Background:
The 1,4-alpha-glucan branching protein (GlgB) plays an important role in the
glycogen biosynthesis and the deficiency in this enzyme has resulted in Glycogen storage disease and
accumulation of an amylopectin-like polysaccharide. Consequently, this enzyme was considered a special
topic in clinical and biotechnological research. One of the newly introduced GlgB belongs to the
Neisseria sp. HMSC071A01 (Ref.Seq. WP_049335546). For in silico analysis, the 3D molecular modeling
of this enzyme was conducted in the I-TASSER web server.
Methods:
For a better evaluation, the important characteristics of this enzyme such as functional properties,
metabolic pathway and activity were investigated in the TargetP software. Additionally, the
phylogenetic tree and secondary structure of this enzyme were studied by Mafft and Prabi software,
respectively. Finally, the binding site properties (the maltoheptaose as substrate) were studied using the
AutoDock Vina.
Results:
By drawing the phylogenetic tree, the closest species were the taxonomic group of Betaproteobacteria.
The results showed that the structure of this enzyme had 34.45% of the alpha helix and
45.45% of the random coil. Our analysis predicted that this enzyme has a potential signal peptide in the
protein sequence.
Conclusion:
By these analyses, a new understanding was developed related to the sequence and structure
of this enzyme. Our findings can further be used in some fields of clinical and industrial biotechnology.
Factors Altering Pyruvate Excretion in a Glycogen Storage Mutant of the Cyanobacterium, Synechococcus PCC7942
