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Literature summary for 3.2.1.173 extracted from
- Rhamnogalacturonan I modifying enzymes an update (2016), New Biotechnol., 33, 41-54 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| phylogenetic analysis | Aspergillus aculeatus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.085 | - |
rhamnogalacturonan I | pH 5.0, 40°C | Aspergillus aculeatus | |
| 0.23 | - |
MHR-S | pH 5.0, 40°C | Aspergillus aculeatus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| rhamnogalacturonan I + H2O | Aspergillus aculeatus | RGI, degrading enzymes are active on the RGI backbone of pectin and are thus strictly specific for cleaving bonds in the repetitive [(1->2)-alpha-L-Rhap-(1->4)-alpha-D-GalpA-(1->2)] structure | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus aculeatus | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| Exohydrolysis of the alpha-D-GalA-(1->2)-alpha-L-Rha bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing D-galacturonic acid from the non-reducing end of rhamnogalacturonan oligosaccharides | mode of action and site of action, overview. RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products | Aspergillus aculeatus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 16 | - |
substrate MHR-S, pH 5.0, 40°C | Aspergillus aculeatus |
| 21 | - |
substrate rhamnogalacturonan I, pH 5.0, 40°C | Aspergillus aculeatus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| MHR-S + H2O | i.e. saponified modified hairy regions of rhamnogalacturonan I, from apple pectin, residue remaining after enzymatic liquefaction of pectin | Aspergillus aculeatus | D-galactose + ? | - |
? | |
| additional information | RGI endo-hydrolases, RGHs, attack the RGI backbone randomly in an endo-fashion and catalyse bond cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap. The mechanism involves an inversion of the anomeric C1 configuration in galacturonic acid releasing oligosaccharides with beta-D-GalpA at the reducing end and L-Rhap at the non-reducing end as products. The RGGH type of exo-enzyme cleaves off the terminal nonreducing galacturonosyl residue by catalysing cleavage of alpha-(1->2) glycosidic bonds between D-GalpA and L-Rhap in the non-reducing terminus, releasing single beta-D-GalpA. The RGGH from Aspergillus aculeatus is active towards different types of rhamnogalacturonan I (RGI), for example, pectin or pure RGI, except for the ones with unsaturated GalpA at the nonreducing end. The enzyme displays preference for smaller RGI substrates since it has higher activities towards RGI fragment DP6 than saponified modified hairy regions of rhamnogalacturonan I (MHR-S). Aspergillus aculeatus RGGH shows no activity towards HG sub-strates, for example, polygalacturonic acid or small size GalpA acid oligomers | Aspergillus aculeatus | ? | - |
? | |
| rhamnogalacturonan I + H2O | RGI, degrading enzymes are active on the RGI backbone of pectin and are thus strictly specific for cleaving bonds in the repetitive [(1->2)-alpha-L-Rhap-(1->4)-alpha-D-GalpA-(1->2)] structure | Aspergillus aculeatus | ? | - |
? | |
| rhamnogalacturonan I + H2O | RGI DP 6 | Aspergillus aculeatus | D-galactose + ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 66000 | Aspergillus aculeatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| RGGH | - |
Aspergillus aculeatus |
| RGI exo-hydrolase | - |
Aspergillus aculeatus |
| RGI galacturonohydrolase | - |
Aspergillus aculeatus |
| RGI hydrolase | - |
Aspergillus aculeatus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Aspergillus aculeatus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
completely stable at for 3 h | Aspergillus aculeatus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4 | - |
- |
Aspergillus aculeatus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
stable up to, unstable above | Aspergillus aculeatus |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Aspergillus aculeatus | - |
- |
5.1 |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | phylogenetic and structural traits of RGI hydrolases, overview. The enzyme belongs to the glycosyl hydrolase family 28, GH28 | Aspergillus aculeatus |
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