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Literature summary for 4.2.1.110 extracted from

  • 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 (2012), J. Mol. Biol., 417, 279-293.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene Audh; ph.chr, expression in Hansenula polymorpha Phanerodontia chrysosporium

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ the enzyme contains a structural Mg2+ located in loop region, metal binding site and structure, overview Phanerodontia chrysosporium
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 Phanerodontia chrysosporium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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 Phanerodontia chrysosporium
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 Phanerodontia chrysosporium

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium P84193 gene Audh; ph.chr
-

Reaction

Reaction Comment Organism Reaction ID
1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O reaction scheme of the bifunctional enzyme, overview Phanerodontia chrysosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,5-D-anhydrofructose 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 Phanerodontia chrysosporium microthecin
-
?
additional information the enzyme is bifunctional and is also active with glucosone and xylosone, the former is converted to cortalcerone Phanerodontia chrysosporium ?
-
?

Subunits

Subunits Comment Organism
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 Phanerodontia chrysosporium
More secondary, quarternary, and overall structure analysis, detailed overview Phanerodontia chrysosporium

Synonyms

Synonyms Comment Organism
aldos-2-ulose dehydratase/isomerase
-
Phanerodontia chrysosporium
AUDH
-
Phanerodontia chrysosporium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Phanerodontia chrysosporium

pI Value

Organism Comment pI Value Maximum pI Value
Phanerodontia chrysosporium recombinant enzyme, isoelectric focusing 5.3 5.2
Phanerodontia chrysosporium sequence calculation
-
5.46

General Information

General Information Comment Organism
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 Phanerodontia chrysosporium
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 Phanerodontia chrysosporium