Cloned (Comment) | Organism |
---|---|
gene Audh; ph.chr, expression in Hansenula polymorpha | Phanerodontia chrysosporium |
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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Phanerodontia chrysosporium | P84193 | gene Audh; ph.chr | - |
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 | 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 | 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 | Comment | Organism |
---|---|---|
aldos-2-ulose dehydratase/isomerase | - |
Phanerodontia chrysosporium |
AUDH | - |
Phanerodontia chrysosporium |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Phanerodontia chrysosporium |
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 | 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 |