Cloned (Comment) | Organism |
---|---|
phylogenetic analysis | Aspergillus aculeatus |
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 | beta-L-rhamnose + ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus aculeatus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
Exohydrolysis of the alpha-L-Rha-(1->4)-alpha-D-GalA bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing beta-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides | mode of action and site of action, overview | Aspergillus aculeatus |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
12.9 | - |
substrate MHR-S, pH 5.0, 60°C | Aspergillus aculeatus |
57.6 | - |
substrate degalactosylated MHR-S, pH 5.0, 60°C | Aspergillus aculeatus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
degalactosylated MHR-S + H2O | degalactosylated saponified modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, galactosyl residues removed. The activity increases 78% when tested with MHR-S without galactose substitutions, and in essence the activity of this enzyme is thus hindered by galactose substitutions | Aspergillus aculeatus | beta-L-rhamnose + ? | - |
? | |
MHR + H2O | i.e. modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, the enzyme is active towards MHR-S as well as unsaponified MHR | Aspergillus aculeatus | beta-L-rhamnose + ? | - |
? | |
MHR-S + H2O | i.e. saponified modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, the enzyme is active towards MHR-S as well as unsaponified MHR | Aspergillus aculeatus | beta-L-rhamnose + ? | - |
? | |
additional information | RGRH exo-enzyme catalyses the cleavage of the alpha-(1->4) glycosidic bonds between L-Rhap and D-GalpA in the non-reducing terminus, releasing single beta-L-Rhap. Enzyme RGRH requires Rhap at the non-reducing end for action | 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 | beta-L-rhamnose + ? | - |
? | |
rhamnogalacturonan I + H2O | Aspergillus aculeatus RGRH is active on the nonreducing end Rhap-linkage in RGI fragments | Aspergillus aculeatus | L-rhamnose + ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 84000 | Aspergillus aculeatus |
Synonyms | Comment | Organism |
---|---|---|
RGI exo-hydrolase | - |
Aspergillus aculeatus |
RGI hydrolase | - |
Aspergillus aculeatus |
RGI rhamnohydrolase | - |
Aspergillus aculeatus |
RGRH | - |
Aspergillus aculeatus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
- |
Aspergillus aculeatus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
60 | - |
pH 5.0, 1 h, stable | Aspergillus aculeatus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
4 | - |
- |
Aspergillus aculeatus |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
3 | 5 | stable at, unstable below and above that range | Aspergillus aculeatus |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Aspergillus aculeatus | - |
5.4 | 4.9 |
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 |