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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 21435400] |
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