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Freas N, Newton P, Perozich J. Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships. FEBS Open Bio. 2016;6(1):77-89doi: 10.1002/2211-5463.12022.
Freas, N., Newton, P., & Perozich, J. (2016). Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships. FEBS open bio, 6(1), 77-89. https://doi.org/10.1002/2211-5463.12022
Freas, Nicholas, et al. "Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships." FEBS open bio vol. 6,1 (2016): 77-89. doi: https://doi.org/10.1002/2211-5463.12022
Freas N, Newton P, Perozich J. Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships. FEBS Open Bio. 2016 Jan 11;6(1):77-89. doi: 10.1002/2211-5463.12022. eCollection 2016 Jan. PMID: 27047744; PMCID: PMC4794789.
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FEBS Open Bio. 2016 Jan 11;6(1):77-89. doi: 10.1002/2211-5463.12022. eCollection 2016 Jan.

Analysis of nucleotide diphosphate sugar dehydrogenases reveals family and group-specific relationships.

FEBS open bio

Nicholas Freas, Peter Newton, John Perozich

Affiliations

  1. Department of Biology Franciscan University of Steubenville OH USA.

PMID: 27047744 PMCID: PMC4794789 DOI: 10.1002/2211-5463.12022

Abstract

UNLABELLED: UDP-glucose dehydrogenase (UDPGDH), UDP-N-acetyl-mannosamine dehydrogenase (UDPNAMDH) and GDP-mannose dehydrogenase (GDPMDH) belong to a family of NAD (+)-linked 4-electron-transfering oxidoreductases called nucleotide diphosphate sugar dehydrogenases (NDP-SDHs). UDPGDH is an enzyme responsible for converting UDP-d-glucose to UDP-d-glucuronic acid, a product that has different roles depending on the organism in which it is found. UDPNAMDH and GDPMDH convert UDP-N-acetyl-mannosamine to UDP-N-acetyl-mannosaminuronic acid and GDP-mannose to GDP-mannuronic acid, respectively, by a similar mechanism to UDPGDH. Their products are used as essential building blocks for the exopolysaccharides found in organisms like Pseudomonas aeruginosa and Staphylococcus aureus. Few studies have investigated the relationships between these enzymes. This study reveals the relationships between the three enzymes by analysing 229 amino acid sequences. Eighteen invariant and several other highly conserved residues were identified, each serving critical roles in maintaining enzyme structure, coenzyme binding or catalytic function. Also, 10 conserved motifs that included most of the conserved residues were identified and their roles proposed. A phylogenetic tree demonstrated relationships between each group and verified group assignment. Finally, group entropy analysis identified novel conservations unique to each NDP-SDH group, including residue positions critical to NDP-sugar substrate interaction, enzyme structure and intersubunit contact. These positions may serve as targets for future research.

ENZYMES: UDP-glucose dehydrogenase (UDPGDH, EC 1.1.1.22).

Keywords: GDP‐mannose dehydrogenase; UDP‐N‐acetyl‐mannosamine dehydrogenase; UDP‐glucose dehydrogenase; multiple sequence alignment; nucleotide diphosphate sugar dehydrogenase

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