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5.4.3.2 |
Description |
Lysine 2,3-aminomutase |
Catalyzed reaction |
L-lysine = (3S)-3,6-diaminohexanoate. |
Cofactor |
Pyridoxal-phosphate. S-adenosyl-L-methionine; [4Fe-4S] cluster |
Comments |
-!- Activity is stimulated by S-adenosyl-L-methionine and pyridoxal- phosphate. |
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An enzyme involved in one possible L-Lys degradation pathway.
The mechanism of the reaction has been delineated as a radical isomerization, in which radical formation is initiated by the [4Fe-4S]-dependent cleavage of the SAM into methionine and the 5'-deoxyadenosyl radical. |
PDB |
2A5H; |
Organisms |
-Eubacteria -Archea |
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Family |
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Links |
Enzyme (activities) 5.4.3.2
BRENDA (activities) 5.4.3.2
KEGG (pathways) 5.4.3.2
PLPMDB (PLP mutants) 5.4.3.2
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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.; Frey, P. A. (2001) Identification of lysine 346 as a functionally important residue for pyridoxal 5'-phosphate binding and catalysis in lysine 2, 3-aminomutase from Bacillus subtilis Biochemistry 40 596-602. 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 |
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last changed |
2019/06/20 13:38 |
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