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Isopentenyl phosphate kinase 
Summary
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
| 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 | ||||||||
| |||||||||
- ATP + isopentenyl phosphate ADP + isopentenyl diphosphate
This enzyme takes part in the mevalonate pathway in Archaea.
References edit
- ^ Grochowski LL, Xu H, White RH (May 2006). "Methanocaldococcus jannaschii uses a modified mevalonate pathway for biosynthesis of isopentenyl diphosphate". Journal of Bacteriology. 188 (9): 3192–8. doi:10.1128/JB.188.9.3192-3198.2006. PMC 1447442. PMID 16621811.
- ^ Lange BM, Croteau R (November 1999). "Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway: isopentenyl monophosphate kinase catalyzes the terminal enzymatic step". Proceedings of the National Academy of Sciences of the United States of America. 96 (24): 13714–9. doi:10.1073/pnas.96.24.13714. PMC 24130. PMID 10570138.
- ^ Chen M, Poulter CD (January 2010). "Characterization of thermophilic archaeal isopentenyl phosphate kinases". Biochemistry. 49 (1): 207–17. doi:10.1021/bi9017957. PMC 3856865. PMID 19928876.
- ^ Mabanglo MF, Schubert HL, Chen M, Hill CP, Poulter CD (May 2010). "X-ray structures of isopentenyl phosphate kinase". ACS Chemical Biology. 5 (5): 517–27. doi:10.1021/cb100032g. PMC 2879073. PMID 20402538.
External links edit
- Isopentenyl+phosphate+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
