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5.4.3.2 |
Activity |
5.4.3.2 |
Description |
Lysine 2,3-aminomutase |
Notes |
Lysine-2,3-aminomutase requires a [4Fe-4S] cluster, S-adenosyl-L-methionine (SAM), and pyridoxal-5'-phosphate as cofactors. |
PDB |
2A5H; |
PLP Fold Type |
VII |
PLP-dependent Domain |
|
Number of sequences |
13 |
Sequences in seed alignment |
|
Reference sequence |
AAB72069 |
Domain interval |
63-348 |
Catalytic site |
346 K |
| |
References |
Lepore, B.W.; Ruzicka, F.J.; Frey, P. A.; Ringe, D. (2005) The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale Proc Natl Acad Sci U S A 102 13819-24. Chen, D.; Ruzicka, F. J.; Frey, P. A. (2000) A novel lysine 2,3-aminomutase encoded by the yodO gene of bacillus subtilis: characterization and the observation of organic radical intermediates Biochem J 348 539-49. Ruzicka, F. J.; Lieder, K. W.; Frey, P. A. (2000) Lysine 2,3-aminomutase from Clostridium subterminale SB4: mass spectral characterization of cyanogen bromide-treated peptides and cloning, sequencing, and expression of the gene kamA in Escherichia coli J Bacteriol 182 469-76. Articles on 5.4.3.2 |
last changed |
2009/07/03 14:56 |
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