ArticleThe Journal of biological chemistry2012
Structural insight into the unique substrate binding mechanism and flavin redox state of UDP-galactopyranose mutase from Aspergillus fumigatus.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- Structural bioinformatics insights into UDP-galactopyranose mutase (UGM) as a novel drug target for antifilarial therapy against human filarial parasite Brugia malayi.Molecular diversity · 2026Article
- N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position.Frontiers in molecular biosciences · 2020Review
- Molecular Dynamics Simulations of Substrate Release from Trypanosoma cruzi UDP-Galactopyranose Mutase.Journal of chemical information and modeling · 2019Article
- Steric Control of the Rate-Limiting Step of UDP-Galactopyranose Mutase.Biochemistry · 2018Article
- Conformational Control of UDP-Galactopyranose Mutase Inhibition.Biochemistry · 2017Article
- Galactofuranose antigens, a target for diagnosis of fungal infections in humans.Future science OA · 2017Review
- The Cell Wall Arabinose-Deficient Arabidopsis thaliana Mutant murus5 Encodes a Defective Allele of REVERSIBLY GLYCOSYLATED POLYPEPTIDE2.Plant physiology · 2016Article
- Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics.Biochemistry · 2014Article
- Structure, mechanism, and dynamics of UDP-galactopyranose mutase.Archives of biochemistry and biophysics · 2014Review
- Article
- Substrate-dependent dynamics of UDP-galactopyranose mutase: Implications for drug design.Protein science : a publication of the Protein Society · 2013Article
- UDP-galactopyranose mutases from Leishmania species that cause visceral and cutaneous leishmaniasis.Archives of biochemistry and biophysics · 2013Article
- UDP-galactopyranose mutase in nematodes.Biochemistry · 2013Article
- Targeting UDP-galactopyranose mutases from eukaryotic human pathogens.Current pharmaceutical design · 2013Review
- Noncanonical reactions of flavoenzymes.International journal of molecular sciences · 2012Review
- Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase.Journal of the American Chemical Society · 2012Article
- Crystal structures of Trypanosoma cruzi UDP-galactopyranose mutase implicate flexibility of the histidine loop in enzyme activation.Biochemistry · 2012Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
UDP-galactopyranose mutase (UGM) is a flavin-containing enzyme that catalyzes the reversible conversion of UDP-galactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf). As in prokaryotic UGMs, the flavin needs to be reduced for the enzyme to be active. Here we present the first eukaryotic UGM structures from Aspergillus fumigatus (AfUGM). The structures are of UGM alone, with the substrate UDP-Galp and with the inhibitor UDP. Additionally, we report the structures of AfUGM bound to substrate with oxidized and reduced flavin. These structures provide insight into substrate recognition and structural changes observed upon substrate binding involving the mobile loops and the critical arginine residues Arg-182 and Arg-327. Comparison with prokaryotic UGM reveals that despite low sequence identity with known prokaryotic UGMs the overall fold is largely conserved. Structural differences between prokaryotic UGM and AfUGM result from inserts in AfUGM. A notable difference from prokaryotic UGMs is that AfUGM contains a third flexible loop (loop III) above the si-face of the isoalloxazine ring that changes position depending on the redox state of the flavin cofactor. This loop flipping has not been observed in prokaryotic UGMs. In addition we have determined the crystals structures and steady-state kinetic constants of the reaction catalyzed by mutants R182K, R327K, R182A, and R327A. These results support our hypothesis that Arg-182 and Arg-327 play important roles in stabilizing the position of the diphosphates of the nucleotide sugar and help to facilitate the positioning of the galactose moiety for catalysis.
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Registered trials
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