ArticleJournal of the American Chemical Society2012
Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Structure and function of a flavin-dependent S-monooxygenase from garlic (The Journal of biological chemistry · 2020Article
- 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
- Flavin oxidation in flavin-dependent N-monooxygenases.Protein science : a publication of the Protein Society · 2019Article
- Steric Control of the Rate-Limiting Step of UDP-Galactopyranose Mutase.Biochemistry · 2018Article
- Identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay.Biochemical and biophysical research communications · 2017Article
- Multiple functionalities of reduced flavin in the non-redox reaction catalyzed by UDP-galactopyranose mutase.Archives of biochemistry and biophysics · 2017Review
- Identification of Aspergillus fumigatus UDP-Galactopyranose Mutase Inhibitors.Scientific reports · 2017Article
- In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction.Biochemistry · 2016Article
- Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase.Archives of biochemistry and biophysics · 2015Article
- An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation.The Journal of biological chemistry · 2015Article
- 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
- 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
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
UDP-galactopyranose mutase (UGM) plays an essential role in galactofuranose biosynthesis in microorganisms by catalyzing the conversion of UDP-galactopyranose to UDP-galactofuranose. The enzyme has gained attention recently as a promising target for the design of new antifungal, antitrypanosomal, and antileishmanial agents. Here we report the first crystal structure of UGM complexed with its redox partner NAD(P)H. Kinetic protein crystallography was used to obtain structures of oxidized Aspergillus fumigatus UGM (AfUGM) complexed with NADPH and NADH, as well as reduced AfUGM after dissociation of NADP(+). NAD(P)H binds with the nicotinamide near the FAD isoalloxazine and the ADP moiety extending toward the mobile 200s active site flap. The nicotinamide riboside binding site overlaps that of the substrate galactopyranose moiety, and thus NADPH and substrate binding are mutually exclusive. On the other hand, the pockets for the adenine of NADPH and uracil of the substrate are distinct and separated by only 6 Å, which raises the possibility of designing novel inhibitors that bind both sites. All 12 residues that contact NADP(H) are conserved among eukaryotic UGMs. Residues that form the AMP pocket are absent in bacterial UGMs, which suggests that eukaryotic and bacterial UGMs have different NADP(H) binding sites. The structures address the longstanding question of how UGM binds NAD(P)H and provide new opportunities for drug discovery.
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