Biology:Trans,polycis-decaprenyl diphosphate synthase
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Short description: Class of enzymes
| Trans,polycis-decaprenyl diphosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 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 [math]\displaystyle{ \rightleftharpoons }[/math] 7 diphosphate + trans,octacis-decaprenyl diphosphate
The enzyme is involved in the biosynthesis of decaprenyl phosphate.
References
- ↑ "Decaprenyl diphosphate synthesis in Mycobacterium tuberculosis". Journal of Bacteriology 186 (22): 7564–70. November 2004. doi:10.1128/JB.186.22.7564-7570.2004. PMID 15516568.
- ↑ "The structural basis of chain length control in Rv1086". Journal of Molecular Biology 381 (1): 129–40. August 2008. doi:10.1016/j.jmb.2008.05.060. PMID 18597781.
- ↑ "Polyprenyl phosphate biosynthesis in Mycobacterium tuberculosis and Mycobacterium smegmatis". Journal of Bacteriology 182 (20): 5771–8. October 2000. doi:10.1128/JB.182.20.5771-5778.2000. PMID 11004176.
External links
- Trans,polycis-decaprenyl+diphosphate+synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
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