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Information on EC 4.2.1.110 - aldos-2-ulose dehydratase
for references in articles please use BRENDA:EC4.2.1.110
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IUBMB Comments
This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose [1,2]. Aldose-2-uloses such as 2-dehydroglucose can also act as substrates, but more slowly [1,2,4]. This is a bifunctional enzyme that acts as both a lyase and as an isomerase . Differs from EC 4.2.1.111, which can carry out only reaction (1a), is inhibited by its product and requires metal ions for activity .
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
showSynonyms
aldos-2-ulose dehydratase, pyranosone dehydratase, aldos-2-ulose dehydratase/isomerase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,5-anhydro-D-fructose dehydratase (microthecin-forming)
aldosulose-utilizing enzyme
AUDH
pyranosone dehydratase
aldosulose-utilizing enzyme
Polyporus obtusus AU124PD
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one
-
-
-
-
1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one
second of two consecutive reactions
-
-
-
1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
-
-
-
-
1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
first of two consecutive reactions
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-
-
1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
-
-
-
1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
overall reaction
-
-
-
1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
reaction scheme of the bifunctional enzyme, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydration
dehydration
Polyporus obtusus AU124PD
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
1,5-anhydro-D-fructose hydro-lyase (microthecin-forming)
This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose [1,2]. Aldose-2-uloses such as 2-dehydroglucose can also act as substrates, but more slowly [1,2,4]. This is a bifunctional enzyme that acts as both a lyase and as an isomerase [2]. Differs from EC 4.2.1.111, which can carry out only reaction (1a), is inhibited by its product and requires metal ions for activity [1].
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CAS REGISTRY NUMBER
COMMENTARY
101920-80-3
-
145266-93-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,5-D-anhydrofructose
microthecin
Substrates: dehydration reaction most likely follows an elimination mechanism, where Zn2+ acts as a Lewis acid polarizing the C2 oxo group of 1,5-D-anhydrofructose. The reaction intermediate ascopyrone M shows binding of this compound at two different sites, with direct coordination to Zn2+ in the propeller domain and as second sphere ligand of the metal ion in the cupin domain
Products: -
Products: -
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
Microthecium sobelii
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
Substrates: -
Products: microthecin + H2O
Products: microthecin + H2O
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: formation of microthecin is irreversible. 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
ir
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
Sarcodontia unicolor
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two 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 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
D-glucosone
cortalcerone + H2O
Polyporus obtusus
-
Substrates: i.e. D-arabino-hexos-2-ulose. The enzyme dehydrates D-arabino-hexos-2-ulose, generating a double bond between C-3 and C-4. This unsaturated compound is proposed to be the steady-state intermediate characterized by the spectral peak at 265 nm. This intermediate is chemically unstable and rearranges from its strained 1,5 ring form to a more stable 2,6 pyranose structure. Then the enzyme acts a second time, dehydrating this pyranose structure to form cortalcerone
Products: i.e. 5,6-dihydro-6-hydroxy-5-oxo-2H-pyran-6-carboxaldehyde
Products: i.e. 5,6-dihydro-6-hydroxy-5-oxo-2H-pyran-6-carboxaldehyde
?
D-glucosone
cortalcerone + H2O
Polyporus obtusus AU124PD
-
Substrates: i.e. D-arabino-hexos-2-ulose. The enzyme dehydrates D-arabino-hexos-2-ulose, generating a double bond between C-3 and C-4. This unsaturated compound is proposed to be the steady-state intermediate characterized by the spectral peak at 265 nm. This intermediate is chemically unstable and rearranges from its strained 1,5 ring form to a more stable 2,6 pyranose structure. Then the enzyme acts a second time, dehydrating this pyranose structure to form cortalcerone
Products: i.e. 5,6-dihydro-6-hydroxy-5-oxo-2H-pyran-6-carboxaldehyde
Products: i.e. 5,6-dihydro-6-hydroxy-5-oxo-2H-pyran-6-carboxaldehyde
?
D-xylosone
?
Polyporus obtusus
-
Substrates: i.e. D-threo-pentos-2-ulose
Products: the product absorbs at 260 nm but no conversion into a 230 nm-absorbing product occurs. Because of its strained nature, the intermediate still rearranges, losing UV absorbance, but since it lacks the 6th carbon, it cannot form a 2,6-pyranose ring to generate a second substrate for the enzyme
Products: the product absorbs at 260 nm but no conversion into a 230 nm-absorbing product occurs. Because of its strained nature, the intermediate still rearranges, losing UV absorbance, but since it lacks the 6th carbon, it cannot form a 2,6-pyranose ring to generate a second substrate for the enzyme
?
D-xylosone
?
Polyporus obtusus AU124PD
-
Substrates: i.e. D-threo-pentos-2-ulose
Products: the product absorbs at 260 nm but no conversion into a 230 nm-absorbing product occurs. Because of its strained nature, the intermediate still rearranges, losing UV absorbance, but since it lacks the 6th carbon, it cannot form a 2,6-pyranose ring to generate a second substrate for the enzyme
Products: the product absorbs at 260 nm but no conversion into a 230 nm-absorbing product occurs. Because of its strained nature, the intermediate still rearranges, losing UV absorbance, but since it lacks the 6th carbon, it cannot form a 2,6-pyranose ring to generate a second substrate for the enzyme
?
glucosone
cortalcerone + H2O
-
Substrates: 20% of the activity with 1,5-anhydro-D-fructose
Products: -
Products: -
?
glucosone
cortalcerone + H2O
Substrates: 2-keto glucose
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is bifunctional and is also active with glucosone and xylosone, the former is converted to cortalcerone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is bifunctional and is also active with glucosone and xylosone, the former is converted to cortalcerone
Products: -
Products: -
?
additional information
?
-
Polyporus obtusus
-
Substrates: no activity with fructose
Products: -
Products: -
?
additional information
?
-
Polyporus obtusus AU124PD
-
Substrates: no activity with fructose
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glucosone
cortalcerone + H2O
Substrates: 2-keto glucose
Products: -
Products: -
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
Microthecium sobelii
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two of the steps in the anhydrofructose pathway, which leads to the degradation of glycogen and starch via 1,5-anhydro-D-fructose. The other enzymes involved in this pathway are EC 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
Sarcodontia unicolor
-
Substrates: 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O (overall reaction), (1a) 1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O, (1b) 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one. This enzyme catalyses two 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 4.2.1.111 (1,5-anhydro-D-fructose dehydratase), EC 4.2.2.13 (exo-(1,4)-alpha-D-glucan lyase) and EC 5.3.3.15 (ascopyrone tautomerase). This is a bifunctional enzyme that acts as both a lyase and as an isomerase. Differs from EC 4.2.1.111, which can carry out only reaction 1a
Products: i.e. microthecin
Products: i.e. microthecin
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
the enzyme contains a structural Mg2+ located in loop region, metal binding site and structure, overview
Zn2+
the enzyme contains a structural Zn2+ located in loop regions and two zinc ions at the bottom of two putative active-site clefts in the propeller and the cupin domain, respectively. Catalysis is dependent on these two zinc ions, as their specific removal leads to loss of enzymatic activity, metal binding site and structure, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,5-anhydro-4-deoxy-D-glycero-hexo-2,3-diulose dihydrate
-
4 mM, 50% inhibition when 1,5-anhydro-D-fructose is used as the substrate at 5 mM and pH 5.8
1,5-Anhydro-D-fructose
substrate inhibition to AUDH at a concentration up to 10% (w/v)
microthecin
product inhibition to AUDH at a concentration up to 10% (w/v)
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KM VALUE [mM]
SUBSTRATE
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
5
at a pH lower than 5.0, the reaction rate is slower and there is a tendency for increased formation of degradation products (FHMK), at a pH higher than 5.5, there is a tendency for more APT dihydrate formation
5.8
-
formation of 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose
7.5
additional information
the reaction medium acidifies by itself due to unknown events related to the AUDH catalysed reaction
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
at a pH lower than 5.0, the reaction rate is slower and there is a tendency for increased formation of degradation products (FHMK), at a pH higher than 5.5, there is a tendency for more APT dihydrate formation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24
at temperatures higher than 24°C there is increased degradation of microthecin
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
removal of two zinc ions at the bottom of two putative active-site clefts in the propeller and the cupin domains leads to loss of enzymatic activity, although the structure of the Zn2+-depleted enzyme is very similar to that of native AUDH
physiological function
the bifunctional enzyme aldos-2-ulose dehydratase/isomerase participates in carbohydrate secondary metabolism, catalyzing the conversion of glucosone and 1,5-D-anhydrofructose to the secondary metabolites cortalcerone and microthecin, respectively
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AUD_PHACH
900
0
98746
Swiss-Prot
other Location (Reliability: 2)
A0A077PR60_XENBV
239
0
26406
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
98700
2 * 98700, recombinant enzyme, SDS-PAGE, 2 * 98746, sequence calculation, the AUDH subunit consists of three domains, all of beta-structure: the N-terminal domain with a beta-propeller fold, a middle domain containing two cupin folds and a C-terminal lectin domain
98746
2 * 98700, recombinant enzyme, SDS-PAGE, 2 * 98746, sequence calculation, the AUDH subunit consists of three domains, all of beta-structure: the N-terminal domain with a beta-propeller fold, a middle domain containing two cupin folds and a C-terminal lectin domain
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
additional information
homodimer
2 * 98700, recombinant enzyme, SDS-PAGE, 2 * 98746, sequence calculation, the AUDH subunit consists of three domains, all of beta-structure: the N-terminal domain with a beta-propeller fold, a middle domain containing two cupin folds and a C-terminal lectin domain
homodimer
Polyporus obtusus AU124PD
-
2 * 95000, SDS-PAGE
-
additional information
secondary, quarternary, and overall structure analysis, detailed overview
additional information
-
secondary, quarternary, and overall structure analysis, detailed overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Microthecin is found to be most stable in de-ionized water at a pH around 7.0 and stable in freeze-dried form. Under acidic conditions microthecin is degraded to 2-furyl-2-hydroxymethylketone (FHMK).
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the best solvent for AUDH-catalysed microthecin reaction is de-ionized water
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme in 0.1 M sodium phosphate buffer (pH 7.0), several months, the enzyme remains stable
Polyporus obtusus
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
precipitation with 20% (w/v) PEG 4000, DEAE-Sepharose column chromatography, and carboxymethyl-Sepharose column chromatography
Polyporus obtusus
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yu, S.
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
2005
Phanerodontia chrysosporium
brenda
Yu, S.; Fiskesund, R.
The anhydrofructose pathway and its possible role in stress response and signaling
Biochim. Biophys. Acta
1760
1314-1322
2006
Gracilariopsis lemaneiformis, Microthecium compressum, Microthecium sobelii, Morchella costata, Morchella vulgaris, Phanerodontia chrysosporium, Sarcodontia unicolor
brenda
Broberg, A.; Kenne, L.; Pedersen, M.
Presence of microthecin in the red alga Gracilariopsis lemaneiformis and its formation from 1,5-anhydro-D-fructose
Phytochemistry
41
151-154
1996
Gracilariopsis lemaneiformis
-
brenda
Yu, S.; Andreassen, M.; Lundt, I.
Enzymatic production of microthecin by aldos-2-ulose dehydratase from 1,5-anhydro-D-fructose and stability studies of microthecin
Biocatal. Biotransform.
26
169-176
2008
Phanerodontia chrysosporium (P84193)
-
brenda
Koths, K.; Halenbeck, R.; Moreland, M.
Synthesis of the antibiotic cortalcerone from D-glucose using pyranose 2-oxidase and a novel fungal enzyme, aldos-2-ulose dehydratase
Carbohydr. Res.
232
59-75
1992
Polyporus obtusus, Polyporus obtusus AU124PD
brenda
Claesson, M.; Lindqvist, Y.; Madrid, S.; Sandalova, T.; Fiskesund, R.; Yu, S.; Schneider, G.
Crystal structure of bifunctional aldos-2-ulose dehydratase/isomerase from Phanerochaete chrysosporium with the reaction intermediate ascopyrone M
J. Mol. Biol.
417
279-293
2012
Phanerodontia chrysosporium (P84193), Phanerodontia chrysosporium
brenda
EXTERNAL LINKS (specific for EC-Number 4.2.1.110)
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Release 2023.1 (January 2023)
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