catalytic acid-base in GH109 resides in a conserved GGHGG loop and allows for comparable α-retaining and β-inverting activity in an N-acetylgalactosaminidase from Akkermansia muciniphila
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- Teze, David (author)
- Technical University of Denmark
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- Shuoker, Bashar (author)
- Lund University
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- Chaberski, Evan Kirk (author)
- Novo Nordisk Foundation
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- (creator_code:org_t)
- American Chemical Society (ACS), 2019
- English.
- In: ChemRxiv. - : American Chemical Society (ACS).
- Other publication (other academic/artistic)
Abstract
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- The study describes the first glycoside hydrolase that exhibits comparable levels of activity on α- and β-linked saccharide substrates. This enzyme, assigned into GH109, is encoded by the genome of the human gut symbiont Akkermansia muciniphila that is a model primary degrader of the heavily O-glycosylated mucin glycoprotein that coats the epithelial enterocytes.The elusive catalytic acid/base catalyst in GH109 enzymes is identified as a histidine that is presented by a flexible loop that positions it for catalysis on both α- and β-substrates. This dual activity may be an evolutionary adaptation to extend the range of substrates targeted by a single non-canonical NAD+-dependant GH.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology (hsv//eng)
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- vet (subject category)
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