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 system 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
- ^ Ferenci, T., Strøm, T. and Quayle, J.R. (1974). "Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from Methylococcus capsulatus". Biochem. J. 144: 477–486. PMID 4219834.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kato, N., Ohashi, H., Tani, Y. and Ogata, K. (1978). "3-Hexulosephosphate synthase from Methylomonas aminofaciens 77a. Purification, properties and kinetics". Biochim. Biophys. Acta. 523: 236–244. PMID 564713.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Yanase, H., Ikeyama, K., Mitsui, R., Ra, S., Kita, K., Sakai, Y. and Kato, N. (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 Microbiol. Lett. 135: 201–205. PMID 8595859.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Yurimoto, H., Kato, N. and Sakai, Y. (2005). "Assimilation, dissimilation, and detoxification of formaldehyde, a central metabolic intermediate of methylotrophic metabolism". Chem. Rec. 5: 367–375. PMID 16278835.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kato, N., Yurimoto, H. and Thauer, R.K. (2006). "The physiological role of the ribulose monophosphate pathway in bacteria and archaea". Biosci. Biotechnol. Biochem. 70: 10–21. PMID 16428816.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Orita, I., Yurimoto, H., Hirai, R., Kawarabayasi, Y., Sakai, Y. and Kato, N. (2005). "The archaeon Pyrococcus horikoshii possesses a bifunctional enzyme for formaldehyde fixation via the ribulose monophosphate pathway". J. Bacteriol. 187: 3636–3642. PMID 15901685.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kato, N., Miyamoto, N., Shimao, M. and Sakazawa, C. (1988). "3-Hexulose phosphate pynthase from a new facultative methylotroph, Mycobacterium gastri MB19". Agric. Biol. Chem. 52: 2659–2661.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- 3-hexulose-6-phosphate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)