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Literature summary for 3.1.1.86 extracted from
- Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus. Synergism between rhamnogalacturonan degrading enzymes (1995), J. Biol. Chem., 270, 27172-17178.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpressed in Aspergillus oryzae | Aspergillus aculeatus |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 26350 | - |
x * 26350, calculated from sequence | Aspergillus aculeatus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetylated rhamnogalacturonan I + H2O | Aspergillus aculeatus | the enzyme acts in synergy with rhamnogalacturonase A as well as rhamnogalacturonase B from Aspergillus aculeatus in the degradation of apple pectin rhamnogalacturonan | acetate + deacetylated rhamnogalacturonan I | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus aculeatus | Q00017 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | the enzymes are heterogeneously glycosylated. The glycan moieties on native and recombinant enzyme are structurally different | Aspergillus aculeatus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Aspergillus aculeatus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1 | - |
pH 6.0, 30°C | Aspergillus aculeatus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acetylated rhamnogalacturonan I + H2O | the enzyme acts in synergy with rhamnogalacturonase A as well as rhamnogalacturonase B from Aspergillus aculeatus in the degradation of apple pectin rhamnogalacturonan | Aspergillus aculeatus | acetate + deacetylated rhamnogalacturonan I | - |
? | |
| acetylated rhamnogalacturonan I + H2O | the recombinant enzyme releases about 60% of the total amount of saponifiable acetyl esters | Aspergillus aculeatus | acetate + deacetylated rhamnogalacturonan I | - |
? | |
| additional information | native and recombinant enzyme do not release acetate from acetylated xylan or mannan | Aspergillus aculeatus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 26350, calculated from sequence | Aspergillus aculeatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RGAE | - |
Aspergillus aculeatus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Aspergillus aculeatus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 6 | upon prolonged incubation the recombinant enzyme hydrolyses acetyl groups from modified hairy regions from apples to the same extent at pH 3.5 as at pH 6.0 | Aspergillus aculeatus |
| 6 | - |
- |
Aspergillus aculeatus |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Aspergillus aculeatus | the expression of rhamnogalacturonan degrading enzymes by Aspergillus aculeatus is regulated at the level of transcription and is subjected to carbon catabolite repression by glucose | down |
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