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 | ||||||||
| |||||||||
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
- ↑ Khaw, L.E.; Bohm, G.A.; Metcalfe, S.; Staunton, J.; 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.
- ↑ Gatto, G.J.; Boyne, M.T.; Kelleher, N.L.; 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.
- ↑ Tsotsou, G.E.; 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)
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