L-lysine cyclodeaminase
| 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 | ||||||||
| |||||||||
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
- Llysine L-pipecolate + NH3
This enzyme requires bound NAD+.
References[edit]
- ^ 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. PMC 106958. PMID 9473033.
- ^ 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. doi:10.1021/ja0587603. PMID 16536560.
- ^ 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.
External links[edit]
- L-lysine+cyclodeaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
