GDP-Mannose 3,5-Epimerase: A View on Structure, Mechanism, and Industrial Potential

GDP-mannose 3,5-epimerase (GM35E, GME) belongs to the short-chain dehydrogenase/reductase (SDR) protein superfamily and catalyses the conversion of GDP-d-mannose towards GDP-l-galactose. Although the overall reaction seems relatively simple (a double epimerization), the enzyme needs to orchestrate a...

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Main Authors: Koen Beerens, Ophelia Gevaert, Tom Desmet
Format: Article
Language:English
Published: Frontiers Media S.A. 2022-01-01
Series:Frontiers in Molecular Biosciences
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fmolb.2021.784142/full
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author Koen Beerens
Ophelia Gevaert
Tom Desmet
author_facet Koen Beerens
Ophelia Gevaert
Tom Desmet
author_sort Koen Beerens
collection DOAJ
description GDP-mannose 3,5-epimerase (GM35E, GME) belongs to the short-chain dehydrogenase/reductase (SDR) protein superfamily and catalyses the conversion of GDP-d-mannose towards GDP-l-galactose. Although the overall reaction seems relatively simple (a double epimerization), the enzyme needs to orchestrate a complex set of chemical reactions, with no less than 6 catalysis steps (oxidation, 2x deprotonation, 2x protonation and reduction), to perform the double epimerization of GDP-mannose to GDP-l-galactose. The enzyme is involved in the biosynthesis of vitamin C in plants and lipopolysaccharide synthesis in bacteria. In this review, we provide a clear overview of these interesting epimerases, including the latest findings such as the recently characterized bacterial and thermostable GM35E representative and its mechanism revision but also focus on their industrial potential in rare sugar synthesis and glycorandomization.
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spelling doaj.art-3c6918e22b3846fd98d9d5851aef115f2022-12-22T04:03:23ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2022-01-01810.3389/fmolb.2021.784142784142GDP-Mannose 3,5-Epimerase: A View on Structure, Mechanism, and Industrial PotentialKoen BeerensOphelia GevaertTom DesmetGDP-mannose 3,5-epimerase (GM35E, GME) belongs to the short-chain dehydrogenase/reductase (SDR) protein superfamily and catalyses the conversion of GDP-d-mannose towards GDP-l-galactose. Although the overall reaction seems relatively simple (a double epimerization), the enzyme needs to orchestrate a complex set of chemical reactions, with no less than 6 catalysis steps (oxidation, 2x deprotonation, 2x protonation and reduction), to perform the double epimerization of GDP-mannose to GDP-l-galactose. The enzyme is involved in the biosynthesis of vitamin C in plants and lipopolysaccharide synthesis in bacteria. In this review, we provide a clear overview of these interesting epimerases, including the latest findings such as the recently characterized bacterial and thermostable GM35E representative and its mechanism revision but also focus on their industrial potential in rare sugar synthesis and glycorandomization.https://www.frontiersin.org/articles/10.3389/fmolb.2021.784142/fullepimeraseGDP-mannoseNS-SDRshort-chain dehydrogenase/reductase (SDR)NDP-sugar active SDR (NS-SDR)L-sugar
spellingShingle Koen Beerens
Ophelia Gevaert
Tom Desmet
GDP-Mannose 3,5-Epimerase: A View on Structure, Mechanism, and Industrial Potential
Frontiers in Molecular Biosciences
epimerase
GDP-mannose
NS-SDR
short-chain dehydrogenase/reductase (SDR)
NDP-sugar active SDR (NS-SDR)
L-sugar
title GDP-Mannose 3,5-Epimerase: A View on Structure, Mechanism, and Industrial Potential
title_full GDP-Mannose 3,5-Epimerase: A View on Structure, Mechanism, and Industrial Potential
title_fullStr GDP-Mannose 3,5-Epimerase: A View on Structure, Mechanism, and Industrial Potential
title_full_unstemmed GDP-Mannose 3,5-Epimerase: A View on Structure, Mechanism, and Industrial Potential
title_short GDP-Mannose 3,5-Epimerase: A View on Structure, Mechanism, and Industrial Potential
title_sort gdp mannose 3 5 epimerase a view on structure mechanism and industrial potential
topic epimerase
GDP-mannose
NS-SDR
short-chain dehydrogenase/reductase (SDR)
NDP-sugar active SDR (NS-SDR)
L-sugar
url https://www.frontiersin.org/articles/10.3389/fmolb.2021.784142/full
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