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Sökning: onr:"swepub:oai:lup.lub.lu.se:bd29e90b-6378-4e06-86fc-09b423b3602b" > The Catalytic Acid-...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003876naa a2200529 4500
001oai:lup.lub.lu.se:bd29e90b-6378-4e06-86fc-09b423b3602b
003SwePub
008200414s2020 | |||||||||||000 ||eng|
0247 a https://lup.lub.lu.se/record/bd29e90b-6378-4e06-86fc-09b423b3602b2 URI
0247 a https://doi.org/10.1021/acscatal.9b044742 DOI
040 a (SwePub)lu
041 a engb eng
042 9 SwePub
072 7a art2 swepub-publicationtype
072 7a ref2 swepub-contenttype
1001 a Teze, Davidu Technical University of Denmark4 aut
2451 0a 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
264 c 2020-02-11
264 1b American Chemical Society (ACS),c 2020
300 a 11 s.
520 a Enzymes active on glycosidic bonds are defined according to the stereochemistry of both substrates and products of the reactions they catalyze. The CAZy classification further assigns these enzymes into sequence-based families sharing a common stereochemistry for substrates (either α- or β-) and products (i.e., inverting or retaining mechanism). Here we describe the N-acetylgalactosaminidases AmGH109A and AmGH109B (i.e., GH109: glycoside hydrolase family 109) from the human gut symbiont Akkermansia muciniphila. Notably, AmGH109A displays α-retaining and β-inverting N-acetylgalactosaminidase activities with comparable efficiencies on natural disaccharides. This dual specificity could provide an advantage in targeting a broader range of host-derived glycans. We rationalize this discovery through bioinformatics, structural, mutational, and computational studies, unveiling a histidine residing in a conserved GGHGG motif as the elusive catalytic acid-base of the GH109 family.
650 7a TEKNIK OCH TEKNOLOGIERx Industriell bioteknikx Biokatalys och enzymteknik0 (SwePub)209062 hsv//swe
650 7a ENGINEERING AND TECHNOLOGYx Industrial Biotechnologyx Biocatalysis and Enzyme Technology0 (SwePub)209062 hsv//eng
653 a GH4
653 a glycoside hydrolase
653 a human gut microbiota
653 a inverting
653 a MD simulations
653 a mechanism
653 a mucin
653 a retaining
7001 a Shuoker, Basharu Lund University,Technical University of Denmark4 aut
7001 a Chaberski, Evan Kirku Technical University of Denmark4 aut
7001 a Kunstmann, Sonjau Technical University of Denmark4 aut
7001 a Fredslund, Folmeru Technical University of Denmark4 aut0 (Swepub:lu)maxl-ffl
7001 a Nielsen, Tine Sofieu Technical University of Denmark4 aut
7001 a Stender, Emil G.P.u Technical University of Denmark4 aut
7001 a Peters, Günther H.J.u Technical University of Denmark4 aut
7001 a Karlsson, Eva Nordbergu Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH4 aut0 (Swepub:lu)biot-eno
7001 a Welner, Ditte Hededamu Technical University of Denmark4 aut
7001 a Hachem, Maher Abouu Technical University of Denmark4 aut0 (Swepub:lu)biot-mah
7102 a Technical University of Denmarkb Lund University4 org
7730 t ACS Catalysisd : American Chemical Society (ACS)g 10:6, s. 3809-3819q 10:6<3809-3819x 2155-5435
8564 u http://dx.doi.org/10.1021/acscatal.9b04474y FULLTEXT
8564 u https://backend.orbit.dtu.dk/ws/files/200750707/TezeD_and_ShuokerB_GH109_ChemRxive.pdf
8564 8u https://lup.lub.lu.se/record/bd29e90b-6378-4e06-86fc-09b423b3602b
8564 8u https://doi.org/10.1021/acscatal.9b04474

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