کد مقاله کد نشریه سال انتشار مقاله انگلیسی ترجمه فارسی نسخه تمام متن
1930582 1050518 2011 5 صفحه PDF سفارش دهید دانلود رایگان
عنوان انگلیسی مقاله ISI
Isolation and characterization of functional Leishmania major virulence factor UDP-galactopyranose mutase
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موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Isolation and characterization of functional Leishmania major virulence factor UDP-galactopyranose mutase
چکیده انگلیسی

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 diseases and over 50,000 deaths occur annually. Recently, it was shown that the flavin-dependent enzyme UDP-galactopyranose mutase (UGM) is a virulence factor in Leishmania major. UGM catalyzes the conversion of UDP-galactopyranose to UDP-galactofuranose. The product, UDP-galactofuranose, is the only source of galactofuranose which is present on the cell surface of this parasite and has been implicated to be important for host-parasite interactions. The recombinant form of this enzyme was obtained in a soluble and active form. The enzyme was shown to be active only in the reduced state. A kcat value of 5 ± 0.2 s−1 and a KM value of 87 ± 11 μM were determined with UDP-galactofuranose as the substrate. Different from the dimeric bacterial and tetrameric fungal UGMs, this parasitic enzyme functions as a monomer.


► Functional recombinant Leishmania major UDP-galactopyranose mutase (LmUGM) was expressed and purified.
► This flavin-dependent enzyme is active only in the reduced form.
► LmUGM functions as a monomeric enzyme.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 407, Issue 3, 15 April 2011, Pages 552–556
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