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Abstract
The oligoHis-tagged versions of glucosamine-6- phosphate deaminase from Giardia lamblia (GlmNagB-HisN, GlmNagB-HisC) were constructed and purified to hear homogeneity, and their kinetic and structural properties were compared to those of the wild-type enzyme (GlmNagB). Introduction of the oligoHis tag at the GlmNagB C-terminus resulted in almost complete loss of the catalytic activity, while the catalytic properties of GlmNagB-HisN and GlmNagB were very similar. The recombinant and wild-type enzyme exhibits heterogeneity of the quaternary structure and in solution exists in three interconvertible forms, namely, monomeric, homodimeric, and homotetrameric. Although the monomeric form is prevalent, the monomer/dimer/tetramer ratios depended on protein concentration and fell within the range from 72:27:1 to 39:23:38. The enzyme is fully active in each of the oligomeric structures, efficiently catalyzes synthesis of D-glucosamine- 6-phosphate from D-fructose-6-phosphate and ammonia, and its activity is not modified by GlcNAc6P, UDPGlcNAc, or UDP-GalNAc. GlcN6P deaminase of G. lamblia represents a novel structural and functional type of enzyme of the NagB subfamily.
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- Publication version
- Accepted or Published Version
- DOI:
- Digital Object Identifier (open in new tab) 10.1007/s00436-014-4174-4
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- Category:
- Articles
- Type:
- artykuł w czasopiśmie wyróżnionym w JCR
- Published in:
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PARASITOLOGY RESEARCH
no. 114,
edition 1,
pages 175 - 184,
ISSN: 0932-0113 - Language:
- English
- Publication year:
- 2015
- Bibliographic description:
- Kwiatkowska-Semrau K., Czarnecka J., Wojciechowski M., Milewski S.: Heterogeneity of quaternary structure of glucosamine-6-phosphate deaminase from Giardia lamblia// PARASITOLOGY RESEARCH. -Vol. 114, iss. 1 (2015), s.175-184
- DOI:
- Digital Object Identifier (open in new tab) 10.1007/s00436-014-4174-4
- Verified by:
- Gdańsk University of Technology
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