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Leucine 2,3-aminomutase

From Wikipedia, the free encyclopedia
leucine 2,3-aminomutase
Identifiers
EC no.5.4.3.7
CAS no.59125-53-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins

In enzymology, a leucine 2,3-aminomutase (EC 5.4.3.7) is an enzyme that catalyzes the chemical reaction

(2S)-alpha-leucine (3R)-beta-leucine

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

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  • 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.