L-lysine cyclodeaminase

L-lysine cyclodeaminase
Identifiers
EC number	4.3.1.28
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

L-lysine cyclodeaminase (EC 4.3.1.28, rapL (gene), fkbL (gene), tubZ (gene), visC (gene)) is an enzyme with systematic name L-lysine ammonia-lyase (cyclizing; ammonia-forming).^[1][2][3] This enzyme catalyses the following chemical reaction

L-lysine $\rightleftharpoons$ L-pipecolate + NH₃

This enzyme requires bound NAD⁺.

References

1. Khaw, L.E., Bohm, G.A., Metcalfe, S., Staunton, J. and Leadlay, P.F. (1998). "Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase". J. Bacteriol. 180 (4): 809–814. PMID 9473033.
2. Gatto, G.J., Jr., Boyne, M.T., 2nd, Kelleher, N.L. and Walsh, C.T. (2006). "Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster". J. Am. Chem. Soc. 128: 3838–3847. doi:10.1021/ja0587603. PMID 16536560.
3. Tsotsou, G.E. and Barbirato, F. (2007). "Biochemical characterisation of recombinant Streptomyces pristinaespiralis L-lysine cyclodeaminase". Biochimie 89 (5): 591–604. doi:10.1016/j.biochi.2006.12.008. PMID 17291665.

External links

• L-lysine cyclodeaminase at the US National Library of Medicine Medical Subject Headings (MeSH)