Heterogeneity of quaternary structure of glucosamine-6-phosphate deaminase from Giardia lamblia - Publikacja - MOST Wiedzy

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Heterogeneity of quaternary structure of glucosamine-6-phosphate deaminase from Giardia lamblia

Abstrakt

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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Informacje szczegółowe

Kategoria:
Publikacja w czasopiśmie
Typ:
artykuł w czasopiśmie wyróżnionym w JCR
Opublikowano w:
PARASITOLOGY RESEARCH nr 114, wydanie 1, strony 175 - 184,
ISSN: 0932-0113
Język:
angielski
Rok wydania:
2015
Opis bibliograficzny:
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:
Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1007/s00436-014-4174-4
Weryfikacja:
Politechnika Gdańska

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