Bifunctional N-acetylglutamate Synthase-Kinase from Xanthomonas campestris
Author Information
Author(s): Qu Qiuhao, Morizono Hiroki, Shi Dashuang, Tuchman Mendel, Caldovic Ljubica
Primary Institution: Children's Research Institute, Children's National Medical Center, The George Washington University
Hypothesis
The genes annotated as argB in Xanthomonadales encode a dual-function enzyme that catalyzes the first two reactions of the arginine biosynthesis.
Conclusion
The close phylogenetic relationship and similar biochemical properties of xanthomonad NAGS-K and mammalian NAGS suggest that we have identified a close relative to the bacterial antecedent of mammalian NAGS.
Supporting Evidence
- Xanthomonad NAGS-K is more closely related to mammalian NAGS than to other bacterial NAGS.
- The enzyme from X. campestris could become a good model for mammalian NAGS in structural, biochemical and biophysical studies.
- Mammalian NAGS and its bacterial homolog have similar affinities for substrates acetyl coenzyme A and glutamate.
Takeaway
Scientists found a new enzyme in bacteria that works like a similar enzyme in humans, helping to understand how these enzymes evolved.
Methodology
Phylogenetic analysis and biochemical characterization of the recombinant NAGS-K protein.
Limitations
The study did not explore the three-dimensional structure of the enzyme or its interactions with other proteins.
Digital Object Identifier (DOI)
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