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Information on EC 4.2.1.111 - 1,5-anhydro-D-fructose dehydratase for references in articles please use BRENDA:EC4.2.1.111Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Pezizales
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1,5-anhydro-D-fructose dehydratase
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1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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glycogen degradation III (via anhydrofructose)
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1,5-anhydro-D-fructose hydro-lyase (ascopyrone-M-forming)
This enzyme catalyses one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose [1,2]. The other enzymes involved in this pathway are EC 4.2.1.110 (aldos-2-ulose dehydratase), EC 4.2.2.13 [exo-(1->4)-alpha-D-glucan lyase] and EC 5.3.2.7 (ascopyrone tautomerase). Requires divalent (Ca2+ or Mg2+) or monovalent cations (Na+) for optimal activity. Unlike EC 4.2.1.110, the enzyme is specific for 1,5-anhydro-D-fructose as substrate and shows no activity towards aldose-2-uloses such as 2-dehydroglucose [1,2,3]. In addition, it is inhibited by its end-product ascopyrone M [2] and it cannot convert ascopyrone M into microthecin, as can EC 4.2.1.110.
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1,5-anhydro-D-arabino-hex-2-ulose dehydratase
1,5-anhydro-D-fructose 4-dehydratase
1,5-anhydro-D-fructose hydro-lyase
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1,5-anhydro-D-fructose hydrolyase
1,5-anhydro-D-arabino-hex-2-ulose dehydratase
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1,5-anhydro-D-arabino-hex-2-ulose dehydratase
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1,5-anhydro-D-fructose 4-dehydratase
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1,5-anhydro-D-fructose 4-dehydratase
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1,5-anhydro-D-fructose hydrolyase
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1,5-anhydro-D-fructose hydrolyase
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AF dehydratase
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AFDH
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1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
additional information
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1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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i.e. 1,5-anhydro-D-arabino-hex-2-ulose. This enzyme catalyses one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose
i.e.ascopyrone M
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ir
1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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i.e. 1,5-anhydro-D-arabino-hex-2-ulose
i.e.ascopyrone M
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ir
1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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AFDH is highly specific towards 1,5-anhydro-D-fructose
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1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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AFDH is highly specific towards 1,5-anhydro-D-fructose
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1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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i.e. 1,5-anhydro-D-arabino-hex-2-ulose
i.e.ascopyrone M
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ir
1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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AFDH is highly specific towards 1,5-anhydro-D-fructose
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1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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i.e. 1,5-anhydro-D-arabino-hex-2-ulose
i.e.ascopyrone M
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ir
1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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AFDH is highly specific towards 1,5-anhydro-D-fructose
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the enzyme is inactive towards: glucosone, glucose, galactose, mannose, fructose, ribose and gamma-gluconolactone
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AFDH is inactive towards D-glucose, D-galactose, D-mannose, D-fructose and D-ribose
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AFDH is inactive towards D-glucose, D-galactose, D-mannose, D-fructose and D-ribose
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AFDH is inactive towards D-glucose, D-galactose, D-mannose, D-fructose and D-ribose
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additional information
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AFDH is inactive towards D-glucose, D-galactose, D-mannose, D-fructose and D-ribose
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1,5-anhydro-D-fructose
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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i.e. 1,5-anhydro-D-arabino-hex-2-ulose. This enzyme catalyses one of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose
i.e.ascopyrone M
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ir
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Ca2+
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the activity increases by around 2fold in the presence of 10 mM CaCl2
CaCl2
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requirement of alkaline earth metal ion for activity. 10 mM, around 2fold increase in activity
Mg2+
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the activity increases by around 2fold in the presence of 25 mM MgCl2
MgCl2
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requirement of alkaline earth metal ion for activity. 25 mM, around 2fold increase in activity
Na+
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the activity increases by around 2fold in the presence of 0.1 M NaCl
NaCl
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0.1 mM, around 2fold increase in activity
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EDTA
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50 mM, 84% inhibition
EDTA
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50 mM of EDTA inhibits AFDH activity by 84%
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6.5
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optimal pH-range is 5.9-7.0
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5.9 - 7
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optimal pH-range
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98000
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x * 98000, SDS-PAGE
98000
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2 * 98000, SDS-PAGE
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dimer
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2 * 98000, SDS-PAGE
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x * 98000, SDS-PAGE
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x * 98000, SDS-PAGE
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Yu, S.; Refdahl, C.; Lundt, I.
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
120-129
2004
Anthracobia melaloma
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Yu, S.; Fiskesund, R.
The anhydrofructose pathway and its possible role in stress response and signaling
Biochim. Biophys. Acta
1760
1314-1322
2006
Anthracobia melaloma, Plicaria anthracina, Plicaria leiocarpa
brenda
Lundt, I.; Yu, S.
1,5-Anhydro-D-fructose: biocatalytic and chemical synthetic methods for the preparation, transformation and derivatization
Carbohydr. Res.
345
181-190
2010
Anthracobia melaloma, Peziza petersii, Plicaria anthracina, Plicaria leiocarpa
brenda
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