Literature summary for 3.2.1.171 extracted from

Petersen, T.N.; Kauppinen, S.; Larsen, S.
The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed parallel beta helix (1997), Structure, 5, 533-544.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure solved by the single isomorphous replacement method including anomalous scattering to 2.0 A resolution. The enzyme folds into a large right-handed parallel beta helix, with a core composed of 13 turns of b strands. Four parallel beta sheets (PB1, PB1a, PB2 and PB3), formed by the consecutive turns, are typically separated by a residue in the conformation of a left-handed a helix	Aspergillus aculeatus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
rhamnogalacturonan I + H2O	Aspergillus aculeatus	RGase A is an enzyme implicated in the enzymatic degradation of rhamnogalacturonan I	rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end	-	?

Organism

Organism	UniProt	Comment	Textmining
Aspergillus aculeatus	Q00001	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	the enzyme is highly glycosylated: two N-linked and eighteen O-linked glycosylation sites in the structure. The glycan groups bound to RGase A are important to the stability of the crystal	Aspergillus aculeatus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
rhamnogalacturonan I + H2O	RGase A is an enzyme implicated in the enzymatic degradation of rhamnogalacturonan I	Aspergillus aculeatus	rhamnogalacturonan I oligosaccharides with D-galacturonic acid at the reducing end and L-rhamnopyranose at the nonreducing end	-	?

Synonyms

Synonyms	Comment	Organism
RGase A	-	Aspergillus aculeatus

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Release 2023.1 (January 2023)