Crystallization (Comment) | Organism |
---|---|
crystals used for structure determination are grown in 1.4 M Li2SO4, 0.1 M Na acetate pH 5.0 with a protein concentration of 40 OD280. The crystals belong to the space group P212121 with a = 52.14 A, b = 56.87 A and c = 71.89 A and one molecule in the asymmetric unit.The structure of RGAE is determined at 1.55 A resolution. RGAE folds into an alpha/beta/alpha structure. The active site of RGAE is an open cleft containing a serine-histidine-aspartic acid catalytic triad. The position of the three residues relative to the central parallel beta sheet and the lack of the nucleophilic elbow motif found in structures possessing the alpha/beta hydrolase fold shows that RGAE does not belong to the alpha/beta hydrolase family | Aspergillus aculeatus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetylated rhamnogalacturonan I + H2O | Aspergillus aculeatus | the deacetylation of the backbone by rhamnogalacturonan acetylesterase is an essential prerequisite for the subsequent action of the enzymes that cleave the glycosidic bonds | acetate + deacetylated rhamnogalacturonan I | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus aculeatus | Q00017 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetylated rhamnogalacturonan I + H2O | the deacetylation of the backbone by rhamnogalacturonan acetylesterase is an essential prerequisite for the subsequent action of the enzymes that cleave the glycosidic bonds | Aspergillus aculeatus | acetate + deacetylated rhamnogalacturonan I | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RGAE | - |
Aspergillus aculeatus |