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B6db activities: 5.4.3.3

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.
Annotation
Kapatral et al. describe a putative lysine utilization operon in Fusarium. The first step of the reaction is the formation of L--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--lysine to 3,5-diaminohexanoic acid by L--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--lysine, is located proximal to the ORF encoding the 2,3-aminomutase.
Organisms -Eubacteria
 
 
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
 
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
 
last changed 2010/02/02 10:18

B6db activities