Biology:L-lysine cyclodeaminase
From HandWiki
| L-lysine cyclodeaminase | |||||||||
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| 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] L-pipecolate + NH3
This enzyme requires bound NAD+.
References
- ↑ "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. February 1998. PMID 9473033.
- ↑ "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. March 2006. doi:10.1021/ja0587603. PMID 16536560.
- ↑ "Biochemical characterisation of recombinant Streptomyces pristinaespiralis L-lysine cyclodeaminase". Biochimie 89 (5): 591–604. May 2007. 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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