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Author Kwiatkowska Semrau, Karolina ♦ Czarnecka, Justyna ♦ Wojciechowski, Marek ♦ Milewski, Sławomir
Source SpringerLink
Content type Text
Publisher Springer Berlin Heidelberg
File Format PDF
Copyright Year ©2014
Language English
Subject Domain (in DDC) Technology ♦ Medicine & health
Subject Keyword Giardia ♦ Glucosamine-6-phosphate deaminase ♦ NagB ♦ Quaternary structure ♦ Medical Microbiology ♦ Microbiology ♦ Immunology
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, UDP-GlcNAc, or UDP-GalNAc. GlcN6P deaminase of G. lamblia represents a novel structural and functional type of enzyme of the NagB subfamily.
ISSN 09320113
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2014-10-19
Publisher Place Berlin/Heidelberg
e-ISSN 14321955
Journal Parasitology Research
Volume Number 114
Issue Number 1
Page Count 10
Starting Page 175
Ending Page 184

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Source: SpringerLink