| Type: | Family | Name: | Leucine carboxyl methyltransferase 1, LCMT1 |
| Description: | Leucine carboxymethyltransferases methylate the carboxyl group of leucine residues to form alpha-leucine ester residues. It includes LCTM1 which regulate the activity of serine/threonine phosphatase 2A (PP2A) through methylation of the C-terminal leucine residue of the catalytic subunit of PP2A [, , ]. This affects the heteromultimeric composition of PP2A which in turn affects protein recognition and substrate specificity. Like many other methyltransferases LCTM1 uses S-adenosylmethionine (SAM) as the methyl donor. LCTM1 contains the common SAM-dependent methyltransferase core fold, with various insertions and additions creating a specific PP2A binding site [].This group represents the LCMT1 subgroup of leucine carboxymethyltransferases. | Short Name: | Leu_CO_MeTrfase_LCMT1 |
