Folmer Fredslund

Technical University of Denmark

Denmark

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Articles (10)

Year:

2022

Year:

2022

Year:

2022

Year:

2021

Year:

2021

Year:

2021

Year:

2021

Year:

2020

Year:

2020

Year:

2020

Collaborators (12)

Cecilie Cetti Hansen

Københavns Universitet

DENMARK

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Bastien Bissaro

Aix-Marseille University

FRANCE

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David Teze

Technical University of Denmark

DENMARK

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Phillip Lowe

University of St. Andrews

UNITED KINGDOM

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Christian Kjeldsen

Technical University of Denmark

DENMARK

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Ditte Hededam Welner

Technical University of Denmark

DENMARK

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Tomas Laursen

Københavns Universitet

DENMARK

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Manuel Nieto-Domínguez

Technical University of Denmark

DENMARK

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Bruna Marques dos Santos

Københavns Universitet

DENMARK

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Rita Del Giudice

SWEDEN

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Natalia Putkaradze

Technical University of Denmark

DENMARK

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Jens Øllgaard Duus

Technical University of Denmark

DENMARK

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Folmer Fredslund

Research Interests

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Articles (10)

Family 1 Glycosyltransferase UGT706F8 from Zea mays Selectively Catalyzes the Synthesis of Silibinin 7-O-β-d-Glucoside

Oligomerization engineering of the fluorinase enzyme leads to an active trimer that supports synthesis of fluorometabolites in vitro

Structure-guided engineering of key amino acids in UGT85B1 controlling substrate and stereo-specificity in aromatic cyanogenic glucoside biosynthesis

O-/N-/S-Specificity in Glycosyltransferase Catalysis: From Mechanistic Understanding to Engineering

Discovery of fungal oligosaccharide-oxidising flavo-enzymes with previously unknown substrates, redox-activity profiles and interplay with LPMOs

Natural product C-glycosyltransferases – a scarcely characterised enzymatic activity with biotechnological potential

Natural product C-glycosyltransferases - a scarcely characterised enzymatic activity with biotechnological potential

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”

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

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

Collaborators (12)

Cecilie Cetti Hansen

Bastien Bissaro

David Teze

Phillip Lowe

Christian Kjeldsen

Ditte Hededam Welner

Tomas Laursen

Manuel Nieto-Domínguez

Bruna Marques dos Santos

Rita Del Giudice

Natalia Putkaradze

Jens Øllgaard Duus

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