Leucine 2,3-aminomutase

Leucine 2,3-aminomutase is an enzyme that catalyzes the reversible interconversion of L-alpha-leucine and beta-leucine (3-amino-4-methylpentanoic acid) [5, 7]. It is found in various organisms, including bacteria, plants, and mammals, including humans [5, 11]. In humans, it plays a role in the minor pathway of leucine catabolism, particularly in the testes [8, 20]. The enzyme is notable for its dependence on Vitamin B12 (cobalamin) as a cofactor [5, 29]. Elevated levels of its product, beta-leucine, in the blood are used as a metabolic indicator of Vitamin B12 deficiency [8, 27]. While not currently a primary target for pharmaceutical drugs, its role in leucine metabolism makes it a subject of interest in metabolic research and potential therapeutic strategies for conditions like acute myeloid leukemia (AML) where amino acid metabolism is dysregulated [12, 16]. The gene encoding the human enzyme has not yet been identified, which remains a challenge for its molecular characterization and drug development [25].

Other names

Leucine aminomutase(2S)-alpha-leucine 2,3-aminomutaseL-leucine 2,3-aminomutaseLeucine mutase

None currently identified; the enzyme naturally catalyzes the reversible interconversion of L-alpha-leucine and (3R)-beta-leucine via a 2,3-shift of the amino group, requiring cobalamin (Vitamin B12) as a cofactor [5, 7].