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{{Infobox enzyme
| Name = 6-phospho-3-hexuloisomerase
| EC_number = 5.3.1.27
| CAS_number =
| IUBMB_EC_number = 5/3/1/27
| GO_code =
| image =
| width =
| caption =
}}
'''6-phospho-3-hexuloisomerase''' ({{EC number|5.3.1.27}}, ''3-hexulose-6-phosphate isomerase'', ''phospho-3-hexuloisomerase'', ''PHI'', ''6-phospho-3-hexulose isomerase'', ''YckF'') is an [[enzyme]] with system name ''D-arabino-hex-3-ulose-6-phosphate isomerase''.<ref>{{cite journal | title = Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from Methylococcus capsulatus |author = Ferenci, T., Strøm, T. and Quayle, J.R. |journal = Biochem. J. |year = 1974 |volume = 144 |pages = 477–486 |pmid = 4219834}}</ref><ref>{{cite journal | title = Assimilation, dissimilation, and detoxification of formaldehyde, a central metabolic intermediate of methylotrophic metabolism |author = Yurimoto, H., Kato, N. and Sakai, Y. |journal = Chem. Rec. |year = 2005 |volume = 5 |pages = 367–375 |pmid = 16278835}}</ref><ref>{{cite journal | title = The physiological role of the ribulose monophosphate pathway in bacteria and archaea |author = Kato, N., Yurimoto, H. and Thauer, R.K. |journal = Biosci. Biotechnol. Biochem. |year = 2006 |volume = 70 |pages = 10–21 |pmid = 16428816}}</ref><ref>{{cite journal | title = The archaeon Pyrococcus horikoshii possesses a bifunctional enzyme for formaldehyde fixation via the ribulose monophosphate pathway |author = Orita, I., Yurimoto, H., Hirai, R., Kawarabayasi, Y., Sakai, Y. and Kato, N. |journal = J. Bacteriol. |year = 2005 |volume = 187 |pages = 3636–3642 |pmid = 15901685}}</ref><ref>{{cite journal | title = Crystal structure of MJ1247 protein from M. jannaschii at 2.0 Å resolution infers a molecular function of 3-hexulose-6-phosphate isomerase |author = Martinez-Cruz, L.A., Dreyer, M.K., Boisvert, D.C., Yokota, H., Martinez-Chantar, M.L., Kim, R. and Kim, S.H. |journal = Structure |year = 2002 |volume = 10 |pages = 195–204 |pmid = 11839305}}</ref><ref>{{cite journal | title = Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis |author = Taylor, E.J., Charnock, S.J., Colby, J., Davies, G.J. and Black, G.W. |journal = Acta Crystallogr. D Biol. Crystallogr. |year = 2001 |volume = 57 |pages = 1138–1140 |pmid = 11468398}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: D-arabino-hex-3-ulose 6-phosphate <math>\rightleftharpoons</math> D-fructose 6-phosphate

This enzyme plays a key role in the ribulose-monophosphate cycle of [[formaldehyde]] fixation.

== References ==
{{reflist}}

== External links ==
* {{MeshName|6-phospho-3-hexuloisomerase}}

[[Category:EC 5.3.1]]

Dodecahedral number - Revision history

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