6-phospho-3-hexuloisomerase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 5.3.1.27 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
6-phospho-3-hexuloisomerase (EC 5.3.1.27, 3-hexulose-6-phosphate isomerase, phospho-3-hexuloisomerase, PHI, 6-phospho-3-hexulose isomerase, YckF) is an enzyme with systematic name D-arabino-hex-3-ulose-6-phosphate isomerase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- D-arabino-hex-3-ulose 6-phosphate D-fructose 6-phosphate
This enzyme plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation.
References
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ Martinez-Cruz LA, Dreyer MK, Boisvert DC, Yokota H, Martinez-Chantar ML, Kim R, Kim SH (February 2002). "Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution infers a molecular function of 3-hexulose-6-phosphate isomerase". Structure. 10 (2): 195–204. doi:10.1016/s0969-2126(02)00701-3. PMID 11839305.
- ↑ Taylor EJ, Charnock SJ, Colby J, Davies GJ, Black GW (August 2001). "Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis" (PDF). Acta Crystallographica Section D. 57 (Pt 8): 1138–40. doi:10.1107/s090744490100748x. PMID 11468398.
External links
- 6-phospho-3-hexuloisomerase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.