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- Publications
- Influence
Characterization of recombinant UDP-galactopyranose mutase from Aspergillus fumigatus.
- Michelle Oppenheimer, Myles B. Poulin, T. Lowary, R. Helm, P. Sobrado
- Biology, Medicine
- Archives of biochemistry and biophysics
- 1 October 2010
UDP-galactopyranose mutase (UGM) is a flavin-containing enzyme that catalyzes the conversion of UDP-galactopyranose to UDP-galactofuranose, the precursor of galactofuranose, which is an important… Expand
Dual role of NADP(H) in the reaction of a flavin dependent N-hydroxylating monooxygenase.
- E. Romero, M. Fedkenheuer, Samuel W Chocklett, J. Qi, Michelle Oppenheimer, P. Sobrado
- Biology, Medicine
- Biochimica et biophysica acta
- 1 June 2012
Aspergillus fumigatus siderophore A (Af SidA) is a flavin-dependent monooxygenase that catalyzes the hydroxylation of ornithine, producing N(5)-hydroxyornithine. This is the first step in the… Expand
Biosynthesis of Galactofuranose in Kinetoplastids: Novel Therapeutic Targets for Treating Leishmaniasis and Chagas' Disease
- Michelle Oppenheimer, A. L. Valenciano, P. Sobrado
- Biology, Medicine
- Enzyme research
- 25 May 2011
Cell surface proteins of parasites play a role in pathogenesis by modulating mammalian cell recognition and cell adhesion during infection. β-Galactofuranose (Galf) is an important component of… Expand
Crystal structures of Trypanosoma cruzi UDP-galactopyranose mutase implicate flexibility of the histidine loop in enzyme activation.
- Richa Dhatwalia, H. Singh, Michelle Oppenheimer, P. Sobrado, J. Tanner
- Biology, Medicine
- Biochemistry
- 19 June 2012
Chagas disease is a neglected tropical disease caused by the protozoan parasite Trypanosoma cruzi. Here we report crystal structures of the galactofuranose biosynthetic enzyme UDP-galactopyranose… Expand
Chemical Mechanism of UDP-Galactopyranose Mutase from Trypanosoma cruzi: A Potential Drug Target against Chagas' Disease
- Michelle Oppenheimer, A. L. Valenciano, Karina Kizjakina, Jun Qi, P. Sobrado
- Chemistry, Medicine
- PloS one
- 20 March 2012
UDP-galactopyranose mutase (UGM) is a flavoenzyme that catalyzes the conversion of UDP-galactopyranose to UDP-galactofuranose, the precursor of galactofuranose (Galf). Galf is found in several… Expand
Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase.
- Richa Dhatwalia, H. Singh, +5 authors J. Tanner
- Chemistry, Medicine
- Journal of the American Chemical Society
- 19 October 2012
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… Expand
Crystal Structures and Small-angle X-ray Scattering Analysis of UDP-galactopyranose Mutase from the Pathogenic Fungus Aspergillus fumigatus*
- Richa Dhatwalia, H. Singh, +4 authors J. Tanner
- Medicine, Biology
- The Journal of Biological Chemistry
- 31 January 2012
Background: UDP-galactopyranose mutase (UGM) catalyzes a step in galactofuranose biosynthesis in pathogens and is a promising drug design target. Results: The first crystal structures and SAXS… Expand
Fluorescence Polarization Binding Assay for Aspergillus fumigatus Virulence Factor UDP-Galactopyranose Mutase
- Jun Qi, Michelle Oppenheimer, P. Sobrado
- Biology, Medicine
- Enzyme research
- 21 August 2011
Aspergillus fumigatus is an opportunistic human pathogenic fungus responsible for deadly lung infections in immunocompromised individuals. Galactofuranose (Galf) residues are essential components of… Expand
Isolation and characterization of functional Leishmania major virulence factor UDP-galactopyranose mutase.
- Michelle Oppenheimer, A. L. Valenciano, P. Sobrado
- Biology, Medicine
- Biochemical and biophysical research…
- 15 April 2011
Human parasitic pathogens of the genus Leishmania are the causative agents of cutaneous, mucocutaneous, and visceral leishmaniasis. Currently, there are millions of people infected with these… Expand
Recombinant expression, purification, and characterization of ThmD, the oxidoreductase component of tetrahydrofuran monooxygenase.
- Michelle Oppenheimer, Brad S. Pierce, J. A. Crawford, K. Ray, R. Helm, P. Sobrado
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 15 April 2010
Tetrahydrofuran monooxygenase (Thm) catalyzes the NADH-and oxygen-dependent hydroxylation of tetrahydrofuran to 2-hydroxytetrahydrofuran. Thm is composed of a hydroxylase enzyme, a regulatory… Expand