Leucine 2,3-aminomutase
(Redirected from Leucine aminomutase)
| leucine 2,3-aminomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.3.7 | ||||||||
| CAS no. | 59125-53-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a leucine 2,3-aminomutase (EC 5.4.3.7) is an enzyme that catalyzes the chemical reaction
Hence, this enzyme is responsible for the conversion of L-leucine to β-leucine.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (2S)-alpha-leucine 2,3-aminomutase. This enzyme participates in valine, leucine and isoleucine degradation. It employs one cofactor, cobamide.
References
[edit]- Freer I, Pedrocchi-Fantoni G, Picken DJ, Overton KH (1981). "Stereochemistry of the leucine 2,3-aminomutase from tissue-cultures of Andrographis paniculata". Journal of the Chemical Society, Chemical Communications (3): 80–82. doi:10.1039/c39810000080.
- Poston JM (1976). "Leucine 2,3-aminomutase, an enzyme of leucine catabolism". J. Biol. Chem. 251 (7): 1859–63. PMID 1270414.
- Poston JM (1976). "Coenzyme B12-dependent enzymes in potatoes: leucine 2,3-aminomutase and methylmalonyl-CoA mutase". Phytochemistry. 17 (3): 401–402. doi:10.1016/S0031-9422(00)89324-3.
