Literature summary for 3.1.1.86 extracted from

Molgaard, A.; Kauppinen, S.; Larsen, S.
Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases (2000), Structure, 8, 373-383.

Crystallization (Commentary)

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

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/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Aspergillus aculeatus	Q00017	-	-

Substrates and Products (Substrate)

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

Synonyms	Comment	Organism
RGAE	-	Aspergillus aculeatus