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2020年2月11日 · 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.

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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.

2019年10月21日 · 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 [opens in a new tab]

2020年9月30日 · Correction to “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”

We rationalise 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. KEYWORDS: glycoside hydrolase, human gut microbiota, inverting, mechanism, MD simulations, mucin, retaining, structure.

2020年2月11日 · We rationalise this discovery through bioinformatics, structural, mutational, and computational studies, unveiling a histidine residing in a conserved GGHGG motif as the elusive catalytic acid ...

We rationalise this discovery through bioinformatics, structural, mutational, and computational studies, unveiling a histidine residing in a conserved GGHGG motif as the elusive catalytic acidbase of the GH109 family.

Request PDF | On Oct 16, 2020, David Teze and others published Correction to “The Catalytic Acid–Base in GH109 Resides in a Conserved GGHGG Loop and Allows for Comparable α-Retaining and β ...