EC - Lysine 2,3-aminomutase

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IntEnz Enzyme Nomenclature


Accepted name:
lysine 2,3-aminomutase
Systematic name:
L-lysine 2,3-aminomutase




This enzyme is a member of the 'AdoMet radical' (radical SAM) family. It contains pyridoxal phosphate and a [4Fe-4S] cluster and binds an exchangeable S-adenosyl-L-methionine molecule. Activity in vitro requires a strong reductant such as dithionite and strictly anaerobic conditions. A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of S-adenosyl-L-methionine, mediated by the iron-sulfur cluster. S-adenosyl-L-methionine is regenerated at the end of the reaction.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0050066
CAS Registry Number: 9075-20-1


  1. Aberhart, D.J., Lim, H.-J. and Weiller, B.H.
    Stereochemistry of lysine 2,3-aminomutase.
    J. Am. Chem. Soc. 103 : 6750-6752 (1981).
  2. Zappia, V. and Barker, H.A.
    Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl groups.
    Biochim. Biophys. Acta 207 : 505-513 (1970). [PMID: 5452674]
  3. Frey, P. A.
    Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin?
    FASEB J. 7 : 662-670 (1993). [PMID: 8500691]
  4. Lieder, K. W., Booker, S., Ruzicka, F. J., Beinert, H., Reed, G. H., Frey, P. A.
    S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance.
    Biochemistry 37 : 2578-2585 (1998). [PMID: 9485408]
  5. Lepore, B. W., Ruzicka, F. J., Frey, P. A., Ringe, D.
    The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale.
    Proc. Natl. Acad. Sci. U.S.A. 102 : 13819-13824 (2005). [PMID: 16166264]
  6. Frey, P. A., Reed, G. H.
    Pyridoxal-5'-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases.
    Biochim. Biophys. Acta 1814 : 1548-1557 (2011). [PMID: 21435400]

[EC created 1972]