| Trans,polycis-decaprenyl diphosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.86 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Trans,polycis-decaprenyl diphosphate synthase ( EC 2.5.1.86, Rv2361c, (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate synthase) is an enzyme with systematic name (2Z,6E)-farnesyl-diphosphate:isopentenyl-diphosphate farnesylcistransferase (adding 7 isopentenyl units) . [1] [2] [3] This enzyme catalyses the following chemical reaction
- (2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate 7 diphosphate + trans,octacis-decaprenyl diphosphate
The enzyme is involved in the biosynthesis of decaprenyl phosphate.
References
- ^ Kaur D, Brennan PJ, Crick DC (November 2004). "Decaprenyl diphosphate synthesis in Mycobacterium tuberculosis". Journal of Bacteriology. 186 (22): 7564–70. doi: 10.1128/JB.186.22.7564-7570.2004. PMC 524883. PMID 15516568.
- ^ Wang W, Dong C, McNeil M, Kaur D, Mahapatra S, Crick DC, Naismith JH (August 2008). "The structural basis of chain length control in Rv1086". Journal of Molecular Biology. 381 (1): 129–40. doi: 10.1016/j.jmb.2008.05.060. PMC 2527485. PMID 18597781.
- ^ Crick DC, Schulbach MC, Zink EE, Macchia M, Barontini S, Besra GS, Brennan PJ (October 2000). "Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and Mycobacterium smegmatis". Journal of Bacteriology. 182 (20): 5771–8. doi: 10.1128/JB.182.20.5771-5778.2000. PMC 94699. PMID 11004176.
External links
- Trans,polycis-decaprenyl+diphosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
