The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

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]
[EC 4.3.1.28 created 2012]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald