| Description | 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 [ ] into subfamilies.One of these, called class-IV, currently consists of proteins of about 270 to 415 amino-acid residues that share a few regions of sequence similarity. Surprisingly, the best conserved region does not include the lysine residue to which the pyridoxal-phosphate group is known to be attached, in ilvE, but is located some 40 residues at the C terminus side of the PlP-lysine.Among the class IV aminotransferases are two phylogenetically separable groups of branched-chain amino acid aminotransferase (IlvE) ( ). The last common ancestor of the two lineages appears also to have given rise to a family of D-amino acid aminotransferases (DAAT). This model represents the IlvE family less similar to the DAAT family. Also included in this group is branched-chain amino acid aminotransferase gloG from the yeast Glarea lozoyensis, which is required for biosynthesis of the mycotoxin pneumocandin, a lipohexapeptide of the echinocandin family [ ]. Transaminase AMT5 from the Alternaria rot fungus is one of many enzymes required for the non-ribosomal biosynthesis of the cyclic depsipeptides known as AM-toxins []. The aminotransferase FGSG_00049 from Fusarium graminearum is part of the gene cluster that mediates the biosynthesis of gramillins A and B, bicyclic lipopeptides that induce cell death in maize leaves but not in wheat, suggesting host-specific adaptation []. | Name | Branched-chain amino acid aminotransferase II |
| Short Name | B_amino_transII | Type | Family |
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