4-Hydroxy-3-methylbut-2-enyl diphosphate reductase
(Redirected from HMB-PP reductase)
| 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.17.1.2 | ||||||||
| CAS no. | 512789-14-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase (EC 1.17.1.2, 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 upon (E)-4-Hydroxy-3-methyl-but-2-enyl pyrophosphate (or "HMB-PP").[1][2][3][4][5][6]
- (1) isopentenyl diphosphate + NAD(P)+ + H2O (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
- (2) dimethylallyl diphosphate + NAD(P)+ + H2O (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H + H+
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase is an iron-sulfur protein that contains either a [3Fe-4S] or a [4Fe-4S] cluster.
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.
- ^ 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.
- ^ 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.
- ^ 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.
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |