ABSTRACT
The older term for the class of enzymes is "transaminases". However, the term "aminotransferases" is preferred by the Nomenclature Committee of the International Union of Biochemistry. The practice has arisen in which the aminotransferases utilizing glutamate as one of a pair of possible amino acid substrates are given the name of the other amino acid substrate, and are listed as such in Chemical Abstracts. For many of the common amino acids the first step of catabolism is removal of the α-amine nitrogen. This removal may be brought about by transamination, oxidative deamination, or nonoxidative deamination. The redox state of the cell also is probably a controlling factor in gluconeogenesis. Thus, the observation by Cornell et al. that inhibition of gluconeogenesis occurs when Aspanate aminotransferase is inhibited may be explained by a disruption of the malate-aspartate shuttle and an increase in the lactate/pyruvate ratio.
