3-hexulose-6-phosphate synthase
| 3-hexulose-6-phosphate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.2.43 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
3-hexulose-6-phosphate synthase (EC 4.1.2.43, D-arabino-3-hexulose 6-phosphate formaldehyde-lyase, 3-hexulosephosphate synthase, 3-hexulose phosphate synthase, HPS) is an enzyme with systematic name D-arabino-hex-3-ulose-6-phosphate formaldehyde-lyase (D-ribulose-5-phosphate-forming).[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction
- D-arabino-hex-3-ulose 6-phosphate D-ribulose 5-phosphate + formaldehyde
This enzyme requires Mg2+ or Mn2+ for maximal activity.
References[edit]
- ^ Ferenci T, Strom T, Quayle JR (December 1974). "Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from Methylococcus capsulatus". The Biochemical Journal. 144 (3): 477–86. doi:10.1042/bj1440477. PMC 1168525. PMID 4219834.
- ^ Kato N, Ohashi H, Tani Y, Ogata K (March 1978). "3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics". Biochimica et Biophysica Acta (BBA) - Enzymology. 523 (1): 236–44. doi:10.1016/0005-2744(78)90026-8. PMID 564713.
- ^ Yanase H, Ikeyama K, Mitsui R, Ra S, Kita K, Sakai Y, Kato N (January 1996). "Cloning and sequence analysis of the gene encoding 3-hexulose-6-phosphate synthase from the methylotrophic bacterium, Methylomonas aminofaciens 77a, and its expression in Escherichia coli". FEMS Microbiology Letters. 135 (2–3): 201–5. doi:10.1111/j.1574-6968.1996.tb07990.x. PMID 8595859.
- ^ Yurimoto H, Kato N, Sakai Y (2005). "Assimilation, dissimilation, and detoxification of formaldehyde, a central metabolic intermediate of methylotrophic metabolism". Chemical Record. 5 (6): 367–75. doi:10.1002/tcr.20056. PMID 16278835.
- ^ Kato N, Yurimoto H, Thauer RK (January 2006). "The physiological role of the ribulose monophosphate pathway in bacteria and archaea". Bioscience, Biotechnology, and Biochemistry. 70 (1): 10–21. doi:10.1271/bbb.70.10. PMID 16428816. S2CID 21562372.
- ^ Orita I, Yurimoto H, Hirai R, Kawarabayasi Y, Sakai Y, Kato N (June 2005). "The archaeon Pyrococcus horikoshii possesses a bifunctional enzyme for formaldehyde fixation via the ribulose monophosphate pathway". Journal of Bacteriology. 187 (11): 3636–42. doi:10.1128/jb.187.11.3636-3642.2005. PMC 1112069. PMID 15901685.
- ^ Kato, N.; Miyamoto, N.; Shimao, M.; Sakazawa, C. (1988). "3-Hexulose phosphate pynthase from a new facultative methylotroph, Mycobacterium gastri MB19". Agric. Biol. Chem. 52 (10): 2659–2661. doi:10.1271/bbb1961.52.2659.
External links[edit]
- 3-hexulose-6-phosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
