L-lysine cyclodeaminase

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L-lysine cyclodeaminase
Identifiers
EC no. 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
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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 L-pipecolate + NH3

This enzyme requires bound NAD+.

References

  1. Khaw LE, Böhm GA, Metcalfe S, Staunton J, Leadlay PF (February 1998). "Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase". Journal of Bacteriology. 180 (4): 809–14. doi:10.1128/JB.180.4.809-814.1998. PMC   106958 . PMID   9473033.
  2. Gatto GJ, Boyne MT, Kelleher NL, Walsh CT (March 2006). "Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster". Journal of the American Chemical Society. 128 (11): 3838–47. Bibcode:2006JAChS.128.3838G. doi:10.1021/ja0587603. PMID   16536560.
  3. Tsotsou GE, Barbirato F (May 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.