EC number:4.3.1.28
| ID: | 4.3.1.28 |
|---|---|
| Description: | L-lysine cyclodeaminase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.3.1.28 |
| BRENDA Enzyme Link: | BRENDA 4.3.1.28 |
| KEGG Enzyme Link: | KEGG4.3.1.28 |
| BioCyc Enzyme Link: | BioCyc 4.3.1.28 |
| ExPASy Enzyme Link: | ExPASy4.3.1.28 |
| EC2PDB Enzyme Link: | EC2PDB 4.3.1.28 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.3.1.28 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.3.1.28 |
| IntEnz Enzyme Link: | IntEnz 4.3.1.28 |
| MEDLINE Enzyme Link: | MEDLINE 4.3.1.28 |
| RHEA:34303 | L-lysine = L-pipecolate + NH4(+) |
| RULE(radius=1) | ([*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[NH2;+0:6])>>[*:1]-[CH;+0:2](-[*:3])-[NH;+0:6]-[*:5].[NH3;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Mutational biosynthesis of novel rapamycins by a strain of Streptomyces hygroscopicus NRRL 5491 disrupted in rapL, encoding a putative lysine cyclodeaminase. | Khaw LE, Böhm GA, Metcalfe S, Staunton J, Leadlay PF | 1998 Feb | 9473033 |
| Biochemical characterisation of recombinant Streptomyces pristinaespiralis L-lysine cyclodeaminase. | Tsotsou GE, Barbirato F | 2007 May | 17291665 |
| Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster. | Gatto GJ Jr, Boyne MT 2nd, Kelleher NL, Walsh CT | 2006 Mar 22 | 16536560 |