1,5-anhydro-D-fructose dehydratase

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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 $\rightleftharpoons$ 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.

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.

[edit] References

IUBMB entry for 4.2.1.111
BRENDA references for 4.2.1.111 (Recommended.)
PubMed references for 4.2.1.111
PubMed Central references for 4.2.1.111
Google Scholar references for 4.2.1.111
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Yu S, Fiskesund R (2006). "The anhydrofructose pathway and its possible role in stress response and signaling". Biochim. Biophys. Acta. 1760: 1314–22. 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: 63–73. PMID 15716041.