Crystallization (Comment) | Organism |
---|---|
hanging-drop vapor diffusion, structure determination of the RGL4_K150A and RGL4_H210A enzyme variants. determination of the 2.4 A crystal structure of the RGL4 mutant RGL4_K150A with an rhamnogalacturonan I hexasaccharide. Crystals of the RGL4_K150A variant soaked with a rhamnogalacturonan digest gave a clear picture of substrate bound in the -3/+3 subsites | Aspergillus aculeatus |
Protein Variants | Comment | Organism |
---|---|---|
H210A | relative activity is 0.001% of wild-type activity | Aspergillus aculeatus |
K150A | relative activity is 0.04% of wild-type activity | Aspergillus aculeatus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
rhamnogalacturonan I | Km-value is 1.3 mg/ml or 0.27 mM cleavable bonds, pH 6.0, 30°C | Aspergillus aculeatus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
rhamnogalacturonan I | Aspergillus aculeatus | RGL4 is involved in the degradation of rhamnogalacturonan-I, an important pectic plant cell wall polysaccharide | rhamnogalacturonan I oligosaccharides with alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the nonreducing end | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus aculeatus | Q00019 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Aspergillus aculeatus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
rhamnogalacturonan I | RGL4 is involved in the degradation of rhamnogalacturonan-I, an important pectic plant cell wall polysaccharide | Aspergillus aculeatus | rhamnogalacturonan I oligosaccharides with alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the nonreducing end | - |
? | |
rhamnogalacturonan I | the actual size of the average oligosaccharide is a 25-mer to 30-mer (Mr= 4600 Da), indicating that some of the rhamnogalacturonan regions have a structure recalcitrant to degradation. Domain I of RGL4 contributes the catalytic and many substrate binding residues, but domain III contributes two conserved arginines also involved in substrate binding. Domain II mediates the correct respective positioning of domains I and III | Aspergillus aculeatus | rhamnogalacturonan I oligosaccharides with alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the nonreducing end | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RGL4 | - |
Aspergillus aculeatus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
rhamnogalacturonan I | kcat-value is 4.1/s, pH 6.0, 30°C | Aspergillus aculeatus |