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To synthesize glycogen two enzymes are needed:
1. UDP-glucose pyrophosphorylase catalyzes the synthesis of UDP-glucose from UTP and glucose 1-phosphate:
The pyrophosphate (PPi) is right away hydrolyzed by inorganic pyrophosphatase, releasing energy. Thus the whole reaction is very exergonic and essentially irreversible.
2. Glycogen synthase now transfers the glucosyl residue from UDP-glucose to the C4 OH group at the nonreducing end of a glycogen molecule, forming a α1-4 glycosidic bond. Amusingly, glycogen synthase can only extend an existing chain. Thus it needs a primer; this is a protein called as glycogenin. Glycogenin holds eight glucosyl units linked via α1-4 link- ages, which are added to the protein by itself for instance Autocatalysis. It is this molecule which glycogen synthase then extends. Each glycogen granule have only a single glycogenin molecule at its core. The reality that glycogen synthase is fully active only when in contact with glycogenin limits the size of the glycogen granule.
Which of the recombination process(transformation, conjugation and transduction) would be most likely to occur in the natural environment?
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