Aminotransferases share certain mechanistic features with other pyridoxal-phosphate dependent enzymes, such as the covalent binding of the pyridoxal-phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [1] into subfamilies. One of these, called class-II, currently consists of the following enzymes:

• Glycine C-acetyltransferase (EC 2.3.1.29), which catalyzes the addition of acetyl-CoA to glycine to form 2-amino-3-oxobutanoate (gene kbl).
• 5-aminolevulinic acid synthase (EC 2.3.1.37) (delta-ALA synthase), which catalyzes the first step in heme biosynthesis via the Shemin (or C4) pathway, i.e. the addition of succinyl-CoA to glycine to form 5- aminolevulinate.
• 8-amino-7-oxononanoate synthase (EC 2.3.1.47) (7-KAP synthase), a bacterial enzyme (gene bioF) which catalyzes an intermediate step in the biosynthesis of biotin: the addition of 6-carboxy-hexanoyl-CoA to alanine to form 8- amino-7-oxononanoate.
• Histidinol-phosphate aminotransferase (EC 2.6.1.9), which catalyzes the eighth step in histidine biosynthetic pathway: the transfer of an amino group from 3-(imidazol-4-yl)-2-oxopropyl phosphate to glutamic acid to form histidinol phosphate and 2-oxoglutarate.
• Serine C-palmitoyltransferase (EC 2.3.1.50) from yeast (genes LCB1 and LCB2), which catalyzes the condensation of palmitoyl-CoA and serine to form 3-ketosphinganine.

The sequence around the pyridoxal-phosphate attachment site of this class of enzyme is sufficiently conserved to allow the creation of a specific pattern.