The breakdown into simpler components of glycogen, a polydisperse, highly branched glucan composed of chains of D-glucose residues.

Catalysis of the reaction: N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP.

The formation from simpler components of any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.

Stops, prevents or reduces the activity of metalloendopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide linkages in oligopeptides or polypeptides and contain a chelated metal ion at their active sites which is essential to their catalytic activity.

Catalysis of the reaction: GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP.

Specialized membrane domains composed mainly of cholesterol and sphingolipids, and are relatively poor in polyunsaturated lipids such as glycerophospholipids. The formation of these membrane domains is promoted by the presence of cholesterol in the lipid bilayer: the rigid hexagonal rings of cholesterol can pack tightly against the saturated hydrocarbon chains of some membrane lipids, allowing these lipids to assemble into cohesive units floating in the mass of loosely packed polyunsaturated plasma membrane components.

The breakdown into simpler components of biogenic amines, any of a group of naturally occurring, biologically active amines, such as norepinephrine, histamine, and serotonin, many of which act as neurotransmitters.

Catalysis of the posttranscriptional addition of a guanyl residue to the 5' end of an RNA molecule.

The chemical reactions involving starch, the most important reserve polysaccharide in plants. It is a glucan consisting of two components, amylose and amylopectin, which are both glucose homopolymers. Starch is synthesized as a temporary storage form of carbon and can be catabolized to produce sucrose.

The chemical reactions involving any of the compounds secreted by the thyroid gland, largely thyroxine and triiodothyronine.