The Enzyme Database

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EC 5.4.3.2     
Accepted name: lysine 2,3-aminomutase
Reaction: L-lysine = (3S)-3,6-diaminohexanoate
For diagram of lysine catabolism, click here
Systematic name: L-lysine 2,3-aminomutase
Comments: 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: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9075-20-1
References:
1.  Zappia, V. and Barker, H.A. Studies on lysine-2,3-aminomutase. Subunit structure and sulfhydryl groups. Biochim. Biophys. Acta 207 (1970) 505–513. [PMID: 5452674]
2.  Aberhart, D.J., Lim, H.-J. and Weiller, B.H. Stereochemistry of lysine 2,3-aminomutase. J. Am. Chem. Soc. 103 (1981) 6750–6752.
3.  Frey, P.A. Lysine 2,3-aminomutase: is adenosylmethionine a poor man’s adenosylcobalamin. FASEB J. 7 (1993) 662–670. [PMID: 8500691]
4.  Lieder, K.W., Booker, S., Ruzicka, F.J., Beinert, H., Reed, G.H. and 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 (1998) 2578–2585. [PMID: 9485408]
5.  Lepore, B.W., Ruzicka, F.J., Frey, P.A. and Ringe, D. The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. Proc. Natl Acad. Sci. USA 102 (2005) 13819–13824. [PMID: 16166264]
6.  Frey, P.A. and Reed, G.H. Pyridoxal-5′-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases. Biochim. Biophys. Acta 1814 (2011) 1548–1557. [PMID: 21435400]
[EC 5.4.3.2 created 1972]
 
 


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