Isopentenyl phosphate kinase
| Isopentenyl phosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.26 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Isopentenyl phosphate kinase (EC 2.7.4.26) is an enzyme with systematic name ATP:isopentenyl phosphate phosphotransferase.[1][2][3][4] This enzyme catalyses the following chemical reaction
This enzyme takes part in the mevalonate pathway in Archaea.
References
- ^ Grochowski, L.L.; Xu, H.; White, R.H. (2006). "Methanocaldococcus jannaschii uses a modified mevalonate pathway for biosynthesis of isopentenyl diphosphate". J. Bacteriol. 188: 3192–3198. doi:10.1128/JB.188.9.3192-3198.2006. PMC 1447442. PMID 16621811.
- ^ Lange, B.M.; Croteau, R. (1999). "Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step". Proc. Natl. Acad. Sci. USA. 96 (24): 13714–13719. doi:10.1073/pnas.96.24.13714. PMID 10570138.
- ^ Chen, M.; Poulter, C.D. (2010). "Characterization of thermophilic archaeal isopentenyl phosphate kinases". Biochemistry. 49 (1): 207–217. doi:10.1021/bi9017957. PMID 19928876.
- ^ Mabanglo, M.F.; Schubert, H.L.; Chen, M.; Hill, C.P.; Poulter, C.D. (2010). "X-ray structures of isopentenyl phosphate kinase". ACS Chem. Biol. 5 (5): 517–527. doi:10.1021/cb100032g. PMID 20402538.
External links
- Isopentenyl+phosphate+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)