+ 2 reduced
ferredoxin
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase
(Redirected from HMB-PP reductase)
| 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.17.7.4 | ||||||||
| CAS no. | 512789-14-9 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase (EC 1.17.7.4, isopentenyl-diphosphate:NADP+ oxidoreductase, LytB, (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase, HMBPP reductase, IspH, LytB/IspH) is an enzyme in the non-mevalonate pathway. It acts on (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate (HMB-PP).[1][2][3]
The enzyme characterised from Zymomonas mobilis and Plasmodium falciparum gives a mixture of dimethylallyl pyrophosphate and isopentenyl pyrophosphate in the ratio of five to one.[4][5][6]
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase is an iron-sulfur protein that contains an unusual [4Fe-4S] cluster.[7][8]
References
[edit]- ↑ Rohdich F, Hecht S, Gärtner K, Adam P, Krieger C, Amslinger S, Arigoni D, Bacher A, Eisenreich W (February 2002). "Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein". Proceedings of the National Academy of Sciences of the United States of America. 99 (3): 1158–63. Bibcode:2002PNAS...99.1158R. doi:10.1073/pnas.032658999. PMC 122160. PMID 11818558.
- ↑ Hintz M, Reichenberg A, Altincicek B, Bahr U, Gschwind RM, Kollas AK, Beck E, Wiesner J, Eberl M, Jomaa H (December 2001). "Identification of (E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate as a major activator for human gammadelta T cells in Escherichia coli". FEBS Letters. 509 (2): 317–22. doi:10.1016/s0014-5793(01)03191-x. PMID 11741609.
- ↑ Gräwert T, Kaiser J, Zepeck F, Laupitz R, Hecht S, Amslinger S, Schramek N, Schleicher E, Weber S, Haslbeck M, Buchner J, Rieder C, Arigoni D, Bacher A, Eisenreich W, Rohdich F (October 2004). "IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis". Journal of the American Chemical Society. 126 (40): 12847–55. doi:10.1021/ja0471727. PMID 15469281.
- ↑ Charon, L.; Pale-Grosdemange, C.; Rohmer, M. (1999). "On the reduction steps in the mevalonate independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis in the bacterium Zymomonas mobilis". Tetrahedron Lett. 40 (40): 7231–7234. doi:10.1016/s0040-4039(99)01531-2.
- ↑ Röhrich RC, Englert N, Troschke K, Reichenberg A, Hintz M, Seeber F, Balconi E, Aliverti A, Zanetti G, Köhler U, Pfeiffer M, Beck E, Jomaa H, Wiesner J (November 2005). "Reconstitution of an apicoplast-localised electron transfer pathway involved in the isoprenoid biosynthesis of Plasmodium falciparum". FEBS Letters. 579 (28): 6433–8. doi:10.1016/j.febslet.2005.10.037. PMID 16289098.
- ↑ Enzyme 1.17.7.4 at KEGG Pathway Database.
- ↑ Wolff M, Seemann M, Tse Sum Bui B, Frapart Y, Tritsch D, Garcia Estrabot A, Rodríguez-Concepción M, Boronat A, Marquet A, Rohmer M (April 2003). "Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein". FEBS Letters. 541 (1–3): 115–20. doi:10.1016/s0014-5793(03)00317-x. PMID 12706830.
- ↑ Faus, Isabelle; Reinhard, Annegret; Rackwitz, Sergej; et al. (2015). "Isoprenoid Biosynthesis in Pathogenic Bacteria: Nuclear Resonance Vibrational Spectroscopy Provides Insight into the Unusual [4Fe-4S] Cluster of the E. Coli LytB/IspH Protein". Angewandte Chemie International Edition. 54 (43): 12584–12587. doi:10.1002/anie.201502494. PMC 4609541. PMID 26118554.
