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Abstract
L-Glutamine: D-fructose-6-phosphate aminotransferase (EC 2.6.1.16), known also as glucosamine-6-phosphate (GlcN-6-P) syntase, catalyzes the first committed step in the amino sugar biosynthetic pathway in prokaryotic and eukaryotic organisms. The enzyme carries out a complex reaction involving ammonia transfer and sugar phosphate isomerization. GlcN-6-P syntase is an important point of metabolic control of amino sugar biosynthesis and postulated a putative target for antifungal chemotherapy. The enzyme is well known for its relative instability and difficulties in purification. One of the possible approaches to facilitate enzyme purification is a construction of its hexaHistag-containing version that can be easily isolated from complex mixtures by the one-step metal affinity chromatography. Unfortunately, introduction of hexahistydyl tags at either N- or C-terminus of GlcN-6-P synthase results in lost of the enzyme activity.
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Details
- Category:
- Conference activity
- Type:
- publikacja w wydawnictwie zbiorowym recenzowanym (także w materiałach konferencyjnych)
- Title of issue:
- 13th International Symposium of Students and Young Mechanical Engineers : Advances in Chemical and Mechanical Engineering, Gdańsk, 20th-22nd May 2010 strony 216 - 217
- Language:
- Polish
- Publication year:
- 2010
- Bibliographic description:
- Kwiatkowska K., Czarnecka J.: Construction of glucosamine-6-phosphate synthase with an internal hexahistydyl fragment// 13th International Symposium of Students and Young Mechanical Engineers : Advances in Chemical and Mechanical Engineering, Gdańsk, 20th-22nd May 2010/ ed. ed. C. Fijało. - Gdansk University of Technology. Gdańsk: GUT, 2010, s.216-217
- Verified by:
- Gdańsk University of Technology
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