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Literature summary 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)

EC Number Cloned (Comment) Organism
4.2.1.110 gene Audh; ph.chr, expression in Hansenula polymorpha Phanerodontia chrysosporium
5.3.2.7 expressed in Hansenula polymorpha Phanerodontia chrysosporium

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.2.7 hanging drop vapor diffusion method, using 0.1 M 4-morpholineethanesulfonic acid (pH 6.0), 0.2 M MgCl2 and 16% (w/v) polyethylene glycol 6000 Phanerodontia chrysosporium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.110 Mg2+ the enzyme contains a structural Mg2+ located in loop region, metal binding site and structure, overview Phanerodontia chrysosporium
4.2.1.110 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
5.3.2.7 Zn2+ contains zinc Phanerodontia chrysosporium

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.110 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
4.2.1.110 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
5.3.2.7 98700
-
 2 * 98700, SDS-PAGE Phanerodontia chrysosporium
5.3.2.7 98746
-
 2 * 98746, calculated from amino acid sequence Phanerodontia chrysosporium

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.2.7 ascopyrone M Phanerodontia chrysosporium
-
 microthecin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.110 Phanerodontia chrysosporium P84193 gene Audh; ph.chr
-
5.3.2.7 Phanerodontia chrysosporium P84193 cf. EC 4.2.1.110
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.2.7
-
 Phanerodontia chrysosporium

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.110 1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O reaction scheme of the bifunctional enzyme, overview Phanerodontia chrysosporium
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.110 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
-
 ?
4.2.1.110 additional information the enzyme is bifunctional and is also active with glucosone and xylosone, the former is converted to cortalcerone Phanerodontia chrysosporium ?
-
 ?
5.3.2.7 ascopyrone M
-
 Phanerodontia chrysosporium microthecin
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.110 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
4.2.1.110 More secondary, quarternary, and overall structure analysis, detailed overview Phanerodontia chrysosporium
5.3.2.7 homodimer 2 * 98700, SDS-PAGE Phanerodontia chrysosporium
5.3.2.7 homodimer 2 * 98746, calculated from amino acid sequence Phanerodontia chrysosporium

Synonyms

EC Number Synonyms Comment Organism
4.2.1.110 aldos-2-ulose dehydratase/isomerase
-
 Phanerodontia chrysosporium
4.2.1.110 AUDH
-
 Phanerodontia chrysosporium
5.3.2.7 AUDH bifunctional enzyme with EC 4.2.1.110 D-arabino-hex-2-ulose dehydratase and ascopyrone M isomerase activities Phanerodontia chrysosporium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.110 7.5
-
-
 Phanerodontia chrysosporium
5.3.2.7 7.5
-
 for microthecin formation Phanerodontia chrysosporium

pI Value

EC Number Organism Comment pI Value Maximum pI Value
4.2.1.110 Phanerodontia chrysosporium recombinant enzyme, isoelectric focusing 5.3 5.2
4.2.1.110 Phanerodontia chrysosporium sequence calculation
-
 5.46
5.3.2.7 Phanerodontia chrysosporium isoelectric focusing 5.3 5.2
5.3.2.7 Phanerodontia chrysosporium calculated from amino acid sequence
-
 5.5

General Information

EC Number General Information Comment Organism
4.2.1.110 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
4.2.1.110 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