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In enzymology, a 1,5-anhydro-D-fructose dehydratase (EC 4.2.1.111) is an enzyme that catalyzes the chemical reaction

1,5-anhydro-D-fructose ⇌{displaystyle rightleftharpoons } 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H₂O

Hence, this enzyme has one substrate, 1,5-anhydro-D-fructose, and two products, 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose and H₂O.

It catalyzes two steps in the anhydrofructose pathway process.^[1]

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is 1,5-anhydro-D-fructose hydro-lyase (ascopyrone-M-forming). Other names in common use include 1,5-anhydro-D-fructose 4-dehydratase, 1,5-anhydro-D-fructose hydrolyase, 1,5-anhydro-D-arabino-hex-2-ulose dehydratase, AFDH, AF dehydratase, and 1,5-anhydro-D-fructose hydro-lyase.

References

• 
  Yu S, Refdahl C, Lundt I (2004). "Enzymatic description of the anhydrofructose pathway of glycogen degradation; I. Identification and purification of anhydrofructose dehydratase, ascopyrone tautomerase and alpha-1,4-glucan lyase in the fungus Anthracobia melaloma". Biochim. Biophys. Acta. 1672 (2): 120–9. doi:10.1016/j.bbagen.2004.03.004. PMID 15110094..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
  


• 
  Yu S, Fiskesund R (2006). "The anhydrofructose pathway and its possible role in stress response and signaling". Biochim. Biophys. Acta. 1760 (9): 1314–22. doi:10.1016/j.bbagen.2006.05.007. PMID 16822618.
  


• 
  Yu S (2005). "Enzymatic description of the anhydrofructose pathway of glycogen degradation II. Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-D-fructose to microthecin with ascopyrone M as the intermediate". Biochim. Biophys. Acta. 1723 (1–3): 63–73. doi:10.1016/j.bbagen.2005.01.004. PMID 15716041.
  

See also

• Anhydrofructose pathway


• Ascopyrone tautomerase


• exo-(1→4)-α-D-glucan lyase