The sites of nucleotide conjugation are few. Two pyrophosphorylase reactions are sufficient to account for the occurrence of the variety of sugar nucleotides previously cited. The pathways for each are different. Whereas UDP-glucose arises from a direct conjugation of glucose 1-phosphate with UTP by a pyrophosphorylase whose specificity has been studied by Albrecht et af. (1968), the hexosamine pathway is far more complex, involving the amination of fructose 6-phosphate by glutamine, the subsequent acetylation, mutation and, only then, conjugation by a specific pyrophosphorylase to form UDP-N-acetylglucosamine. Whereas considerable information is available on the UDPglucose pyrophosphorylase, information on the enzymology of the hexosamine pathway is scant. Fructose 6-phosphate-glutanline aminotransferase has been purified extensively from rat liver and its steady-state kinetic parameters have been established (Winterburn & Phelps, 1970, 1971). The acetylation by acetyl-CoA has been thoroughly investigated by P. J. Winterburn &A. Corfield (unpublished work), but scant information is available on the specific mutase interconverting N-acetylglucosamine 6-phosphate and its l-phosphate counterpart (Fernandez-Sorenson, 1968), and detailed information is similarly lacking on the synthesis of UDP-N-acetylglucosamine from this last intermediate and UTP (Strominger & Smith, 1959). Interconversion of nircleotide sitgars One of the most potentially productive areas of research in this field involves the study of the vast variety of interconversion reactions of which nucleotide sugars are capable. These involve precise inversions, dehydrogenations, reductions, decarboxylations and simultaneous performances of these reactions. Of immediate concern in the context of glycosaminoglycan biosynthesis is the formation of UDP-galactose from UDP-glucose by the 4’-epimerase. This enzyme has been studied in a variety of tissues. The n~ammalian enzyme is potently inhibited by NADH, though requiring catalytic amounts of NAD+ for its reaction (Maxwell, 1957). UDP-xylose arises from the decarboxylation of UDP-glucuronic acid and has been demonstrated in a wide variety of tissues, e.g. hen oviduct (Bdolah & Feingold, 1965), mouse cell mastocytoma (Silbert & Deluca, 1967) and cartilage (Castellani eta/., 1967). The enzyme from Cryptococciis lairventii and yeast has been intensively and elegantly studied by Schutzbach & Feingold (1970), who proposed an interesting mechanism of reaction. The enzyme is potently inhibited by NADH and UDP, though containing tighly bound NAD+. UDP-glucuronic acid arises by dehydrogenation of UDP-glucose (Strominger et a/., 1957). The reaction is noteworthy for being a four-electron oxidation. The enzyme from bovine liver contains six identical subunits, and some details of its protein chemistry have