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en>Frietjes: /* Dyadic operators */
2014-01-16T00:19:13Z
<p><span class="autocomment">Dyadic operators</span></p>
<p><b>New page</b></p><div>{{Infobox enzyme<br />
| Name = 3-hexulose-6-phosphate synthase<br />
| EC_number = 4.1.2.43<br />
| CAS_number = <br />
| IUBMB_EC_number = 4/1/2/43<br />
| GO_code = <br />
| image = <br />
| width = <br />
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}}<br />
'''3-hexulose-6-phosphate synthase''' ({{EC number|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)''.<ref>{{cite journal | title = Purification and properties of 3-hexulose phosphate synthase and phospho-3-hexuloisomerase from <em>Methylococcus capsulatus</em> |author = Ferenci, T., Str&oslash;m, T. and Quayle, J.R. |journal = Biochem. J. |year = 1974 |volume = 144 |pages = 477–486 |pmid = 4219834}}</ref><ref>{{cite journal | title = 3-Hexulosephosphate synthase from <em>Methylomonas aminofaciens</em> 77a. Purification, properties and kinetics |author = Kato, N., Ohashi, H., Tani, Y. and Ogata, K. |journal = Biochim. Biophys. Acta |year = 1978 |volume = 523 |pages = 236–244 |pmid = 564713}}</ref><ref>{{cite journal | title = Cloning and sequence analysis of the gene encoding 3-hexulose-6-phosphate synthase from the methylotrophic bacterium, <em>Methylomonas aminofaciens</em> 77a, and its expression in <em>Escherichia coli</em> |author = Yanase, H., Ikeyama, K., Mitsui, R., Ra, S., Kita, K., Sakai, Y. and Kato, N. |journal = FEMS Microbiol. Lett. |year = 1996 |volume = 135 |pages = 201–205 |pmid = 8595859}}</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 <em>Pyrococcus horikoshii</em> 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 = 3-Hexulose phosphate pynthase from a new facultative methylotroph, <em>Mycobacterium gastri</em> MB19 |author = Kato, N., Miyamoto, N., Shimao, M. and Sakazawa, C. |journal = Agric. Biol. Chem. |year = 1988 |volume = 52 |pages = 2659–2661 |pmid = }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]<br />
<br />
: D-arabino-hex-3-ulose 6-phosphate <math>\rightleftharpoons</math> D-ribulose 5-phosphate + [[formaldehyde]]<br />
<br />
This enzyme requires Mg<sup>2+</sup> or Mn<sup>2+</sup> for maximal activity.<br />
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== References ==<br />
{{reflist}}<br />
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== External links ==<br />
* {{MeshName|3-hexulose-6-phosphate+synthase}}<br />
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[[Category:EC 4.1.2]]</div>
en>Frietjes