EC |
4.3.1.28 |
Accepted name: |
L-lysine cyclodeaminase |
Reaction: |
L-lysine = L-pipecolate + NH3 |
Other name(s): |
rapL (gene name); fkbL (gene name); tubZ (gene name); visC (gene name) |
Systematic name: |
L-lysine ammonia-lyase (cyclizing; ammonia-forming) |
Comments: |
Requires bound NAD+. The enzyme produces the non-proteinogenic amino acid L-pipecolate, which is incorporated into multiple secondary metabolite products, including rapamycin, tobulysin, virginiamycin and pristinamycin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Khaw, L.E., Bohm, G.A., Metcalfe, S., Staunton, J. and Leadlay, P.F. Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase. J. Bacteriol. 180 (1998) 809–814. [PMID: 9473033] |
2. |
Gatto, G.J., Jr., Boyne, M.T., 2nd, Kelleher, N.L. and Walsh, C.T. Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster. J. Am. Chem. Soc. 128 (2006) 3838–3847. [DOI] [PMID: 16536560] |
3. |
Tsotsou, G.E. and Barbirato, F. Biochemical characterisation of recombinant Streptomyces pristinaespiralis L-lysine cyclodeaminase. Biochimie 89 (2007) 591–604. [DOI] [PMID: 17291665] |
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[EC 4.3.1.28 created 2012] |
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