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Information on EC 4.2.1.110 - aldos-2-ulose dehydratase and Organism(s) Phanerodontia chrysosporium and UniProt Accession P84193

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.110 aldos-2-ulose dehydratase
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 .
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Phanerodontia chrysosporium
UNIPROT: P84193
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The taxonomic range for the selected organisms is: Phanerodontia chrysosporium
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aldos-2-ulose dehydratase, pyranosone dehydratase, aldos-2-ulose dehydratase/isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aldos-2-ulose dehydratase
bifunctional enzyme
aldos-2-ulose dehydratase/isomerase
-
1,5-anhydro-D-fructose dehydratase (microthecin-forming)
-
-
pyranosone dehydratase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
show the reaction diagram
reaction scheme of the bifunctional enzyme, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
ascopyrone M (APM) to microthecin
dehydration
1,5-anhydro-D-fructose to ascopyrone M (APM)
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].
CAS REGISTRY NUMBER
COMMENTARY hide
101920-80-3
-
145266-93-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
show the reaction diagram
-
microthecin + H2O
-
?
1,5-D-anhydrofructose
microthecin
show the reaction diagram
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
-
-
?
glucosone
cortalcerone + H2O
show the reaction diagram
2-keto glucose
-
-
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
show the reaction diagram
glucosone
cortalcerone + H2O
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
glucosone
cortalcerone + H2O
show the reaction diagram
2-keto glucose
-
-
?
1,5-anhydro-D-fructose
2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
show the reaction diagram
-
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
i.e. microthecin
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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)
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.4
1,5-Anhydro-D-fructose
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
6.8
-
formation of microthecin
additional information
the reaction medium acidifies by itself due to unknown events related to the AUDH catalysed reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
at temperatures higher than 24°C there is increased degradation of microthecin
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2 - 5.3
recombinant enzyme, isoelectric focusing
5.46
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AUD_PHACH
900
0
98746
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
97400
-
x * 97400, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
?
-
x * 97400, SDS-PAGE
additional information
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).
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the best solvent for AUDH-catalysed microthecin reaction is de-ionized water
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Audh; ph.chr, expression in Hansenula polymorpha
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team