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Enzyme Nomenclature
Information on EC 4.2.1.111 - 1,5-anhydro-D-fructose dehydratase
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The expected taxonomic range for this enzyme is: Pezizales
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EC NUMBER 
COMMENTARY 
4.2.1.111
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RECOMMENDED NAME
GeneOntology No.
1,5-anhydro-D-fructose dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
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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CAS REGISTRY NUMBER
COMMENTARY
9044-86-4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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?
additional information
?
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the enzyme is inactive towards: glucosone, glucose, galactose, mannose, fructose, ribose and gamma-gluconolactone
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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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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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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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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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.9 - 7
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
98000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.1.111)
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