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Novel insights into the existence of the putative UDP-glucuronate 5-epimerase specificity

Ophelia Gevaert (UGent) , Stevie Van Overtveldt (UGent) , Matthieu Da Costa (UGent) , Koen Beerens (UGent) and Tom Desmet (UGent)
(2020) CATALYSTS. 10(2).
Author
Organization
Abstract
C5-epimerases are promising tools for the production of rare l-hexoses from their more common d-counterparts. On that account, UDP-glucuronate 5-epimerase (UGA5E) attracts attention as this enzyme could prove to be useful for the synthesis of UDP-l-iduronate. Interestingly, l-iduronate is known as a precursor for the production of heparin, an effective anticoagulant. To date, the UGA5E specificity has only been detected in rabbit skin extract, and the respective enzyme has not been characterized in detail or even identified at the molecular level. Accordingly, the current work aimed to shed more light on the properties of UGA5E. Therefore, the pool of putative UGA5Es present in the UniProt database was scrutinized and their sequences were clustered in a phylogenetic tree. However, the examination of two of these enzymes revealed that they actually epimerize UDP-glucuronate at the 4- rather than 5-position. Furthermore, in silico analysis indicated that this should be the case for all sequences that are currently annotated as UGA5E and, hence, that such activity has not yet been discovered in nature. The detected l-iduronate synthesis in rabbit skin extract can probably be assigned to the enzyme chondroitin-glucuronate C5-epimerase, which catalyzes the conversion of d-glucuronate to l-iduronate on a polysaccharide level.
Keywords
Physical and Theoretical Chemistry, Catalysis, UDP-glucuronate 5-epimerase, UDP-glucuronate 4-epimerase, CEP1 family, L-iduronate, biocatalysis, phylogenetic tree, recombinant expression, CARBOHYDRATE EPIMERASES, DERMATAN SULFATE, ENZYME, BIOSYNTHESIS, C5-EPIMERASE, SEQUENCE, GENE

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Citation

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MLA
Gevaert, Ophelia, et al. “Novel Insights into the Existence of the Putative UDP-Glucuronate 5-Epimerase Specificity.” CATALYSTS, vol. 10, no. 2, 2020, doi:10.3390/catal10020222.
APA
Gevaert, O., Van Overtveldt, S., Da Costa, M., Beerens, K., & Desmet, T. (2020). Novel insights into the existence of the putative UDP-glucuronate 5-epimerase specificity. CATALYSTS, 10(2). https://doi.org/10.3390/catal10020222
Chicago author-date
Gevaert, Ophelia, Stevie Van Overtveldt, Matthieu Da Costa, Koen Beerens, and Tom Desmet. 2020. “Novel Insights into the Existence of the Putative UDP-Glucuronate 5-Epimerase Specificity.” CATALYSTS 10 (2). https://doi.org/10.3390/catal10020222.
Chicago author-date (all authors)
Gevaert, Ophelia, Stevie Van Overtveldt, Matthieu Da Costa, Koen Beerens, and Tom Desmet. 2020. “Novel Insights into the Existence of the Putative UDP-Glucuronate 5-Epimerase Specificity.” CATALYSTS 10 (2). doi:10.3390/catal10020222.
Vancouver
1.
Gevaert O, Van Overtveldt S, Da Costa M, Beerens K, Desmet T. Novel insights into the existence of the putative UDP-glucuronate 5-epimerase specificity. CATALYSTS. 2020;10(2).
IEEE
[1]
O. Gevaert, S. Van Overtveldt, M. Da Costa, K. Beerens, and T. Desmet, “Novel insights into the existence of the putative UDP-glucuronate 5-epimerase specificity,” CATALYSTS, vol. 10, no. 2, 2020.
@article{8667027,
  abstract     = {C5-epimerases are promising tools for the production of rare l-hexoses from their more common d-counterparts. On that account, UDP-glucuronate 5-epimerase (UGA5E) attracts attention as this enzyme could prove to be useful for the synthesis of UDP-l-iduronate. Interestingly, l-iduronate is known as a precursor for the production of heparin, an effective anticoagulant. To date, the UGA5E specificity has only been detected in rabbit skin extract, and the respective enzyme has not been characterized in detail or even identified at the molecular level. Accordingly, the current work aimed to shed more light on the properties of UGA5E. Therefore, the pool of putative UGA5Es present in the UniProt database was scrutinized and their sequences were clustered in a phylogenetic tree. However, the examination of two of these enzymes revealed that they actually epimerize UDP-glucuronate at the 4- rather than 5-position. Furthermore, in silico analysis indicated that this should be the case for all sequences that are currently annotated as UGA5E and, hence, that such activity has not yet been discovered in nature. The detected l-iduronate synthesis in rabbit skin extract can probably be assigned to the enzyme chondroitin-glucuronate C5-epimerase, which catalyzes the conversion of d-glucuronate to l-iduronate on a polysaccharide level.},
  articleno    = {222},
  author       = {Gevaert, Ophelia and Van Overtveldt, Stevie and Da Costa, Matthieu and Beerens, Koen and Desmet, Tom},
  issn         = {2073-4344},
  journal      = {CATALYSTS},
  keywords     = {Physical and Theoretical Chemistry,Catalysis,UDP-glucuronate 5-epimerase,UDP-glucuronate 4-epimerase,CEP1 family,L-iduronate,biocatalysis,phylogenetic tree,recombinant expression,CARBOHYDRATE EPIMERASES,DERMATAN SULFATE,ENZYME,BIOSYNTHESIS,C5-EPIMERASE,SEQUENCE,GENE},
  language     = {eng},
  number       = {2},
  pages        = {11},
  title        = {Novel insights into the existence of the putative UDP-glucuronate 5-epimerase specificity},
  url          = {http://dx.doi.org/10.3390/catal10020222},
  volume       = {10},
  year         = {2020},
}

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