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5.4.3.3 |
Description |
Beta-lysine 5,6-aminomutase |
Alternative names |
Beta-lysine mutase. |
Catalyzed reaction |
(3S)-3,6-DIaminohexanoate = (3S,5S)-3,5-diaminohexanoate. |
Cofactor |
Cobalamin. Pyridoxal-phosphate. |
Comments |
This activity is included in EC 5.4.3.4, and the corresponding sequences have therefore been included in the 5.4.3.4 family.
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Annotation
Kapatral et al. describe a putative lysine utilization operon in Fusarium. The first step of the reaction is the formation of L-ß-lysine from L-lysine by L-lysine 2,3-aminomutase, and F. nucleatum contains a homolog of the L-lysine 2,3-aminomutase from Clostridium subterminale. The second step is conversion of L-ß-lysine to 3,5-diaminohexanoic acid by L-ß-lysine 5,6-aminomutase. A homolog of the D-lysine 5,6-aminomutase (5.4.3.4) of Clostridium sticklandii, which also acts on L-ß-lysine, is located proximal to the ORF encoding the 2,3-aminomutase. |
Organisms |
-Eubacteria |
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Links |
Enzyme (activities) 5.4.3.3
BRENDA (activities) 5.4.3.3
KEGG (pathways) 5.4.3.3
PLPMDB (PLP mutants) 5.4.3.3
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References |
Kapatral V, Anderson I, Ivanova N, Reznik G, Los T, et al. (2002) Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum strain ATCC 25586 J Bacteriol 184 2005-18. Barker, H. A.; Kahn, J. M.; Hedrick, L. (1982) Pathway of lysine degradation in Fusobacterium nucleatum J Bacteriol 152 201-7. Baker, J.J.; van der Drift, C.; Stadtman, T.C. (1973) Purification and properties of beta-lysine mutase, a pyridoxal phosphate and B12 coenzyme dependent enzyme Biochemistry 12 1054-63. Articles on 5.4.3.3 |
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last changed |
2019/06/20 13:38 |
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