When glycogen phosphorylase reaches a branching point in glycogen, the bonds switch from being alpha-1,4-glycosidic bonds to alpha-1,6-glycosidic bonds.  It is unable to cleave these bonds, and so other enzymes (a transferase and a glucosidase) must come into play.

Glycogen is first debranched and broken down from its non-reducing end by glycogen phosphorylase to give the product G1P, which is then converted into G6P by phosphoglutomutase. Glycogen synthase, glycogen branching enzyme, and UDP-glucose pyrophosphorylase are required for glycogen synthesis.

Glycogen phosphorylase, the rate-limiting enzyme of glycogenolysis  does not breaks alpha 1,6 glycosidic bonds. It releases glucose from glycogen by hydrolyzing alpha 1,4 glycosidic bonds until it reaches a branch point in the glycogen molecule. At this time, another enzyme, a debranching alpha 1,6 glycosidase hydrolyzes the alpha 1,6 glycosidic bonds. Glycogen phosphorylase is under regulation by many hormones, including insulin and glucagon, as well as epinephrine.

In order to break down glycogen into individual glucose-6-phosphate units, all of the above enzymes are required. Each plays a specific role in one of the following activities: degradation of glycogen initially, remodeling of the glycogen so that it can be acted upon by the enzymes, and conversion of glucose-1-phosphate to glucose 6-phosphate.

Glycogen is mostly stored in the liver and skeletal muscle. When it is broken down in the liver, the last enzyme, a phosphatase, removes the last phosphate group to release plain glucose into the bloodstream. In the muscle, there is no need to release the glucose, so glycogen is only broken down as far as glucose-6-phosphate. Skeletal muscle cells lack the last phosphatase required to remove the phosphate from carbon 6. This isn't an obstacle, however, because the glucose-6-phosphate is already on to the second stage of glycolysis.

Insulin is released in response to high blood glucose. It causes a signaling cascade that, in addition to other things, stops glycogenolysis. This is done by converting glycogen phosphorylase from it's active "a" form to its inactive "b" configuration. The "R" state is the active state, so the presence of glucose would not trigger the breakdown of glycogen. 5' AMP would not inhibit an inactive form of an enzyme. High AMP would mean a demand for ATP, so it would convert the enzyme to its "a" form.

Oxaloacetate is the four-carbon molecule that is regenerated by the enzyme malate dehydrogenase in order to continue the cycle to form citrate with acetyl-CoA in the first step of the Krebs cycle. The other answer choices are intermediates of the citric acid cycle, but only oxaloacetate is regenerated, making it a true cycle.

Phosphorylation of glycogen phosphorylase activates it, converting it from its inactive B-form to its active A-form. 

Phosphorolysis is the name given to the addition of phosphate across a bond. Remember that in glycogenolysis, glycogen phosphorylase adds a phosphate across the a-1,4-glycosidic bonds between the glucose units of glycogen. The result is that glucose leaves as glucose-1-phosphate. If hydrolysis were performed instead of phosphorolysis, free glucose would be severed from glycogen and would be able to leave the cell.

AMP is an activator of GP, whereas ATP is an inhibitor of GP. GP cleaves the alpha 1-4 glycosidic bond between a terminal glucose molecule and the rest of the glycogen straight chain, yielding glucose-1-phosphate during glycogenolysis.